학술논문
Partitioning the effects of changes in a protein to the folded or unfolded forms by using a thermodynamic cycle: a change in Escherichia coli thioredoxin does not affect the unfolded state
Document Type
Academic Journal
Author
Source
Biochemistry. Nov 30, 1993, Vol. 32 Issue 47, p12922, 6 p.
Subject
Language
ISSN
0006-2960
Abstract
Modification of a cysteine residue after denaturant-induced unfolding by a protein produces new disulfide side chains in the protein. Urea concentration is used for standardizing the disulfide equilibrium exchange constants. Thermodynamic link exists between the disulfide exchange reaction and the stability of the proteins. Folded proteins favor the disulfide exchange reaction.