Publications

PUBLICATION STATISTICS (11/17/16)

Web of Science
__________________________________________

H-INDEX: 36    
Total Cites: 4237  
Cites/Paper: 15.35

 

1.1 Papers which emerged from my PhD-thesis at the University of Bremen
 

  1. (1)R. Schweitzer-Stenner, W. Dreybrodt, A. Mayer and S. el Naggar.  Influence of the solvent environment on the polarization properties of resonance Raman scattering in hemoglobin. J . Raman  Spectrosc. 13, 139-148, 1982.

  2. (2)R. Schweitzer-Stenner, W. Dreybrodt and S el Naggar, Investigation of pH-induced Symmetry Distortions of the Prosthetic Group in Deoxyhemoglobin by Resonance Raman Scattering. Biophys. Struct. Mech. 10, 241-256, 1984. 

  3. (3)S. el Naggar, R. Schweitzer-Stenner, W. Dreybrodt and A. Mayer. Determination of the Raman Tensor of the Haem Group in Myoglobin by Resonance Raman Scattering in Solution and Single Crystals.  Biophys. Struct. Mech. 10., 257-273, 1984.




1.2. University Assistant at the University of Bremen (1983-1985; 1986-1990)


  1. (4)R. Schweitzer-Stenner, W. Dreybrodt, D. Wedekind and S. el Naggar. Investigation of pH-induced symmetry distortions of the prosthetic group in oxyhaemoglobin by resonance Raman scattering. Eur. Biophys. J. 11,61-76, 1984.

  2. (5)R. Schweitzer-Stenner and W. Dreybrodt. Excitation Profiles and Depolarization Ratios of Some Prominent Raman Lines in Oxyhemoglobin and Ferrocytochrome c in the Pre-Resonant and Resonant Region of the Q-band. J. Raman Spectrosc.  16, 111-123, 1985

  3. (6)S. el Naggar, W. Dreybrodt and R. Schweitzer-Stenner.  Haem-apoprotein interactions detected by resonance Raman scattering in Mb- and Hb-derivatives lacking the saltbridge His 146b-Asp 94b. Eur. Biophys. J.  12, 43-49, 1985.

  4. (7)D. Wedekind, R. Schweitzer-Stenner and W. Dreybrodt. Heme-apoprotein interaction in the modified oxyhemoglobin-bis-(N-maleimidomethyl)ether and in oxyhemoglobin at high Cl-concentration detected by resonance Raman scattering.  Biochim. Biophys. Acta.  830, 224-232, 1985.

  5. (8)D. Wedekind, U. Brunzel, R. Schweitzer-Stenner and W. Dreybrodt. Correlation of pH-dependent Resonance Raman and Optical Absorption Data Reflecting Haem-Apoprotein Interaction in Oxyhaemoglobin. J. Mol. Struc. 143, 457-460, 1986.

  6. (9)R. Schweitzer-Stenner, W. Dreybrodt, D. Wedekind and U. Kubitscheck. The Analyzation of the Depolarization Ratio Dispersion of Resonant Raman Lines in Hemeproteins. A Suitable Tool to  Detect Heme-Apoprotein Interactions. J. Mol. Struc. 143, 453-457, 1986.

  7. (10) Kubitscheck, W. Dreybrodt and R. Schweitzer-Stenner. Detection of heme distortions in ferri- and ferrocytochrome c by resonance Raman scattering. Spectrosc. Lett. 19, 681-689, 1986.  

  8. (11) U. Brunzel, W. Dreybrodt and R. Schweitzer-Stenner.  pH-dependent absorption in the B- and Q-bands of oxyhemoglobin and chemically modified oxyhemoglobin (BME) at low Cl--concentrations. Biophys. J.  49, 1069-1076, 1986.

  9. (12) R. Schweitzer-Stenner,  D. Wedekind and W. Dreybrodt. Correspondence of the pK-values of oxyHb-titration states detected by resonance Raman scattering to kinetic data of ligand dissociation  and association. Biophys. J. 49, 1077-1088, 1986.  

  10. (13) U. Bobinger, R. Schweitzer-Stenner and W. Dreybrodt. Highly resolved depolarization dispersion and excitation profiles of Raman fundamentals of protoporphyrin IX in a cytochrome c matrix.  J. Raman Spectrosc.  20, 191-202, 1989

  11. (14) R. Schweitzer-Stenner and W. Dreybrodt.  An extended MWC-model expressed in terms of the Herzfeld-Stanley  formalism applied to oxygen and carbonmonoxide binding curves of hemoglobin trout IV.  Biophys. J.  55,691-701,1989.

  12. (15) R. Schweitzer-Stenner,  D. Wedekind and W. Dreybrodt. Detection of heme perturbations caused by the quaternary R->T transition in oxyhemoglobin trout IV by resonance Raman scattering. Biophys. J. 55, 703-712, 1989.

  13. (16) R. Schweitzer-Stenner, D. Wedekind and W. Dreybrodt. The influence of structural variations in the F- and FG-helix of the β-subunit modified oxyHb-NES on the heme structure detected by resonance Raman scattering. Eur. Biophys. J.  17, 87-100, 1989.

  14. (17) E. Ortega, R. Schweitzer-Stenner  and I. Pecht. Receptor-Effector Coupling Processes Probed by Monoclonal Antibodies. In: Computer Assisted Modeling of Receptor-Ligand Interaction. Theoretical Aspects  and Applications to Drug Design. Edited by A. Golombeck and R. Rein, New York, 317-326, 1988.

  15. (18) E. Ortega, R. Schweitzer-Stenner and I. Pecht. Possible configurational constraints determine secretory signals induced by aggregation of IgE receptors on mast cells. EMBO J. 7, 4101-4109, 1988.

  16. (19) E. Ortega, R. Schweitzer-Stenner, and I. Pecht. Receptor-effector coupling processes probed by monoclonal antibodies. Prog. Clin. Biol. Res. 289, 317-326, 1989.

  17. (20) I. Pecht, R. Schweitzer-Stenner and E. Ortega. Is there specificity in Fcε-receptor aggregation which leads to an effective secretory stimulus?  Prog. Immunol. 7, 676-682, 1989.

 

 


1.3. Visiting Research Scientist at the Weizmann Institute of Science, (1985-1986).


  1. (21) A.Corcia, R. Schweitzer-Stenner , I. Pecht and B. Rivnay. Characterization of the ion channel activity in planar bilayers containing IgE-Fce receptor and cromolyn binding protein.  EMBO J. 5, 849-854, 1986.

  2. (22) I. Pecht, R. Schweitzer-Stenner, R. Gertler, M. Wolf, Y. Zisman and B. Reck. Immunological stimulation of mast cells degranulation: role of cytosolic pH, Na+ and Ca2+ ions NATO ASI Series: Life Sciences, 133, 73-86.  

  3. (23) R. Schweitzer-Stenner, A. Licht, I. Luescher and I. Pecht. Oligomerization and Ring Closure of Immunglobulin E Class Antibody by Divalent Haptens.  Biochemistry 26, 3602-3612, 1987.



 

1.4 Senior University Assistant at the University of Bremen, (1990-1994).


  1. (24) R. Schweitzer-Stenner, U. Bobinger and W. Dreybrodt.  Multimode analysis of depolarization ratio dispersion and excitation profiles of seven Raman fundamentals from the heme group in ferrocytochrome c. J. Raman Spectrosc.  22, 65-78, 1991.

  2. (25) U. Bobinger, R. Schweitzer-Stenner and W. Dreybrodt. Investigation of asymmetric perturbations of Ni(II)-octaethylporphyrin in CH2Cl2 by Raman Dispersion Spectroscopy. J. Phys. Chem.  95, 7625-7635, 1991.

  3. (26) E. Ortega, R. Schweitzer-Stenner and I. Pecht. Kinetics of ligand binding to the type I Fce receptor on mast cells. Biochemistry 30, 3473-3483, 1991.

  4. (27) U. Kubitscheck, M. Kircheis, R. Schweitzer-Stenner, W. Dreybrodt, T.M. Jovin and I. Pecht.  Fluorescence Resonance Energy Transfer on Single Living Cells: Application to Binding of Monovalent Haptens to Cell-Bound Immunoglobulin E. Biophys. J. 60, 307-318, 1991.  

  5. (28) I. Pecht, E. Ortega and R. Schweitzer-Stenner. Membrane receptor clustering as a cellular stimulus - the mast cell case. In: Biological Signal Transduction.  Edited by E.M Ross and K.W.A. Wirtz, NATO ASI Series Vol. H52,  Springer Verlag, Berlin and Heidelberg, 147-161, 1991.

  6. (29) R. Schweitzer-Stenner,  A. Licht and I. Pecht. Dimerization kinetics of the IgE-class antibodies by divalent haptens. I. The Fab-hapten interactions. Biophys. J. 63, 551-562, 1992.  

  7. (30) R. Schweitzer-Stenner, A. Licht and I. Pecht. Dimerization kinetics of the IgE-class antibodies by divalent haptens. II. The interactions between intact IgE and haptens. Biophys. J. 63, 563-568, 1992.

  8. (31) R. Schweitzer-Stenner, U. Dannemann and W. Dreybrodt. Investigation of heme distortions and heme-protein coupling in isolated subunits of oxygenated hemoglobin by resonance Raman dispersion spectroscopy.  Biochemistry  31, 694-702, 1992.  

  9. (32) M. Bosenbeck, R. Schweitzer-Stenner  and W. Dreybrodt. pH-induced conformational changes of the Fe2+-His F8 linkage in deoxyhemoglobin trout IV detected by the Raman active Fe2+-Ne (His F8) stretching mode. Biophys. J 61, 31-41, 1992.  

  10. (33) R. Schweitzer-Stenner  and W. Dreybrodt. Investigation of Haem-Protein Coupling and Structural Heterogenity in Myoglobin and Haemoglobin by Resonance Raman Spectroscopy. J. Raman Spectrosc. 23, 539-550, 1992.  

  11. (34) R. Schweitzer-Stenner,  M. Bosenbeck and W. Dreybrodt. Raman dispersion spectroscopy probes heme distortions in deoxy-Hb trout IV involved in its T-state Bohr-effect.  Biophys. J. 64, 1194-1209, 1993.

  12. (35) A. Stichternath, R. Schweitzer-Stenner,  W. Dreybrodt, R.S. W. Mak, X.-y. Li, L. D. Sparks, J. A. Shelnutt, C.J. Medforth and K.M. Smith. Macrocycle and Substituent Vibrational Modes of Nonplanar Ni(II)-Octaethyltetraphenylporphyrin from its Resonance Raman, Near-Infrared-Excited FT-Raman, FT-IR Spectra and Deuterium Isotope Shifts.  J. Phys. Chem. 97, 3701-3708, 1993.

  13. (36) E. Unger, U. Bobinger, W. Dreybrodt and R. Schweitzer-Stenner.  Vibronic coupling in Ni(II)-porphine derived from resonant excitation profiles. J. Phys. Chem.  97, 9956-9968, 1993.  

  14. (37) H. Gilch, R. Schweitzer-Stenner and W. Dreybrodt. Structural Heterogeneity of the Fe2+-Nε(HisF8) Bond in Various Hemoglobin and Myoglobin Derivatives Probed by the Raman active Iron Histidine Stretching Mode.  Biophys. J. 65, 1470-1485, 1993.  

  15. (38) U. Kubitscheck, R. Schweitzer-Stenner,  D.J. Arndt-Jovin, T.M. Jovin and I. Pecht. Distribution of Type I Fcε-Receptors on the Surface of Mast Cells Probed by Fluorescence Energy Transfer. Biophys. J.  64, 110-120, 1993.  

  16. (39) R. Schweitzer-Stenner, E. Ortega and I. Pecht. Kinetics of FcεRI Dimer Formation by Specific Monoclonal Antibodies on Mast Cells. Biochemistry  33, 8813-8825,  1994.  

  17. (40) R. Schweitzer-Stenner. Revisited Depolarization Ratio Dispersion of Raman Fundamentals from Heme c in Ferrocytochrome c Confirms That Asymmetric Perturbations Affect the Electronic and Vibrational Structure of the Chromophore's Macrocycle. J. Phys. Chem. 98, 9374-9379, 1994.

 



1.5. Research Scientist at the University of Michigan (1993-1994).


  1. (41) X.G. Chen, R. Schweitzer-Stenner, S. Krimm, N.G. Mirkin and S.A. Asher. N-Methylacetamide and Its Hydrogen-Bonded Water Molecules Are Vibrationally Coupled. J. Am. Chem. Soc. 116, 11141-11142, 1994.

  2. (42) X.G. Chen, S.A. Asher, R. Schweitzer-Stenner,  N.G. Mirkin, and S. Krimm. UV Raman Determination of the pi* Excited State Geometry of N-methylacetamide: Vibrational Enhancement Pattern. J. Am. Chem. Soc. 117, 2884-2895, 1995.  

  3. (43) X.G. Chen, R. Schweitzer-Stenner, S.A. Asher, N.G. Mirkin and S. Krimm. Vibrational Assignments of trans N-methylacetamide and Some of its Deuterated Isotopomers from Band Decomposition of IR, Visible and Resonance Raman Spectra. J. Phys. Chem. 99, 3074-3083, 1995. 

 



1.6. University Lecturer at the University of Bremen (1995-1996).


  1. (44) R. Schweitzer-Stenner, E. Unger, G. Karvounis and W. Dreybrodt. Spectral Analyses Is Suitable to Decompose Overcrowded Resonance Raman Spectra of Metallporphyrins and Yields Reliable Depolarization Ratios. J. Phys. Chem. 99, 7195-7196, 1995.  

  2. (45) H. Gilch, W. Dreybrodt, and R. Schweitzer-Stenner. Thermal fluctuations between conformational substates of the Fe2+-His F8 linkage in deoxymyoglobin probed by the Raman active Fe-Ne(His F8) stretching vibration. Biophys. J., 69, 214, 1995.

  3. (46) H. Gilch, R. Schweitzer-Stenner, W. Dreybrodt, M. Leone, A. Cupane and L. Cordone. Conformational substates of the Fe2+- His F8 linkage in deoxymyoglobin and hemoglobin probed in parallel by the Raman band of the Fe-His stretching vibration and the near infrared absorption band III. Int. J. Quant.Chem. 59, 301-313, 1996.

  4. (47) W. Jentzen, E. Unger, G Karvounis, J.A. Shelnutt, W. Dreybrodt, and R. Schweitzer-Stenner. Conformational Properties of Nickel(II) Octaethyl-porphyrin in Solution. I. Resonance Excitation Profiles and Temperature Dependence of Structure Sensitive Raman Lines. J. Phys. Chem., 100, 14184-14191, 1996.  

  5. (48) A. Cupane, M. Leone, L. Cordone, H. Gilch, W. Dreybrodt, E. Unger and R. Schweitzer-Stenner. Conformational Properties of Nickel(II)-Octaethylporphyrin in Solution. II. A Low Temperature Optical Absorption Spectroscopy Study. J. Phys. Chem., 100, 14192-14199, 1996.

  6. (49) I. Tamir, R. Schweitzer-Stenner and I. Pecht. Immobilization of the type I receptor for IgE initiates signal transduction in mast cells. Biochemistry, 35, 6872-6883, 1996.  

 



1.7. Distinguished Professor at the University of Bremen (1996-1999).


  1. (50) R. Schweitzer-Stenner, A. Stichternath, W. Dreybrodt, W. Jentzen, X.-Z. Song, J.A. Shelnutt, O.F. Nielsen, C.J. Medforth and K.M. Smith.  Raman Dispersion Spectroscopy on the Highly Saddled Nickel(II)-Octaethyltetraphenylporphyrin Reveals the Symmetry of Non-Planar Distortions and the Vibronic Coupling Strength of Normal Modes.  J. Chem. Phys. 107,1794-1815, 1997.  

  2. (51) E. Unger, W. Dreybrodt, and R. Schweitzer-Stenner. Conformational Properties of Nickel(II)-meso-Tetraphenylporphyrin in Solution. Raman Dispersion Spectroscopy Reveals the Symmetry of Distortions for a Nonplanar Conformer. J. Phys. Chem. A, 101, 5997-6007, 1997.  

  3. (52) W. Jentzen, E. Unger, X-Z. Song, I. Turowska-Tyrk, R. Schweitzer-Stenner, W. Dreybrodt, R.W. Scheidt, and J.A. Shelnutt. Planar and Nonplanar Conformations of (Meso-Tetraphenyl-porphinato)nickel(II) in Solution as Inferred from Solution and Solid-State Raman Spectroscopy.  J. Phys. Chem. A, 101, 5789-5798, 1997.  

  4. (53) G. Sieler and R. Schweitzer-Stenner. The Amide I Mode of Peptides in Aqueous Solution Involves Vibrational Coupling Between The Peptide Group and Water Molecules of The Hydration Shell. J. Am. Chem. Soc. 119, 1720-1726, 1997.  

  5. (54) S. A. Asher, P. Li, Z. Chi, X.G. Chen, R. Schweitzer-Stenner, N.G. Mirkin, and S. Krimm. Reply to:”Comment on ‘Vibrational Assignments of trans-N-Methylacetamide and Some of Its Deuterated Isotopomers from Band Decomposition of IR, Visible, and Resonance Raman Spectra’. J. Phys. Chem. A  101, 3992-3994, 1997.  

  6. (55) R. Schweitzer-Stenner,  I. Tamir and I. Pecht. Analysis of FcεRI-Mediated Mast Cell Stimulation by Surface-Carried Antigens. Biophys. J., 72, 2470-2478, 1997.  

  7. (56) U. Lippert, M. Artuc, A. Grützkau, A. Möller, A Kenderessy-Szabo, D. Schadendorf, J. Norgauer, K. Hartmann, R. Schweitzer-Stenner, B.M. Henz, and S. Krüger-Krtasagakes.  Expression and Functional Activity of the IL-8 Receptor Type CXCR1 and CXCR2 on Human Mast Cells. J. Immunol. 161, 2600-2608, 1998.  

  8. (57) R. Schweitzer-Stenner, G. Sieler, N.G. Mirkin and S. Krimm.  Intermolecular Coupling in Liquid and Crystalline States of trans N-Methylacetamide Investigated by Polarized Raman and FT-IR  Spectroscopies.  J. Phys. Chem. A. 102, 118-127, 1998.  

  9. (58) A. Cupane, M. Leone, E. Unger, C. Lemke, M. Beck, W. Dreybrodt, and R. Schweitzer-Stenner.  Dynamics of various metal-octaethylporphyrins in solution studied through resoance Raman and low-temperature optical absorption spectroscopies.  Role of the central metal. J. Phys. Chem. B, 102, 6612-6620,1998.  

  10. (59) C. Lemke, W. Dreybrodt, J.A. Shelnutt, J.M.E. Quirke and R. Schweitzer-Stenner. Polarized Raman Dispersion Spectroscopy probes planar and non-planar distortions ofNi(II)-porphyrins with different peripheral substituents. J. Raman Spectrosc., 29, 945-953, 1998 (Invited paper, guest editor: W. Kiefer, special issue on Resonance Raman Spectroscopy).  

  11. (60) R. Schweitzer-Stenner, G. Sieler H. Christiansen. Competition between peptide-peptide and peptide-solvent hydrrogen bonding probed by polarized Raman spectroscopy on N’-methylacetamide. Asian J. Phys. 7, 287-312, 1998 (Invited paper, guest editor: W. Kiefer, special issue on the 70th anniversary of the discovery of the Raman effect).  

  12. (61) E. Unger, R.J. Lipski, W. Dreybrodt and R. Schweitzer-Stenner. A New Method for the Evaluation of Normal Modes and Molecular Mechanics with Reduced Sets of Force Constants. 1. Principle and Reliability Test. J. Raman Spectrosc. 30, 3-28, 1999.

  13. (62) G. Sieler, R. Schweitzer-Stenner, J.S.W. Holtz, V. Pajcini and S.A. Asher.  Different Conformers and Protonation States of Dipeptides Probed by Polarized Raman, UV-resonance Raman and FTIR-spectroscopy.  J. Phys. Chem. B. 103, 372-384, 1999.  

  14. (63) R.J. Lipski, E. Unger, and R. Schweitzer-Stenner. Polarized Resonance Raman Spectroscopy Reveals Two Different Conformers of Metallo(II)octamethylchlorins in CS2. J. Phys. Chem. B., 103, 9777-9781, 1999.

  15. (64) E. Unger, M. Beck, R.J. Lipski, W. Dreybrodt, C.J. Medforth, K.M. Smith, and R. Schweitzer-Stenner.  A New Method for Evaluating the Conformations and Normal Modes of Macromolecule Vibrations.  2. Application to nonplanarily distorted metal porphyrins.  J. Phys. Chem. B., 103, 10022-10031, 1999.  

  16. (65) R. Schweitzer-Stenner, Michael Engelke, Arieh Licht and Israel Pecht.  Mast cell stimulation by co-clustering the type I Fcε-receptors with mast cell function-associated antigens. Immunol. Lett. 68, 71-78, 1999.

  17. (66) N. Engler, A. Ostermann, A. Grassmann, D.C. Lamb, V.E. Prusakov, J. Schott, R. Schweitzer-Stenner, and F.G. Parak.  Protein dynamics in an intermediate state of myoglobin: Investigations by optical absorption spectroscopy, resonance Raman spectroscopy and X-ray structure analysis. Biophys. J., 78, 2081-2092, 2000.



 

1.8. Papers submitted after assuming an Associated Professorship at the University of Puerto Rico (1999-2003).


  1. (67) R. Schweitzer-Stenner, A. Cupane, M. Leone, C. Lemke, J. Schott, and W. Dreybrodt. Anharmonic protein motions and heme deformations in myoglobin cyanide probed by absorption and resonance Raman spectroscopy. J. Phys. Chem. B. 19, 4754-4764, 2000.

  2. (68) G. Mix, R. Schweitzer-Stenner, and S.A. Asher.  Uncoupled Adjacent Amide Vibrations in Small Peptides. J. Am. Chem. Soc. 122, 9028-9029, 2000. 

  3. (69) R.J. Lipski, E. Unger, W. Dreybrodt, V. Militello, M. Leone, and R. Schweitzer-Stenner. Vibrational Analysis of Ni(II)- and Cu(II)-Octamethylchlorin by Polarized Resonance Raman and FTIR Spectroscopy.  J. Raman Spectrosc. 32, 521-542, 2001 (Invited paper, guest editor: H. Schrötter, special issue dedicated to celebrate the 90th birthday of Prof. Shorygin).

  4. (70) C. Lemke, R. Schweitzer-Stenner, J.A. Shelnutt, and J.M. Quirke. Vibrational Analysis if Metalloporphyrins with Electron Withdrawing NO2 – Substitutents at Different meso Positions. J. Phys. Chem. A, 105, 6668-6679, 2001.

  5. (71) R. Schweitzer-Stenner, C. Lemke, R. Haddad, Y. Qiu, J.A. Shelnutt, J.M. Quirke, and W. Dreybrodt. Conformational Distortions of Metalloporphyrins With Electron Withdrawing NO2 Substituents at Different meso Positions. A Structural Analysis By Polarized Resonance Raman Dispersion Spectroscopy and Molecular Mechanics Calculations.  J. Phys. Chem. A., 105, 6680-6694, 2001.

  6. (72) M. Heid, S. Schlücker, U. Schmitt, T. Chen, R. Schweitzer-Stenner, V. Engel and W. Kiefer. Two-dimensional probing of ground state vibrational dynamics in porphyrin molecules by fs-CARS. J. Raman Spectrosc. 32, 771-784, 2001.

  7. (73) J. Schott, W. Dreybrodt, and R. Schweitzer-Stenner. The Fe2+-HisF8 Raman Band Shape of Deoxymyoglobin Reveals Taxonomic Conformational Substates of the Proximal Linkage.  Biophys. J., 81,1624-1631, 2001.

  8. (74) R. Schweitzer-Stenner and D. Bigman. Electronic and Vibronic Contributions to The Band Splitting in Optical Spectra of Heme Proteins. J. Phys. Chem. B. 105, 7064-7073, 2001.

  9. (75) R. Schweitzer-Stenner, F. Eker, Q. Huang, and K. Griebenow. The Dihedral Angles of Tri-Alanine in D2O Determined by Combining FTIR- and Polarized Visible Raman Spectroscopy. J. Am. Chem. Soc., 123, 9628-9633, 2001.

  10. (76) S.A. Asher, A. Ianoul, G. Mix, M.N. Boden, A. Karnoup, M. Diem, and R. Schweitzer-Stenner.  Dihedral y Angle Dependence of the Amide III Vibration: A Uniquely Sensitive UV Resonance Raman Secondary Structural Probe. J. Am. Chem. Soc., 123, 9628-9633, 2001.

  11. (77) R. Schweitzer-Stenner. Dihedral angles of Tripeptides in Solution Determined by Polarized Raman and FTIR Spectroscopy. Biophys. J. 83, 523-532, 2002.  

  12. (78) R. Schweitzer-Stenner, F. Eker, Q. Huang, K. Griebenow, P. Mrosz, and P.M. Kozlowski. Structure Analysis of Dipeptides in Water By Exploring and Utilizing the Structural Sensitivity of Amide III by Polarized Visible Raman, FTIR-Spectroscopy and DFT based normal coordinate analysis.  J. Phys. Chem. B. 106,4294-4304, 2002.  

  13. (79) W. Al-Azzam, E.A. Pastrana, Y.Ferrer, Q.Huang, R.Schweitzer-Stenner, and Kai Griebenow. Structure of PEG-modified HRP in organic solvents.  IR amide I spectral changes upon protein dehydration are largely due to protein structural changes and not to water removal per se. Biophys. J., 83, 363-3651, 2002.  

  14. (80) F. Eker, X. Cao, L. Nafie, and R. Schweitzer-Stenner. Tripeptides Adopt Stable Structures in Water. A Combined Polarized Visible Raman, FTIR and VCD Spectroscopy Study. J. Am. Chem. Soc. 124, 14330-14341, 2002.

  15. (81) F. Eker, X. Cao, L. Nafie, and R. Schweitzer-Stenner. The Structure of Alanine Based Tripeptides in Water and Dimethylsulfoxide Probed by Vibrational Spectroscopy. J. Phys. Chem. B., 107, 358-365, 2003. .

  16. (82) M. Laberge, Q. Huang, R. Schweitzer-Stenner, and J. Fidy. The Endogenous Calcium Ions of Horseradish Peroxidase C are Required to Maintain the Functional Nonplanarity of the Heme. Biophys. J., 84, 2542-2552, 2003.

  17. (83) Q. Huang, W. Al-Azzam, K. Griebenow, and Reinhard Schweitzer-Stenner. Heme Structural Perturbation of PEG-Modified Horseradish Peroxidase C in Aromatic Organic Solvents Probed by Optical Absorption and Resonance Raman Dispersion Spectroscopy.  Biophys. J., 84, 3285-3298, 2003. 

  18. (84) Q. Huang, K. Szigeti, J. Fidy and R. Schweitzer-Stenner. Structural Disorder of Native Horseradish Peroxidase C probed by Resonance Raman and Low Temperature Optical Absorption spectroscopy. J. Phys. Chem. B, 107, 2822-2830, 2003.

  19. (85) Q. Huang, M. Laberge, K. Szigeti, J. Fidy, and R. Schweitzer-Stenner. Change of The Iron Spin State in Horseradish Peroxidase C Induced By the Removal of Ca2+ probed by Resonance Raman Spectroscopy. Biopolymers (Biospectroscopy), 72, 241-248, 2003.  

  20. (86) F. Eker, K. Griebenow, and R. Schweitzer-Stenner. Stable Conformations of Tripeptides in Aqueous Solution Studied by UV Circular Dichroism Spectroscopy. J. Am. Chem. Soc. 125, 8178-8185, 2003. 

  21. (87) W. Dreybrodt, J. Schott, and R. Schweitzer-Stenner. Comments to the paper "Temperature dependence of the iron-histidine Resonance Raman Band of deoxyheme proteins: Anharmonic coupling versus distribution over taxonomic conformational substates“ by Korostishevsky et al. Biophys. J., 86, 660-661, 2004.




1.9. Papers submitted after assuming an Associate Professorship at Drexel University (2003-2009).


  1. (88) R. Schweitzer-Stenner, F. Eker, A. Perez, K. Griebenow, X. Cao, and L. Nafie. The Structure of Tri-Proline in Water Probed by Polarized Raman, FTIR, VCD and ECD Spectroscopy. Biopolymers (Peptide Science), 71, 558-568, 2003.

  2. (89) R. Schweitzer-Stenner, F. Eker, K. Griebenow, X. Cao, and L. Nafie. The Conformation of Tetraalanine in Water Determined by Polarized Raman, FTIR and VCD ". J. Am. Chem. Soc. 126, 2768-2776, 2004.

  3. (90) F. Eker, K. Griebenow, X. Cao, L. Nafie, and R. Schweitzer-Stenner. Tripeptides with Ionizable Side-Chains Adopt a Perturbed Polyproline II Structure in Water. Biochemistry, 43, 613-621, 2004.

  4. (91) Q. Huang and R. Schweitzer-Stenner. Conformational analysis of tetrapeptides by exploiting the excitonic coupling between amide I modes. J. Raman Spectros. 35, 586, 2004.  

  5. (92) F. Eker , K. Griebenow, X. Cao, L.A. Nafie and R. Schweitzer-Stenner. Preferred peptide backbone conformations in the unfolded state revealed by the structure analysis of alanine-based (AXA) tripeptides in aqueous solution. Proc. Natl. Acad. Sci. USA 101 (27), 11054, 2004.

  6. (93) R. Schweitzer-Stenner. Secondary Structure Analysis of Polypeptides Based on an Excitonic Coupling Model to Describe the Band Profile of Amide I’ of IR, Raman and Vibrational Circular Dichroism Spectra. J. Phys. Chem B. 108, 16965, 2004.

  7. (94) F. Eker , K. Griebenow and R. Schweitzer-Stenner. AB1-28 Fragment of the Amyloid Peptide Predominantly Adopts a Polyproline II Conformation in Acidic Solution. Biochemistry, 43, 6893-6898, 2004.

  8. (95) Q. Huang, Q. Huang, R. Pinto, K. Griebenow, R. Schweitzer-Stenner, and W.J. Weber. Inactivation of Horseradish Peroxidase by Phenoxyl Radical Attack. J. Am. Chem. Soc., 127, 1431-1437, 2005. 

  9. (96) Q. Huang and R. Schweitzer-Stenner. Nonplanar Heme Deformations and Excited State Displacements in Horseradish Peroxidase Detected by Raman Spectroscopy at Soret Excitation. J. Raman Spectrosc. (special issue on ‘Structure and Dynamics of Biomolecules) 36 (4), 363-375, 2005.

  10. (97) R. Schweitzer-Stenner. Structure and Dynamics of Biomolecules probed by Raman Spectroscopy. J. Raman Spectrosc. 36 (4), 276-275, 2005.

  11. (98) R. Schweitzer-Stenner and I. Pecht. Death of a Dogma or Enforcing the Artificial? Monomeric IgE binding may initiate mast cells response by inducing its receptor aggregation. J. Immunol. (cutting edge article), 174, 4461-4464, 2005.

  12. (99) A. Licht, I. Pecht and R. Schweitzer-Stenner. Regulation of mast cells’ secretory response by co-clustering the Type 1 Fcε receptor with the mast cell function-associated antigen. Eur. J. Immunol., 35 (5), 1621-1633, 2005.

  13. (100) T. Measey, A. Hagarman, F. Eker, K. Griebenow and R. Schweitzer-Stenner. Side chain dependence of intensity and wavenumber position of amide I’ in IR and visible Raman spectra of XA and AX dipeptides. J. Phys. Chem. B. 109, 8195-8205, 2005.

  14. (101) T. Measey and R. Schweitzer-Stenner. Simulation of amide I band profiles of trans-polyproline based on an excitonic coupling model. Chem. Phys. Letts. 408, 123-127, 2005.

  15. (102) M. Levantino, Q. Huang, A. Cupane, M. Laberge, A. Hagarman and R. Schweitzer-Stenner. The importance of vibronic perturbations in ferrocytochrome c spectra: A reevaluation of spectral properties based on low-temperature optical absorption, resonance Raman, and molecular-dynamics simulations. J. Chem. Phys. 123, 054508, 2005.

  16. (103) Q. Huang, C. J. Medforth, and R. Schweitzer-Stenner*. Nonplanar Heme deformations and Excited State Displacements in Nickel Porphyrins Detected by Raman Spectroscopy at Soret Excitation. J. Phys. Chem. A. 109, 14093-10502, 2005.

  17. (104) T. Measey, and R. Schweitzer-Stenner. The Conformations Adopted by The Octamer Peptide (AAKA)2 in Aqueous Solution Probed By FTIR and Polarized Raman Spectroscopy. J. Raman Spectrosc. (invited article for a special issue celebrating the 65th birthday of Prof. Wolfgang Kiefer), 37, 248-254, 2006.

  18. (105) A. Hagarman, T. Measey, R. Doddasomayajula, I. Dragomir, F. Eker, K. Griebenow, and R. Schweitzer-Stenner.  Conformational Analysis of XA and AX Dipeptides in Water by Electronic Circular Dichroism and 1H NMR Spectroscopy.  J. Phys. Chem.  B.  (2006) 110, 6979-6986.

  19. (106) R. Schweitzer-Stenner, T. Measey, A. Hagarman, F. Eker, and K. Griebenow.  Salmon Calcitonin and Amyloid b:  Two Peptides with Amyloidogenic Capacity Adopt Different Conformational Manifolds in Their Unfolded States.  Biochemistry. (2006) 45, 2810-2819. 

  20. (107) I.C. Dragomir, T.J. Measey, A.M. Hagarman, and R. Schweitzer-Stenner.  Environment-Controlled Interchromophore Charge Transfer Transitions in Dipeptides Probed by UV Absorption and Electronic Circular Dichroism Spectroscopy.  J. Phys. Chem. B.  (2006) 110, 13235-13241.

  21. (108) T. J. Measey, and R. Schweitzer-Stenner.  Aggregation of the Amphipathic Peptides (AAKA)n into Antiparellel β-Sheets.  J. Am. Chem. Soc.  (2006) 128, 13324-13325.

  22. (109) R. Schweitzer-Stenner, M. Levantino, A. Cupane, C. Wallace, M. Laberge, and Q. Huang.  Functionally Relevant Electric Field Induced Perturbations of the Prosthetic Group of Yeast Ferrocytochrome c Mutants Obtained From a Vibronic Analysis of Low Temperature Absorption Spectra.  (2006) J. Phys. Chem. B. 110, 12155-12161.

  23. (110)R. Schweitzer-Stenner, T. Measey, L. Kakalis, F. Jordan, S. Pizzanelli, C. Forte, and K. Griebenow.  Conformations of Alanine-Based Peptides in Water Probed by FTIR, Raman, Vibrational Circular Dichroism, Electronic Circular Dichroism, and NMR Spectroscopy.  Biochemistry (2007)  46 (6), 1587-1596.

  24. (111) I. Dragomir, A. Hagarman, C. Wallace, and R. Schweitzer-Stenner.  Optical Band Splitting and Electronic Perturbations of the Heme Chromophore in Cytochrome c at Room Temperature Probed by Visible Electronic Circular Dichroism Spectroscopy.  (2007)  Biophys. J. 92, 989-998.  

  25. (112) R. Schweitzer-Stenner and T. Measey.  The Alanine-Rich XAO Peptide Adopts a Heterogeneous Population, Including Turn-Like and PPII Conformations. (2007)  Proc. Natl. Acad. Sci. 104, 6649-6654.

  26. (113) R. Schweitzer-Stenner, Q. Huang, A. Hagarman, M. Laberge, and C. Wallace. Static normal coordinate deformations of the heme group in mutants of ferro-cytochrome c from Saccharomyces Cerevisiae probed by resonance Raman spectroscopy.  (2007) J. Phys. Chem. B., 111, 6527-6533.

  27. (114) R. Schweitzer-Stenner, R. Shah, A. Hagarman, and I. Dragomir.  Conformational Substates of Horse Heart Cytochrome c Exhibit Different Thermal Unfolding of the Heme Cavity.  (2007) J. Phys. Chem. B. 111, 9603-9607.

  28. (115) R. Schweitzer-Stenner, J. P. Gordon, A. Hagarman.  The Asymmetric Band Profile of the Soret Band of Deoxymyoglobin is Caused by Electronic and Vibronic Perturbations of the Heme Group Rather Than by a Doming Deformation.  (2007)  J. Chem. Phys.  127, 135103, 2007.

  29. (116) R. Schweitzer-Stenner, W. Gonzales, G. T. Bourne, J.A. Feng, and G.R. Marshall. The Conformational Manifold of -Aminoisobutyric Acid (Aib) Containing Alanine-Based Tripeptides in Aqueous Solution Explored by Vibrational Spectroscopy, Electronic Circular Dichroism Spectroscopy, and Molecular Dynamics Simulations. J. Am. Chem. Soc. 129, 13095-13109, 2007.

  30. (117) S. Pizzanelli, C. Forte,S. Monti and R. Schweitzer-Stenner. Interaction of a Tripeptide with Cesium Perfluorooctanoate Micelles. J. Phys. Chem. B. 112, 1251-1261, 2008.

  31. (118)N. Hadjiliadis, K. Panagiotou, M. Panagopoulou, T. Karavelas, V. Dokorou, A. Hagarman, J. Soffer, R. Schweitzer-Stenner and G. Malandrinos. Cu(II) and Ni(II) interactions with the terminally blocked hexapeptide Ac-Leu-Ala-His-Tyr-Asn-Lys-amide, (LAHYNK) model of histone H2B (80-85). Bioinorganic Chem.  Appl., 2008, 257038, 2008.   

  32. (119) R. Shah and R. Schweitzer-Stenner. Structural changes of horse heart ferricytochrome c induced by changes of ionic strength and anion binding. Biochemistry, 47, 5250-5257, 2008.

  33. (120) R. Schweitzer-Stenner. The Internal Electric Field in Cytochrome C Explored by Visible Electronic Circular Dichroism Spectroscopy. J. Phys. Chem. B. 112(33); 10358-10366, 2008. 

  34. (121) A. Hagarman, C. Wallace, M. Laberge, and R. Schweitzer-Stenner. Out-of-plane deformations of the heme group in different ferrocytochrome c proteins probed by resonance Raman spectroscopy. J. Raman Spectrosc., 9999, 2008.

  35. (122) A. Hagarman, Duitch, Laura, and Schweitzer-Stenner, Reinhard. The Conformational Manifold of Ferricytochrome c Explored by Visible and Far-UV Electronic Circular Dichroism. Biochemistry, 47(36); 9667-9677, 2008.

  36. (123) D. Verbaro, A. Hagarman, J.B. Soffer, and Schweitzer-Stenner, Reinhard. The pH Dependence of the 695 nm Charge Transfer Band Reveals the Population of an Intermediate State of the Alkaline Transition of Ferricytochrome c at Low Ion Concentrations. Biochemistry, 48 (13) 2990-2996, 2009.

  37. (124) D. Verbaro, A. Hagarman, A. Kohli and R.Schweitzer-Stenner. Microperoxidase 11: a model system for porphyrin networks and heme–protein interactions. J. Bio. Inorg. Chem.14,1289–1300, 2009.

  38. (125) S. Yang, J-M. Yuan, J. Shin, T.J. Measey, and R. Schweitzer-Stenner and F-Y Li. Energy Landscape Associated with the Self-Aggregation of an alanine-Based Oligopeptide (AAKA). J. Phys. Chem. B. 113, 6054-6061, 2009.

  39. (126) R. Schweitzer-Stenner. Distributions of Conformations Sampled by The Central Amino Acid in Tripeptides Inferred from amide I Band Profiles and Scalar NMR Coupling Constants, J. Phys. Chem. B. 113, 2922-2932, 2009.

  40. (127) A. Hagarman, T. Measey, D. Mathieu, H. Schwalbe and R. Schweitzer-Stenner. Intrinsic Propensities of Amino Acid Residues in GxG Peptides Inferred from Amide I′ Band Profiles and NMR Scalar Coupling Constants. J. Am. Chem. Soc. 132, 540-551,2009.

  41. (128) T.J. Measey, K. Smith, S. Decatur, L. Zhao, G. Yang and R. Schweitzer-Stenner. The Self-aggregation of A Polyalanine Octamer Promoted by Its C-Terminal Tyrosine And Probed By A Strongly Enhanced VCD Signal. J. Am. Chem. Soc. (communication), 131 (51) 18218-18219, 2009.

  42. (129)  L. Tooke, L. Duitch, T.J. Measey and R. Schweitzer-Stenner. Kinetics of the Self-Aggregation and Film Formation of Poly-L-Proline at High Temperatures Explored by Circular Dichroism Spectroscopy. Biopolymers, 93, 451-457, 2010.



1.10. Papers submitted after promotion to Full Professor at Drexel University (2010-present).


  1. (130)  S. Pizzanelli, C. Forte, S. Monti, G. Zandomeneghi, A. Hagarman, T.J.     Measey, and Reinhard Schweitzer-Stenner. Conformations of Phenylalanine     in the Tripeptides AFA     and GFG Probed by Combining MD Simulations     with NMR, FTIR, Polarized Raman,     and VCD Spectroscopy  J. Phys. Chem. B., 114, 3956-3978,  2010.

  2. (131)T. J. Measey and R. Schweitzer-Stenner, Simulation of IR, Raman and VCD  Amide I Band Profiles of Self-Assembled Peptides. Spectroscopy, 24,  25-36, 2010.

  3. (132) T.J. Measey, R. Schweitzer-Stenner, V. Sa, and K. Kornev. Anomalous Conformational Instability and Hydrogel formation of a cationic Class of Self-Assembling Oligopeptides. Macromolecules, 43, 7800-7806, 2010.

  4. (133) D. Verbaro, I. Gosh, W.M. Nau and R. Schweitzer-Stenner. Discrepancies between Conformational Distributions of a Polyalanine Peptide in Solution Obtained from Molecular Dynamics Force Fields and Amide I′ Band Profiles. J. Phys. Chem. B. 114, 17201-17208, 2010.

  5. (134)T.J. Measey and R. Schweitzer-Stenner. Vibrational Circular Dichroism as a Probe of Fibrillogenesis: The Origin of the Anomalous Intensity Enhancement of the Amide I Signal of Amyloid-like Fibrils. J. Am. Chem Soc. 133, 1066-1076, 2011. 

  6. (135)M. Alessi, A. Hagarman, J. B. Soffer and R. Schweitzer-Stenner. In-plane deformations of the heme group in native and non-native oxidized cytochrome c probed by resonance Raman dispersion spectroscopy. J. Raman Spectrosc. 42, 917-924, 2011.

  7. (136)A. Hagarman. D. Mathieu, S. Toal, T.J. Measey, H. Schwalbe, and R. Schweitzer-Stenner. Amino Acids with Hydrogen-Bonding Side Chains have an Intrinsic Tendency to sample various Turn Conformations in Aqueous Solution. Chem. Eur. J. 17, 6789-6797, 2011.

  8. (137)S. Toal, A. Omidi and R. Schweitzer-Stenner. Conformational Changes of Trialanine Induced by Direct Interactions between Alanine Residues and Alcohols in Binary Mixtures of Water with Glycerol and Ethanol. J. Am. Chem. Soc. 133, 12728–12739, 2011

  9. (138) R. Schweitzer-Stenner. Simulated IR, Isotropic and Anisotropic Raman, and Vibrational Circular Dichroism Amide I Band Profiles of Stacked β-Sheets. J. Phys. Chem B., 116, 4141-4153 2012.  

  10. (139) L. Duitch, S. Toal, T.J. Measey, and R. Schweitzer-Stenner. Triaspartate: A Model System for Conformationally Flexible DDD Motifs in Proteins. J. Phys. Chem B. 116, 5160-5171, 2012.

  11. (140) D. Verbaro, D. Mathieu, S.E. Toal, H. Schwalbe, and R. Schweitzer-Stenner. Ionized Trilysine: A Model system for Understanding the Nonrandom Structure of Poly-L-lysine and Lysine-containing Motifs in Proteins. J. Phys. Chem. B. 116, 8084-8094, 2012

  12. (141) R. Schweitzer-Stenner, A. Hagarman, S. Toal, D. Mathieu and H. Schwalbe. Disorder and order in unfolded and disordered peptides and proteins: A view derived from tripeptide conformational analysis. I. Tripeptides with long and predominantly hydrophobic side chains. Proteins, 81, 955-967, 2013. 

  13. (142)  K. Rybka, S. Toal, D. Verbaro, D. Mathieu, H. Schwalbe and R. Schweitzer-Stenner.Disorder and order in unfolded and disordered peptides and proteins: A view derived from tripeptide conformational analysis. II. Tripeptides with short side chains populating asx and β-type like turn conformations. Proteins 81, 968-983, 2013.

  14. (143) J.B. Soffer, E. Fradkin, L. A. Pandiscia and R. Schweitzer-Stenner. The (Not Completely Irreversible) Population of a Misfolded State of Cytochrome c under Folding Conditions. Biochemistry, 52, 1397-1408, 2013.

  15. (144)S.E. Toal, D. Meral, D.J. Verbaro, B. Urbanc and R. Schweitzer-Stenner. The pH-Independence of Trialanine and the Effects of Termini Blocking in Short Peptides: A Combined Vibrational, NMR, UVCD, and Molecular Dynamics Study. J. Phys. Chem. B. 117, 3689-3706, 2013.

  16. (145) R. Schweitzer-Stenner. Different Degrees of disorder in Long Disordered Peptides Can Be Discriminated by Vibrational Spectroscopy. J. Phys. Chem. B., 117,6927-6936. 

  17. (146) N. A. Dixon, J. S. Kraus, A. B. McQuarters, J. B. Soffer, N. Lehnert, R. Schweitzer-Stenner, and E. T. Papish. Dramatic Tuning og Ligand Donor properties in (Ttz)CuCO through Remote Binding of H +(Ttz=Hydrotris(triazolyl)borate). Chem. Comm. 49, 5571, 2013, 2013.

  18. (147)  L. Pandiscia and R. Schweitzer-Stenner. Salt as a Catalyst in the Mitochondria: Returning Cytochrome c to its Native State after it Misfolds on the Surface of Cardiolipin Containing Membranes. Chem. Comm. 19, 1811-1194, 2014.

  19. (148)S.E. Toal, D.J. Verbaro and R. Schweitzer-Stenner, Role of Enthalpy−Entropy Compensation Interactions in Determining the Conformational Propensities of Amino Acid Residues in Unfolded Peptides. J. Phys. Chem. B. 118, 1309-1318, 2014. 

  20. (149) J.B. Soffer and R. Schweitzer-Stenner. Near-exact enthalpy–entropy compensation governs the thermal unfolding of protonation states of oxidized cytochrome c. J. Biol. Inorg. Chem.19:1181–1194, 2014.

  21. (150) R. Schweitzer-Stenner and S.E. Toal. Entropy reduction in unfolded peptides (and proteins) due to conformational preferences of amino acid residues. PhysChemChemPhys. 6, 22527-22536, 2014.

  22. (151) D. Malyshka, L.A. Pandiscia, and R. Schweitzer-Stenner. Cardiolipin containing liposomes are fully ionized at physiological pH.  An FT-IR study of phosphate group ionization. Vib. Spectrosc. 75, 86-92, 2014.

  23. (152) L. A. Pandiscia, and R. Schweitzer-Stenner. Coexistence of Native-like and Non-Native Partially Unfolded Ferricytochrome c on the Surface of Cardiolipin Containing Liposomes. J. Phys. Chem. B, 119, 1334-1349, 2015

  24. (153) S.E. Toal, N. Kobutova, C. Richter, V. Linhard, H. Schwalbe and R. Schweitzer-Stenner.  Randomizing the Unfolded State of Peptides (and) Proteins by Nearest Neighbor Interactions. Chem. Eur. J., 21, 5173-5192, 2015, 2015

  25. (154)D. Meral, S.E. Toal, R. Schweitzer-Stenner and B. Urbanc. Water-Centered Interpretation of Intrinsic pPII Propensities of Amino Acid Residues: In Vitro-Driven Molecular Dynamics Study. J. Phys. Chem. B 119, 13237-13251, 2015.

  26. (155)L. Pandiscia and R. Schweitzer-Stenner. Coexistence of Native-Like and Non-Native Cytochrome c on Anionic Liposomes with Different Cardiolipin Content. J. Phys. Chem. B., 119, 12846-12859, 2015.

  27. (156)B. Milorey, S. Farrell, S.E. Toal and R. Schweitzer-Stenner. Demixing of water and ethanol causes conformational redistribution and gelation of the cationic GAG tripeptide. Chem. Comm. 51, 16498-16501, 2015

  28. (157)N.V. Ilawe, A.E. Raeber, R. Schweitzer-Stenner, S.E. Toal, and B.M. Wong. Assessing backbone solvation effects in the conformational propensities of amino acid residues in unfolded peptides. Phys.Chem.Chem.Phys. 17, 24917-24924, 2015.

  29. (158) E.Crenshaw, B.P. Leung, C.K. Kwok, M.Sharoni, K. Olson ; N.P. Sebastian, S. Ansaloni, R. Schweitzer-Stenner, Reinhard, M.R. Akins ; P.C.   Bevilacqua, and A.J. Saunders. Amyloid Precursor Protein Translation Is Regulated by a 3 ' UTR Guanine Quadruplex. PLOS, 10, e0143160, 2015.

  30. (159) D. DiGuiseppi and R. Schweitzer-Stenner. Probing conformational propensities of histidine in different protonation states of the unblocked glycyl-histidyl-glycine peptide by vibrational and NMR spectroscopy. J. Raman Spectrosc. 47, 1063-1072, 2016.

  31. (160) S. Farrell, D. DiGuiseppi, N.J. Alvarez, and R. Schweitzer-Stenner. The interplay of aggregation, fibrilization and gelation  of an unexpected low molecular weight gelator: glycyleanalylglycine in ethanol/water. Soft Matter  12, 6096-6610, 2016.

  32. (161)  J. Smith, D. Hagarman, D. DiGuiseppi, R. Schweitzer-Stenner and H.-F. Ji. Ultra-Long Crystalline Red Phosphorus Nanowires from Amorphous Red Phosphorus Thin Films. Angew. Chemie (Int. Edition), 55, 11829-11833, 2016.

  33. (162)   Schweitzer-Stenner and S.E. Toal. Construction and Comparison of the Statistical Coil States of Unfolded and Intrinsically Disordered Proteins from Nearest-Neighbor Corrected Conformational Propensities of Short Peptides. Mol. BioSys. 12, 3294-3306, 2016

  34. (163)   D.DiGuiseppi, J. Kraus, S.E. Toal, N. Alvarez and R. Schweitzer-Stenner.Investigating the Formation of a Repulsive Hydrogel of a Cationic 16mer Peptide at Low Ionic Strength in Water by Vibrational  Spectroscopy and Rheology. J. Phys. Chem B.120, 10079−10090, 2016.

  35. (164)    L. Serpas, B. Milorey, L.A. Pandiscia, A.W. Addison, and R. Schweitzer-Stenner. Autoxidation of Reduced Horse Heart Cytochrome c Catalyzed by Cardiolipin-Containing Membranes. J. Phys. Chem. B. 120, 12219-12231, 2016

  36. (165)    D. Malyshka, and R. Schweitzer-Stenner. Ferrocyanide-mediated Photoreduction of Ferricytochrome c Utilized to Selectively Probe Non-Native Conformation Induced by Binding to Cardiolipin Containing Membranes. Chem. Eur. J.23, 1151-1156, 2017

  37. (166)   B. Milorey, D. Malyshka and R. Schweitzer-Stenner. pH Dependence of Ferricytochrome c Conformational Transitions during Binding to Cardiolipin Membranes: Evidence for Histidine as the Distal Ligand at neutral pH. J. Phys. Chem. Lett. 8, 1993-1998, 2017.


2.0. Invited review and book articles (1989 - Present).


  1. (167) R. Schweitzer-Stenner. Allosteric linkage induced distortions of the prosthetic group in heme proteins as derived from the theoretical interpretation of the depolarization ratio in resonance Raman scattering. Q. Rev. Biophys. 32, 381-490, 1989.

  2. (168) R. Schweitzer-Stenner. Parameters determining the stimulatory capacity of the type I Fcε-receptor. Immunol. Lett. 68, 59-69, 1999. . 

  3. (169) R. Schweitzer-Stenner. Polarized Resonance Raman Dispersion Spectroscopy on Metalporphyrins. J. Porphyr. Phthal. 5, 198-224, 2001.

  4. (170) R. Schweitzer-Stenner. Visible and UV-resonance Raman spectroscopy on model peptides. J. Raman Spectrosc., 32,711-732, 2001.

  5. (171) R. Schweitzer-Stenner. Advances in Vibrational Spectroscopy as a Sensitive Probe of Peptide and Protein Structure. A critical review.  Vib. Spectrosc. 98-117, 2006.

  6. (172)R. Schweitzer-Stenner. Conformational analysis of unfolded peptides by vibrational spectroscopy. In: Unfolded Proteins. From Denatured States to Intrinsically Disordered, Ed. T. Creamer. Novalis Press, 101-142, 2008.

  7. (173) R. Schweitzer-Stenner, A. Hagarman, D. Verbaro and J. Soffer.  Conformational Stability of Cytochrome c Probed by Optical Spectroscopy, Meth. Enzymol.109-153, 2009.

  8. (174)R. Schweitzer-Stenner, T. Measey, A. Hagarman, and I. Dragomir. The Structure of unfolded peptides and proteins explored by Raman and IR spectroscopies. In: Assessing Structures and Conformation of Intrinsically Disordered Proteins”, Editors: S. Longhi and V.N. Uversky. Wiley & Sons, 171-224, 2010.

  9. (175) R. Schweitzer-Stenner and J.B. Soffer. Other Spectroscopy: UV-Vis, CD, Raman, Vibrational CD Applied in Biophysical Research. In: Comprehensive Biophysics, Vol. 1.  Biophysical Techniques for Structural Characterization  of Macromolecules. Ed. Jane Dyson, Elsevier, 533-591, 2011.

  10. (176) R. Schweitzer-Stenner, Conformational propensities and residual structures in unfolded peptides and proteins. (Invited Review) Mol. BioSys. 8, 122-133, 2012.

  11. (177) R. Schweitzer-Stenner. Using Spectroscopic Tools To Probe Porphyrin Deformation and Porphyrin-Protein Interactions. J. Porphyrins Phthalocyanines (invited review for special issue dedicated to the 65th birthday of Prof. John A. Shelnutt), 15, 312-337, 2011.

  12. (178) T.J. Measey and R. Schweitzer-Stenner. Self-Assembling Alanine-Rich Peptides of Biomedical and Biotechnological Relevance. In: Proteins and Peptides. Folding, Misfolding and Unfolding. Ed: R. Schweitzer-Stenner, Wiley & Sons, Chichester, pp. 309-350, 2012.

  13. (179)  J.B. Soffer, S. Toal and D. Verbaro. Structural Analysis of Unfolded Peptides by Raman Spectroscopy. In: Experimental Tools for the Intrinsically Disordered Protein Analysis. Volume I, Eds. V. Usversky and K. Dunker,  Humana Press (Springer), pp. 271-314, 2012.

  14. (180) R. Schweitzer-Stenner, J.B. Soffer and D. Verbaro. Structural Analysis of Unfolded Peptides by Vibrational Circular Dichroism Spectroscopy. In: Experimental Tools for the Intrinsically Disordered Protein Analysis. Volume I, Eds. V. Usversky and K. Dunker,  Humana Press (Springer), 315-346, 2012.

  15. (181)  R. Schweitzer-Stenner. Cytochrome c: A Multifunctional Protein Combining Conformational Rigidity with Flexibility. New J. Sci. i484538, 2014.

  16. (182)  S.E. Toal and R. Schweitzer-Stenner. Local Order in the Unfolded State: Conformational Biases and Nearest Neighbor Interactions. Biomolecules, 4, 725-773, 2014.



  1. 3.Invited talks, lectures and conference organization 1983-present


A. Talks at Conferences and Symposia


  1. 1.R. Schweitzer-Stenner, B. Milorey, D. Malyshka, L. Pandiscia,and L. Serpas. Probing the Binding of Cytochrome c to Cardiolipin by Optical and Resonance Raman Spectroscopy, 6th. CanBic, Perry Sound, Canada, 2017.

  2. 2.R. Schweitzer-Stenner, L.A. Pandiscia, L. Serpas and D. Malyshka. Exploring Different Binding Sites of Cytochrome c to Cardiolipin Containing Anionic Liposomes Explored By Fluorescence, Circular Dichroism and Resonance Raman Spectroscopy, 5th. CanBic, Perry Sound, Canada, 2015.

  3. 3.R.Schweitzer-Stenner, L.A. Pandiscia, L. Serpas and D. Malyshka. Conformational Diversity of Cytochrome c on Cardiolipin Containing Liposomes Probed by Fluorescence and Circular Dichroism Spectroscopy. Spring Meeting of the American Chemical Society. Denver, March, 2015 (unable to attend for medical reasons, the talk was given by the second author, L.A. Pandiscia).

  4. 4.R. Schweitzer-Stenner and T.J. Measey: Unexpected Self-Assembly of Peptides and their Structural Analysis. PittCon 2013, Philadelphia.

  5. 5.R. Schweitzer-Stenner: Partially Unfolded States of Cytochrome c in Solution and on Liposomes. 4th. CanBic, Perry Sound, Canada, 2013.

  6. 6.R. Schweitzer-Stenner, S. Toal, D. Verbaro, D. Meral and Brigita Urbanc  Conformational Distributions of Amino Acid Residues in Unfolded Peptides and Proteins: How Random is The So Called Random Coil State. International Scientific Seminar - Kavli Seminar: Multiscale systems: linking quantum chemistry, molecular dynamics, and microfluidic hydrodynamics. London, 2013.

  7. 7.R. Schweitzer-Stenner, S.E. Toal, S. Zimmer, Y. Lee, H. Schwalbe. Influence of nearest neighbors and solvent composition on conformational propensities of amino acid residues in unfolded peptides. Annual Meeting of the American Chemical Society, San Diego, CA, March 2012.

  8. 8.R. Schweitzer-Stenner, A. Hagarman, T.J. Measey, D. Verbaro and Siobhan Toal,  Using Vibrational, Optical and NMR Spectroscopy to Explore Unfolded and Misfolded States of Peptides. PittCon, Orlando, FL, March 2012.

  9. 9.R. Schweitzer-Stenner. Using Vibrational, Optical and NMR Spectroscopy To Explore Unfolded and Misfolded State of Peptides. 1st Symposium on Higher Order Structure of Protein Therapeutics, Rockville, MD, September 2011.

  10. 10.R. Schweitzer-Stenner, J.B. Soffer, L.Pandiscia, E. Fradkin, and D. Verbaro. Using Circular Dichroism and Resonance Raman Spectroscopy to Probe Non-Native States of Cytochrome c. 3rd Georgian Bay Conference on Bio-Inorganic Chemistry, Pary Sound, Canada, June 2011. 

  11. 11.R. Schweitzer-Stenner. Electronic and vibronic perturbations of porphyrins in heme proteins by combining absorption, circular dichroism and resonance Raman spectroscopy. Sixth International Conference on Porphyrins and Phthalocyanines (ICPP), Santa Ana Pueblo, New Mexico (July 2010).  

  12. 12.R. Schweitzer-Stenner. Probing the VCD signal of amide Iʼ is pivotal for probing conformational propensities of amino acids in unfolded peptides and peptide self-aggregation in aqueous solution. 2nd International Conference on the Vibrational optical activity of Biomolecules. Albany, NY, August 2010. 

  13. 13.R. Schweitzer-Stenner, Unfolded and Self-Aggregated States of Unfolded Peptides. European Conference on the Spectroscopy of Biological Systems, Palermo, August 31-September 4, 2009. 

  14. 14.“Peptides as Model Systems for The Unfolded State of Proteins Explored By Vibrational Spectroscopy.” International Conference on Perspectives in Vibrational Spectroscopy, Trivandrum, India, February, 2008.  

  15. 15.“Non-planar deformations of metal porphyrins in solution and in proteins probed by Resonance Raman spectroscopy.”  Pacifichem 2005, Honolulu, December, 2005.  

  16. 16.“The excitonic coupling between amide I modes as a tool for the structure analysis of polypeptides.” Invited lecture at COBRE II conference on the ‘Structure, Function and Dynamics of Biomolecules, San Juan, Puerto Rico, San Juan, February 16-19, 2005.  

  17. 17.“Exploring the Structure of ‘Unfolded Peptides’ by Combining VCD and ECD with IR and Polarized Raman Spectroscopy.” Invited lecture at 10th International Conference on Circular Dichroism Spectroscopy (CD 2005), Destin, Florida,  August 21- 25, 2005.   

  18. 18.“Structure Analysis of Unfolded Peptides by Combining IR, Polarized Raman, Vibrational and Electronic Circular Dichroism Spectroscopy.” Invited lecture at the International Conference on Advanced Vibrational Spectroscopy (ICAVS 3), Delevan, Wisconsin, August 14-19, 2005. 

  19. 19.“Structure Analysis of Tripeptides in Solution by Polarized Raman, FTIR and Vibrational Circular Dichroism Spectroscopy” Invited Lecture at the XVIIIth International Raman Conference in Budapest, Hungary, organized by Janos Minsk, July 2002.   

  20. 20.“Structure Analysis of Di- and Tripeptides by Polarized Raman, FTIR and Vibrational Circular Dichroism Spectroscopy”  Invited Lecture at the First International Conference on Biomedical Spectroscopy, Cardiff, UK, organized by Dr. Parvez Haris, June 2002.  

  21. 21.“Electronic and Vibronic Distortions of Metalloporphyrins in Organic Solvents Probed by Resonance Raman Dispersion Spectroscopy“ Symposium lecture at the 1st International Conference on Porphyrins and Phthalocyanines, Dijon, France, organized by Roger Guilard and Karl M. Kadish, July 2000.

  22. 13."Resonance Raman Dispersion Spectroscopy probes asymmetric distortions of porphyrins in solution and proteins", Plenary lecture at the 8th European Conference on the Spectroscopy on Biological Molecules, Enschede, NL, organized by Prof. Jan Greve, September, 1999. 

  23. 14.”Life Time and Spatial Proximity. An Attempt to Quantitatively Assess the Relationship Between Receptor Aggregation and Transmembrane Signaling in Mast Cells” ‘10th Symposium on Signals and Signal Processing in the Immune System’ in Balatonöszöd, Hungary, organized by Prof. Janós Gergely, Göd, September 1998.

  24. 15.”The Impact of Protein Dynamics on Metal-Containing Chromophores: Taxonomic versus Continous Distribution of Substates”  ”Are proteins organized hierachically” Workshop in the Academy of Telluride, Telluride, CO, organized by Profs. Friedmann (New York) and Agmon (Jerusalem),  Telluride, USA, July 1997.

  25. 16.Vibrational mixing between model peptides and water probed by Raman and FT-IR spectroscopy.” 2nd Workshop of the EU-network ‘The Dynamics of Protein Function’ in San Miniato, Italy, organized by Prof. F. Parak, TU München, September 1996.  

  26. 17.”Conformational substates of the proximal Fe-His F8 linkage in myoglobin and hemoglobin probed by resonance Raman and optical spectroscopy” ‘The Dynamic-Heme Symposium, (organized by N. Agmon and J. Friedman)  Jerusalem 1995.  

  27. 18.”Conformational substates of the proximal Fe- His F8 complex in hemoglobin trout IV” Gordon Conference on ‘Vibrational Spectroscopy’ in Wolfboro, New Hampshire, USA, July 1992.  5)”pH-induced heme-protein interactions in hemoglobin derivatives detected by resonance Raman spectroscopy” Symposium on ‘Dynamics and Function of Heme Proteins’, NIH, Bethesda, USA, June 1990. 

  28. 19.”Correlation between Root-effect and conformational changes of the active site detected by resonance Raman scattering at haemoglobin trout IV.”  Annual Meeting of the ‘Society for Experimental Biology’, Edingburgh, April 1989. 


 

B. Talks at Scientific Institutions


1.  “Conformational Ensembles of Amino Acid Residues in Unfolded Peptides Probed by Combining Vibrational, Circular Dichroism and NMR Spectroscopy. Institute of Organic Chemistry Seminar, Johann Wolfgang Goethe University, Frankfurt, Germany, December 2013.

2.  Biophysical and Spectroscopic Investigations of Cytochrome . Seminar, Department of Chemistry, University of Akron, February 2011

3.“Is the Unfolded State of Peptides Really Random? Department of Chemistry Seminar. Mary and William College, Wiilimasburg, A, October 2010

4.“Using vibrational, optical and NMR spectroscopy to explore unfolded and self-aggregated peptides.” Department of Chemistry, SUNY-Albany, NY, September 2009.

5.“Different conformations of cytochrome c in solution Explored by resonance Raman, low temperature absorption and CD spectroscopy”, Department of Biophysics and Physiology, Albert Einstein College of Medicine, New York, NY, May 2008. 

6.“The conformational manifold of unfolded peptides probed by vibrational and NMR spectroscopy” Department of Chemistry, University of Pennsylvannia, Philadelphia, PA April 2008. 

7.“Is the unfolded state of peptides (and proteins) really a random coil” Department of Chemistry, Muhlenberg College, Allentown, PA, September 2007. 

8.“Is the unfolded state of peptides (and proteins) really a random coil” Department of Chemistry, New York University, New York, NY, March, 2007. 

9.“Is the unfolded state of peptides (and proteins) really a random coil” Department of Chemistry, Shippensburg University, Shippensburg, PA, November 2006. 

10.“Is the unfolded state of peptides (and proteins) really a random coil”, Department of Physics, Applied Physics and Astronomy, Rensselaer Polytechnic Institute, Troy, NY, November 2006. 

11.“A Physicists look on Myoglobin and Cytochrome c” Department of Chemistry, Wikes University, Wilkes-Barre, PA, November 2006. 

12.“Is the unfolded state of peptides (and proteins) really a random coil” Department of Chemistry, University of Illinois, Chicago, IL, October, 2006. 

13.“Is the unfolded state of peptides (and proteins) really a random coil” Department of Chemistry, Rutgers University, Newark, NJ, September, 2006. 

14.“Is the unfolded state of peptides (and proteins) really a random coil” Department of Chemistry, University of Science, Philadelphia, PA, September, 2006.

15.“Deformations and Perturbations of Porphyrins in Solution and in Proteins Probed By Resonance Raman and Low Temperature Absorption Spectroscopy” Institute of Physics and Astronomy, Palermo, Italy, July 2006. 

16.“Is the unfolded state of peptides (and proteins) really a random coil” Institute of Physics and Astronomy, Palermo, Italy, July 2006. 

17.“Is the unfolded state of peptides (and proteins) really a random coil” Consiglio Nazionale della Richereche, Pisa, Italy, July 2006. 

18.“Functionally relevant heme distortions in horseradish peroxidase and cytochrome c probed by resonance Raman dispersion and optical absorption spectroscopy” Franklin and Marshall College, Lancaster, PA, March 2006. 

19.“Functionally relevant heme distortions in horseradish peroxidase and cytochrome c probed by resonance Raman dispersion and optical absorption spectroscopy.” Department of Chemistry, Juniata College, Huntingdon, PA, April 2005. 

20.“Structure Analysis of Short Peptides in Solution: A Tool to Understand The Unfolded State of Peptides and Proteins.” Department of Chemistry, SUNY-Potsdam, Potsdam, NY, March 2005.

21.“Structure Analysis of Short Peptides in Solution: A Tool to Understand The Unfolded State of Peptides and Proteins.” Department of Chemistry, St. Lawrence University, Canton, NY, March 2005. 

22.“Structure Analysis of Short Peptides in Solution: A Tool to Understand The Unfolded State of Peptides and Proteins.” Center for Computational Biology, Washington University, St. Louis, February 2005. 

23.“Resonance Raman Dispersion Spectroscopy: An Ideal Tool to Probe Functionally Relevant Deformations of The Active Site of Heme Proteins. Department of Biochemistry, University of Pennsylvania, Medical School, Philadlephia, April 2004. 

24.“Tri- and Tetrapeptides as Model Systems for The Understanding of the Unfolded State of Peptides and Proteins”  Department of Biology, International University Bremen, Bremen, Germany, March 2004. 

25.“Tri- and Tetrapeptides as Model Systems for The Understanding of the Unfolded State of Peptides and Proteins” `Theoretical Biology and Biophysics Group, Los Alamos National Laboratory, Los Alamos, February 2004. 

26.“Tripeptides as Model Systems for The Understanding of the Unfolded State of Peptides and Proteins.” Institut für Biophysik, Johann Wolfgang Goethe Universität, Frankfurt, Germany, June 2003. 

27.“Tripeptides as Model Systems for The Understanding of the Unfolded State of Peptides and Proteins.” Department of Physics, Georgia State University, Atlanta, GA, February 2003.

28.“Tripeptides as Model Systems for The Understanding of the Unfolded State of Peptides and Proteins.” Department of Chemistry, Drexel University, Philadelphia, PA, January 2003.

29.“Secondary structure of tripeptides in solution probed by visible Raman, IR and VCD spectroscopy” Department of Immunology, The Weizmann Institute of Science, Rehovot, Israel, October 2002.

30.“Secondary structure of tripeptides in solution probed by visible Raman, IR and VCD spectroscopy” Department of Physical Chemistry, Hebrew University, Jerusalem, Israel, October 2002. 

31.“Secondary structure of tripeptides in solution probed by visible Raman, IR and VCD spectroscopy” Institut für Physikalische Chemie, Johann Wolfgang Goethe Universität Frankfurt, Frankfurt, Germany, October 2002.

32.“Secondary structure of tripeptides in solution probed by visible Raman, IR and VCD spectroscopy”. Department of Chemistry, Duquesne University, Pittsburgh, September 2002. 

33.“Structure analysis of tripeptides by polarized visible Raman, FTIR  and VCD spectroscopy”. Department of Chemistry, University of Lethbridge, Lethbridge, Canada,  June, 2002.

34.“Functional relevant distortions of the prosthetic groups in heme proteins probed by resonance Raman Dispersion Spectroscopy”. Department of Chemistry, University of Western Ontario, London, Canada, April 2002. 

35.“Structure analysis of tripeptides by polarized visible Raman, FTIR  and VCD spectroscopy.” Department of Chemistry, University of Windsor, Windsor, Canada, April 2002.

36.“Structure analysis of di- and tripeptides by polarized visible Raman and FTIR spectroscopy. Department of Chemistry, Syracuse University, Syracuse, February 2002.

37.“Functional relevant distortions of the prosthetic groups in heme proteins probed by resonance Raman Dispersion Spectroscopy.  Institute of Biophysics and Radiation Biology, Semmelweis University, Budapest, Hungary, July 2001. 

38.“Di- and Tripeptides as The Cornerstone for The Structure Analysis of Proteins” Department of Chemistry, University of Maryland, Baltimore County, April 2001. 

39.“Vibrational and structural dynamics of model peptides” Department of Chemistry, University of Louisville, Louisville, KY, November 2000. 

40.“Influence of peripheral substituents and metal on structure and dynamics of porphyrins”  Institute of Physical Chemistry, University of Würzburg, Würzburg, May 2000. 

41."Structural Heterogeneity and Vibrational Dynamics of Model Peptides Probed by IR, Visible, and UV-Resonance Raman Spectroscopy" Department of Chemistry, University of Copenhagen, Copenhagen, Denmark,  May 1999. 

42.“Resonance Raman Dispersion Spectroscopy. A Tool to Probe Functionally Relevant Distortions of Chromophores in Biological Macromolecules.” Department of Physics, Washington University, St. Louis, USA, January 1999. 

43."Structural Heterogeneity and Vibrational Dynamics of Model Peptides Probed by IR, Visible, and UV-Resonance Raman Spectroscopy", Department of Chemistry, University of Puerto Rico, Rio Pedras, San Juan, USA, December 1998.

44.”Peptide Structure and Vibrational Dynamics Probed By Non-Resonance,  Resonance UV-Raman and FTIR-Spectroscopy” Istituto di Fisica, Universita di Palermo, Palermo, Italia, July 1998. 

45.”Peptide Structure and Vibrational Dynamics Probed By Non-Resonance And Resonance UV-Raman Spectroscopy” National Institute of Standards, Gaithersburg, MA, February, 1998. 

46.”Struktur und Dynamik von Peptiden” Drittes Physikalisches Institut der Universität Göttingen. Göttingen, December, 1997.

47.”Ramanspektroskopie an Myoglobin: Subkonformationen und statische Verzerrungen des aktiven Zentrums.” Institut für Biophysik, Universität Ulm, Ulm, July 1997. 

48.”Raman- und optische Spektroskopie an Myoglobin” Institut für Biophysik, TU München, München, June 1997. 

49.”Raman Dispersionsspektroskopie an Porphyrinen in organischen Lösungen und Proteinen. Institut für Physikalische und Theroretische Chemie, TU München, München, May 1997. 

50.”Struktur und Dynamik von Modellpeptiden” Insitut für Biophysik und Medizinische Physik, Universität Münster, Münster, November 1996. 

51.”Raman dispersion spectroscopy probes out-off-plane distortions of metalloporphyrins in organic solvents” Department of Physics, University of Palermo, Palermo, Italy, März 1996. 

52.”Bindung von Liganden an den Typ I Fce - Rezeptor auf der Oberfläche von Mastzellen”, Humboldt-Universität Berlin, Berlin,  October 1995.  

53.”Raman dispersion spectroscopy probes asymmetric distortions of porphyrins in solution and in a protein environment” Sackler Institut of Medicine, Tel Aviv University, Tel Aviv, Israel, September 1995. 

54."Conformational substates in hemoglobin and myoglobin probed by the Raman active Fe2+-Ne (His F8) stretching mode." Department of Physics, University of Illinois, Urbana-Champaign, USA,  September 1994. 

55."Conformational substates in myoglobin probed by vibrational spectroscopies. Do proteins behave like glasses?" Department of Chemistry, University of Pittsburgh, Pittsburgh, USA, June, 1994.

56."Raman dispersion spectroscopy probes electronic and vibronic coupling in metalloporphyrins and their dependence on steric and electronic properties of the peripheral substituents" Fuel Science Division, Sandia National Laboratories and Department of Chemistry, University of New Mexico, Albuquerque, USA,  April, 1994. 

57.”Stimulus-Secretion Coupling. The Mast Cell Case” Department of Chemistry, Cornell University, Ithaca, USA, February 1994. 

58."Raman Dispersion Spectroscopy and the Fe2+ - His F8 Raman band are used to probe heme - protein interactions in hemoglobin and myoglobin" Department of Biophysics and Physiology, Albert Einstein Institute of Medicine, Bronx, USA, January, 1994. 

59."Resonance Raman Spectroscopy probes different conformations of metalloporphyrins in solution" Department of Chemistry, University of Pittsburgh, Pittsburgh, USA, December, 1993.

60."Conformational substates in myoglobin and hemoglobin probed by vibrational spectroscopies" Biophysics Research Division, University of Michigan, Ann Arbor, USA, November, 1993. 

61."Conformational substates in myoglobin probed by vibrational spectroscopies." Physics Department, University of Twente, Enschede, Netherland,  September, 1993. 

62."Receptor crosslinking by monoclonal antibodies in solution and on the surface of mast cells" Department of Biological Chemistry, University of Michigan, Ann Arbor, USA, November, 1993.

63."Allosteric mechanism and heme - protein coupling in hemoglobin derivatives investigated by Raman Dispersion Spectroscopy" Department of Physics, University of Illinois, Urbana-Champaign, USA, February, 1993.

64."Untersuchung von Konformationssubzustände in Hämoglobin durch resonante Ramanspektroskopie" Max Delbrück Institut für Molekulare Medizin, Berlin, Germany, September, 1992. 

65."Ramanspektroskopische Untersuchungen an Porphyrinen" Institut für Physik, Medizinische Hochschule Lübeck, Lübeck, Germany, February, 1992. 

66."Allosteric coupling in hemoglobin derivatives probed by resonance Raman spectroscopy" Physics Department, University of Michigan, Ann Arbor, USA, February, 1992. 

67."Untersuchung von allosterischen Wechselwirkungen in Hämproteinen durch resonante Ramanspektroskopie" Institut für Physikalische Chemie, Universität Würzburg, Würzburg, Germany, December, 1991. 

68."Vernetzung von Rezeptoren in Lösung und auf der Oberfläche von Mastzellen" Institut für Physikalische Chemie, Johannes Gutenberg Universität, Mainz, Germany,  November, 1991. 

69."Allosteric mechanism in hemoglobin probed by resonance Raman spectroscopy" Abteilung Biophysik, Biozentrum der Universität, Basel, Switzerland, November, 1990. 

  1. 70."pH-induced distortions in hemoglobin investigated by resonance Raman spectroscopy" Polymer Department, The Weizmann Institute of Science, Rehovot, Israel,  November, 1985.

  2. 71.pH-induced distortions in hemoglobin investigated by resonance Raman spectroscopy"  Max Planck Institut für Biophysikalische Chemie (AG. Prof. Manfred Eigen), Göttingen, Germany, August, 1983. 




C. Guest Teaching


1.Lectures on ‘Vibrational spectroscopy on Bioinoganic Metal Complexes’ at ‘Department of Chemsitry Summerschool’, University of Ionannina, Ioannina, Greece. May 26-31, 2008. 

2.Lectures on : ‘Raman Spectroscopy on Biological Molecules’ at ‘Istituto di Fisica, Universita’ di Palermo’, Palermo, Italy, July 13-25, 1998.



D. Organization of Conferences


1.Raman Spectroscopy on Biological Molecules’ in Bremen 1992 as a satellite meeting of the XIV-th International Conference on Raman Spectroscopy in Würzburg (R. Schweitzer-Stenner and W. Dreybrodt, Co-Organizers).



F. Official Tasks at National and International Meetings


1.American Biophysical Society, Annual Meeting 2011 in Baltimore, MD: Organizer and chairperson of the platform: ‘Unfolded Peptides and Proteins.

2.American Biophysical Society, Annual Meeting 2009 in Boston, MA: Organizer and chairperson of the platform: ‘Unfolded Peptides and Proteins.

3.International Conference on Perspectives in Vibrational Spectroscopy, Trivandrum, India, 2008: Session chair.

4.American Biophysical Society, Annual Meeting 2007 in Baltimore, MD: Organizer and chairperson of the platform: ‘Unfolded Peptides and Proteins.

5.American Chemical Society, Pacifichem 2004, Honolulu, HW Chairperson of a session on porphyrin non-planarity.

6.American Biophysical Society, Annual Meeting 2003 in San Antonio, TX: Organizer and chairperson of the platform: ‘Structure and Dynamics of Peptides’.

7.First Colloquium on Protein Structure, Function and Dynamics 2003 in Ponce, Puerto Rico, Organizer and Chairman of a session on “Vibrational Spectroscopy”.

8.First International Conference on Biomedical Spectroscopy 2002 in Cardiff, UK: Chairman of a session on FTIR-spectroscopy.

9.American Biophysical Society, Annual Meeting 2002 in San Francisco, CA: Organizer and chairperson of the platform: ‘Structure and Dynamics of Biomolecules Probed By Vibrational spectroscopy.

10.American Biophysical Society, Annual Meeting 1998 in Kansas City, MO: Organizer and chairperson of the platform: ‘Vibrational spectroscopy on proteins, peptides and related model compounds’.

11.American Biophysical Society, Annual Meeting 1997 in New Orleans, LO’: Chairperson of the platform on ‘ Conformations of Peptides and Proteins’

12.XVth International Conference on Raman Spectroscopy, Pittsburgh, 1996: Presider of the session on ‘Vibrational Dynamics’.

13.The Dynamic-Heme Symposium”, Jerusalem 1995: Chairperson of a session.