학술논문
Development of nonpolar surfaces in the folding of Escherichia coli dihydrofolate reductase detected by 1-anilinonaphthalene-8-sulfonate binding
Document Type
Academic Journal
Source
Biochemistry. Dec 27, 1994, Vol. 33 Issue 51, p15250, 9 p.
Subject
Language
ISSN
0006-2960
Abstract
Stopped-flow refolding methods analyzing the folding process and binding of 1-anilinonaphthalene-8-sulfonate (ANS) during folding of Escherichia coli dihydrofolate reductase indicate the presence of hydrophobic surfaces in the folding intermediate, followed by formation of intermediates with increase in intensity of fluorescence of ANS. Several ANS binding sites and subdomains arise during rate-limiting steps, which are then transformed to the final conformation. The similarity in kinetics of ANS binding for various proteins indicate a single mechanism for folding reactions.