Native conformational tendencies in unfolded polypeptides: development of a novel method to assess native conformational tendencies in the reduced forms of multiple disulfide-bonded proteins
Details
Serval ID
serval:BIB_5EFA560264C6
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Native conformational tendencies in unfolded polypeptides: development of a novel method to assess native conformational tendencies in the reduced forms of multiple disulfide-bonded proteins
Journal
Journal of the American Chemical Society
ISSN
0002-7863 (Print)
Publication state
Published
Issued date
02/2003
Volume
125
Number
8
Pages
2036-7
Notes
Journal Article
Research Support, U.S. Gov't, P.H.S. --- Old month value: Feb 26
Research Support, U.S. Gov't, P.H.S. --- Old month value: Feb 26
Abstract
Oxidative folding is the concomitant formation of the native disulfide bonds and the native tertiary structure from the reduced and unfolded polypeptide. Of interest is the inherent conformational tendency (bias) present in the reduced polypeptide to dictate the formation of the full set of native disulfide bonds. Here, by application of a novel tool, we have been able to assess this "native conformational tendency" present in reduced and unfolded bovine pancreatic ribonuclease A (RNase A). The essence of this method lies in the ability of the oxidant [Pt(en)(2)Cl(2)](2+) (where "en" is ethylenediamine) to oxidize disulfide bonds under conditions in which both reduction and disulfide reshuffling, which are essential for rearranging non-native disulfide bonds, are extremely slow. When applied to RNase A, the method revealed little or no bias toward formation of the full native set of disulfide bonds in the fully reduced protein.
Keywords
Animals
Cattle
Disulfides/*chemistry
Ethyl Methanesulfonate/*analogs & derivatives/chemistry
Hydrogen-Ion Concentration
Oxidation-Reduction
Protein Conformation
Protein Folding
Ribonuclease, Pancreatic/*chemistry
Pubmed
Web of science
Create date
24/01/2008 14:40
Last modification date
20/08/2019 14:16