Deuteron field-cycling relaxation spectroscopy and translational water diffusion in protein hydration shells.
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.
Schauer
G
G
Universität Ulm, Sektion Kernresonanzspektroskopie, Federal Republic of Germany.
Kimmich
R
R
Nusser
W
W
D055592:Biophysical Phenomena; D001703:Biophysics; D003903:Deuterium; D004058:Diffusion; D009682:Magnetic Resonance Spectroscopy; D008962:Models, Theoretical; D011487:Protein Conformation; D011506:Proteins; D012710:Serum Albumin, Bovine; D014867:Water
D011506:Proteins; D014867:Water; D012710:Serum Albumin, Bovine; D003903:Deuterium