Effects of thermal denaturation on the longitudinal relaxation time (T1) of water protons in protein solutions: study of the factors determining the T1 of water protons.
The factors determining the longitudinal relaxation time (T1) of water protons in protein solutions were investigated by analyzing the effects of thermal denaturation on the T1 of the water protons. We treated the water protons and the protein protons "on a protein surface" as a dipole-dipole coupled two-spin system where relative translational diffusion is the dominant mechanism, and measured the change in the time development of the nuclear Overhauser effect (NOE) factors of the water protons. The T1 of the water protons was shortened markedly when the proteins were thermally denatured. Our analysis indicates that this relaxation enhancement is due to an increase in the value of the translational correlation time as well as the fraction of hydration water molecules, though the influence of "proton exchange" between the water protons and the labile protein protons cannot be completely neglected.
Aso
M
M
Department of Radiology, Saiseikai Takaoka Hospital, Takaoka City, Japan.
Yui
Y
Y
Kakishita
M
M
D000818:Animals; D006358:Hot Temperature; D006801:Humans; D008279:Magnetic Resonance Imaging; D011489:Protein Denaturation; D012710:Serum Albumin, Bovine; D014867:Water
D014867:Water; D012710:Serum Albumin, Bovine