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The relationship of bound water to the IR amide I bandwidth of albumin
Author(s) -
Jakobsen R. J.,
Wasacz F. M.,
Brasch J. W.,
Smith K. B.
Publication year - 1986
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360250409
Subject(s) - chemistry , amide , albumin , adsorption , molecule , bound water , hydrogen bond , water soluble , crystallography , chromatography , organic chemistry , biochemistry
Four different types of ir experiments, involving changes in pH, changes in pressure, and the use of nonaqueous solvents, and with either albumin molecules dissolved in saline or adsorbed albumin films, support the hypothesis that the bandwidth of the amide I vibration of albumin is directly related to the amount of bound water in this protein. From the amide I band narrowing and the amide I shift to higher frequencies, it is proposed that a more ordered helix structure results as the amount of bound water is decreased.