학술논문
Interaction between two discontiguous chain segments from the beta-sheet of Esherichia coli thioredoxin suggests an initiation site for folding
Document Type
Statistical Data Included
Source
Biochemistry. Sept 5, 2000, Vol. 39 Issue 35, p10613, 6 p.
Subject
Language
ISSN
0006-2960
Abstract
Folding of oxidized Escherichia coli thioredoxin (Trx) and folding and binding of its complementary fragments have been studied. Results of studying the isolated and recombined fragments by size-exclusion chromatography, far-UV CD and (super.1)H-(super.15)N NMR spectroscopy. Studies indicate Trx folding begins with zipping together two discontiguous chain segments that correspond to two adjacent strands of the native beta-sheet. The chain segments are rather hydrophobic.