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Urea‐generated free rotating water molecules are active in the protein unfolding process
Author(s) -
Khurgin Yu.,
Maksareva E.
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)81152-p
Subject(s) - urea , chemistry , aqueous solution , chymotrypsinogen , molecule , chromatography , spectroscopy , bovine serum albumin , biophysics , crystallography , analytical chemistry (journal) , biochemistry , organic chemistry , trypsin , biology , physics , quantum mechanics , chymotrypsin , enzyme
The critical urea concentration (C 3 ∗ ) which destabilizes the structure of bovine serum albumin and chymotrypsinogen was determined by UV difference spectroscopy. The increase of the relative content of mobile rotating water molecules in aqueous urea was formerly shown by millimeter spectroscopy [1]. The rise of rotator content at a urea concentration C 3 ⩾ C 3 ∗ when the bulk water is practically exhausted is suggested as a main driving force of protein unfolding.