Deuteron field-cycling relaxation spectroscopy and translational water diffusion in protein hydration shells

Journal Article · Tue Mar 01 04:00:00 EST 1988 · Biophys. J.; (United States)

DOI:https://doi.org/10.1016/S0006-3495(88)83116-3· OSTI ID:7000118

Schauer, G; Kimmich, R; Nusser, W

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.

• Research Organization: Universitaet Ulm (Germany F.R.)
• OSTI ID: 7000118
• Journal Information: Biophys. J.; (United States), Journal Name: Biophys. J.; (United States) Vol. 53:3; ISSN BIOJA
• Country of Publication: United States
• Language: English

Related Subjects

550201* -- Biochemistry-- Tracer Techniques
59 BASIC BIOLOGICAL SCIENCES
ALBUMINS
ANIMALS
BIOPHYSICS
CATTLE
DEUTERIUM
DIFFUSION
DOMESTIC ANIMALS
HYDROGEN COMPOUNDS
HYDROGEN ISOTOPES
ISOTOPE APPLICATIONS
ISOTOPES
LIGHT NUCLEI
MAGNETIC RESONANCE
MAMMALS
MOLECULAR STRUCTURE
NUCLEAR MAGNETIC RESONANCE
NUCLEI
ODD-ODD NUCLEI
ORGANIC COMPOUNDS
OXYGEN COMPOUNDS
PROTEINS
RESONANCE
RUMINANTS
STABLE ISOTOPES
TRACER TECHNIQUES
VERTEBRATES
WATER