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 in Frankfurt
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:
Do Molecular Dynamics Force Fields Capture Conformational Dynamics of Alanine in Water
Shuting Zeng, Reinhard Schweitzer-Stenner and Brigita Urbanc
Journal of Chemical Theory and Computation 16, 510-527, 2020
Exploring the thermal reversibility and tunability of a low molecular weight gelator using
vibrational and electronic spectroscopyand rheology†
David DiGuiseppi, Lavenia Thursch, Nicolas J. Alvarez and Reinhard Schweitzer-Stenner
Soft Matter, 15, 3418-3431, 2019
Cationic glycylalanylglycine (GAG) self-assembles into a gel in a 55 mol% ethanol/45 mol% water mixture. The gel exhibits a network of crystalline fibrils grown to lengths on a sub-millimeter scale Rheological data are indicative of a rather strong gel with storage modulus in the 10 kPa regime. Spectroscopic data revealed the existence of two gel phases; one forms belowT = 15 C phase I) while the other one forms in a temperature range between 15 C and the melting temperature of ca. 35 C (phase II). We explored the reformation of the cationic GAG gel in 55 mol%/ethanol/45 mol% water after thermal annealing by spectroscopic and rheological means. Our data revealthat even a short residence time of 5 minutes in the sol phase at 50 C produced a delay of the gelation process and a gel of lesser strength. These observations suggest that the residence time at the annealing temperature can be used to adjust the strength of both gel phases. Our spectroscopic data show that the annealing process does not change the chirality of peptide fibrils in the two gel phases and that the initial aggregation state of the reformation process is by far more ordered for phase I than it is for phase II. Inthe gel phases of GAG/ethanol/water mixtures, ethanol seems to function as a sort of catalyst that enables the self-assembly of the peptide in spite of its low intrinsic propensity for aggregation.
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.
Please direct questions and comments to Reinhard Schweitzer-Stenner
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