Deuteron Field-cycling Relaxation Spectroscopy and Translational Water Diffusion in Protein Hydration Shells

Overview

Journal Biophys J

Publisher Cell Press

Specialty Biophysics

Date 1988 Mar 1

PMID 3349132

Citations 7

Authors

G Schauer

R Kimmich

W NUSSER

Affiliations

Soon will be listed here.

Abstract

The deuterated hydration shells of bovine serum (BSA) albumin, and purple membrane sheets have been studied by the aid of deuteron field-cycling relaxation spectroscopy. The deuteron Larmor frequency range was 10(3) to 10(8) Hz. The temperature and the water content has been varied. The data distinguish translational diffusion on the protein surface from macromolecular tumbling or exchange with free water. A theory well describing all dependences has been developed on this basis. All parameters have successfully been tested concerning consistency with other sources of information. The concept is considered as a major relaxation scheme determining, apart from cross-relaxation effects, the water proton relaxation in tissue.

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