The Drexel Biospectroscopy Research Group
The Drexel Biospectroscopy Research Group
More about our Group
Drexel University
Department of Chemistry
32nd and Chestnut Street
Philadelphia, PA 19104
Group events: Bridget Milorey celebrates her successful thesis defense.
Book Spotlight
Schweitzer-Stenner, Reinhard ; Uversky, Vladimir
Peptide Folding, Misfolding, and Nonfolding
Wiley Series in Protein and Peptide Science
Edition - April 2012
2012. 576 Pages, Hardcover
ISBN-10: 0-470-59169-2
ISBN-13: 978-0-470-59169-7 - John Wiley & Sons
Uversky, Vladimir N.; Dunker, A. Keith
Intrinsically Disordered Protein Analysis
Volume 1, Methods and Experimental Tools
Springer Series in Methods in Molecular Biology, Vol. 896
Edition - June 2012
2012. 470 Pages, Hardcover
ISBN-13: 978-1-61779-926-6 - Humana Press
Chapers 18 and 19 Contributed to the Series
Egelman, E
Comprehensive Biophysics
1st Edition, Biophysical Techniques for Structural Characterization of Macromolecules
Elsevier
Edition - May 2012
2012. 3524 Pages, Hardcover
ISBN: 9780123749208 - Academic Press
Chaper 1.23 Contributed to the Series
Spotlight on recent publications:
Bridget in front of a 800 Mhz NMR spectrometer in the Wasserwerk (Johann Wolfgang Goethe University), She uses a 600 Mhz instrument in the same building
Bridget on City Hall Square in Frankfurt am Main.
Concentration Dependence of a Hydrogel Phase Formed by the Deprotonation of the Imidazole Side Chain of Glycylhistidylglycine
Morgan Hesser, Lavenia J. Thursch, Todd R. Lewis, Thamires A. Lima, Nicolas J. Alvarez,*and Reinhard Schweitzer-Stenner Langmuir, 37, 6935-6946
ABSTRACT: Upon deprotonation of its imidazole group at ∼pH 6, the
unblocked tripeptide glycylhistidylglycine (GHG) self-assembles into very
long crystalline fibrils on a 10−1000 μm scale which are capable of forming
a volume spanning network, that is, hydrogel. The critical peptide
concentration for self-assembly at a pH of 6 lies between 50 and 60 mM.
The fraction of peptides that self-assemble into fibrils depends on the
concentration of deprotonated GHG. While IR spectra seem to indicate
the formation of fibrils with standard amyloid fibril β-sheet structures,
vibrational circular dichroism spectra show a strongly enhanced amide I′
signal, suggesting that the formed fibrils exhibit significant chirality. The
fibril chirality appears to be a function of peptide concentration. Rheological measurements reveal that the rate of gelation is concentration-dependent and that there is an optimum gel strength atintermediate peptide concentrations of ca. 175 mM. This paper outlines the unique properties of the GHG gel phase which is underlain by a surprisingly dense fibril network with an exceptionally strong modulus that make them potential additives for biomedical applications.
Repeating Aspartic Acid Residues Prefer Turn-like Conformations in the Unfolded State: Implications for Early Protein Folding
Bridget Milorey, Harald Schwalbe, Nichole O’Neill, and Reinhard Schweitzer-Stenner. JPC B 125, 11392-11407, 2021
Please direct questions and comments to Reinhard Schweitzer-Stenner
Page created by Jonathan B. Soffer
Page maintained by Reinhard Schweitzer-Stenner