Journal of Spectroscopy

Journal of Spectroscopy / 2010 / Article
Special Issue

From Molecule to Tissue: XIII European Conference on the Spectroscopy of Biological Molecules, Palermo, Italy, August 28–September 2, 2009, Part 2 of 2

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Open Access

Volume 24 |Article ID 816505 | 5 pages | https://doi.org/10.3233/SPE-2010-0432

Thermally Stimulated Depolarization Currents (TSDC): A sensitive technique for analyzing protein structure

Abstract

The water molecules surrounding proteins as a thin layer and those packaged in pockets and cavities shape and control their structure. Thermally Stimulated Depolarization Currents (TSDC) technique has been applied to investigate the hydration structure of six proteins with different structural motifs: pepsin, β-lactoglobulin, α-chymotrypsin, bovine serum albumin, human serum albumin and myoglobin, at very low hydration level (water vapor activity aw≈0.80) both in the native state and after treatment in trifluoroethanol/water mixture 80% (v/v). A combined approach based on the use of the TSDC technique, able to distinguish H2O dipoles belonging to the solvation shell in terms of their order degree and mobility, and of FTIR and CD spectroscopies has allowed us to reexamine the problem of conformational stability of macromolecules as a function of their hydration.

Copyright © 2010 Hindawi Publishing Corporation. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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