Urea-generated free rotating water molecules are active in the protein unfolding process.

Abstract:

:The critical urea concentration (C3*) 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 C3 > or = C3* when the bulk water is practically exhausted is suggested as a main driving force of protein unfolding.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Khurgin Yu,Maksareva E

doi

10.1016/0014-5793(93)81152-p

subject

Has Abstract

pub_date

1993-01-04 00:00:00

pages

149-52

issue

2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(93)81152-P

journal_volume

315

pub_type

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