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Observation of unfreezable water in aqueous solution of globule protein by microwave dielectric measurement
Author(s) -
Miura Nobuhiro,
Hayashi Yoshihito,
Shinyashiki Naoki,
Mashimo Satoru
Publication year - 1995
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.360360103
Subject(s) - chemistry , aqueous solution , bound water , dielectric , molecule , differential scanning calorimetry , relaxation (psychology) , microwave , solvation shell , analytical chemistry (journal) , crystallography , chromatography , thermodynamics , organic chemistry , materials science , solvation , psychology , social psychology , physics , optoelectronics , quantum mechanics
A freezing process analyzed by the dielectric method on aqueous solution of albumin has revealed water structure around protein molecule. A relaxation peak due to bound water attached on the protein surface around 100 MHz at room temperature was found. It could be seen commonly in globule proteins. Another peak due to a different kind of unfreezable water was found around 1 GHz at −6°C. The amount of this water is estimated as 0.36 g water/g protein and in good agreement with that obtained by differential scanning calorimetry and nmr measurements. The water molecules form a shell layer around the protein molecule. © 1995 John Wiley & Sons, Inc.