Infrared Spectroscopic Studies of Major Cellular Components. Part I: The Effect of Hydration on the Spectra of Proteins

Author:

Pevsner Alex1,Diem Max1

Affiliation:

1. Departments of Chemistry and Biochemistry, City University of New York, The Graduate Center, 365 Fifth Avenue, New York, New York 10016-4309 (A.P.); and Department of Chemistry and Biochemistry, City University of New York, Hunter College, 695 Park Avenue, New York, New York 10021 (M.D.)

Abstract

The infrared absorption spectra of two sample proteins as dry, lyophilized powders in KBr pellets, as hydrated proteins in KBr pellets, as hydrated or dehydrated films, and in solution phase are reported. We find an enormous increase in the absorption intensities of the amide I and amide II vibrations between the dry and the hydrated phases. This intensity enhancement was observed for hydration by both H2O and D2O. Furthermore, we observe significant changes in the amide I/amide II intensity ratios when comparing solution spectra acquired in transmission and attenuated total reflection (ATR) modes. Observed intensity changes between dry and hydrated protein samples were interpreted in terms of variations in the dielectric constant of the immediate surroundings of the peptide linkages.

Publisher

SAGE Publications

Subject

Spectroscopy,Instrumentation

Reference16 articles.

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