[Temperature relationship of the NMR 1H spectrum of hydrated collagen].
It is shown from temperature relationship analysis of spin-spin interaction constant (alpha) that at temperature below 265K the donor and acceptor adsorptive sites probability occupation in collagen surface accounts for P(S+) less than or equal to 1/10, P(S-) = 0, but at temperature 265-283K it is P(S+) less than or equal to 1/30, P(S-) = 0. If the temperature is above 283K, fine structure NMR 1H spectrum diminishes which may be explained by the clathrate--like structure collapse of protein hydrate shell.
D000818:Animals; D003094:Collagen; D006801:Humans; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D011487:Protein Conformation; D013696:Temperature
D003094:Collagen
Temperaturnaia zavisimost' spektra IaMR 1H gidratirovannogo kollagena.