The barriers in protein folding
- 1 March 1994
- journal article
- research article
- Published by Springer Nature in Nature Structural & Molecular Biology
- Vol. 1 (3) , 149-156
- https://doi.org/10.1038/nsb0394-149
Abstract
Elimination of an interaction which forms in denatured cytochrome c enables the majority of the molecules to fold to the native state on a 15 ms time scale, without populating observable intermediates. These results are contrary to the current view that particular steps in protein folding, including the supposedly rate–limiting molten globule to native transition, are intrinsically slow. Instead it appears that intermediates characterized so far may be kinetically trapped by barriers that are optional rather than integral to the folding process. Major barriers may result from misorganization of the chain in the initial condensation step.Keywords
This publication has 52 references indexed in Scilit:
- PATHWAYS OF PROTEIN FOLDINGAnnual Review of Biochemistry, 1993
- Pulsed H/D-exchange studies of folding intermediatesCurrent Opinion in Structural Biology, 1993
- The Protein Folding ProblemPhysics Today, 1993
- Kinetic analysis of folding and unfolding the 56 amino acid IgG-binding domain of streptococcal protein GBiochemistry, 1992
- The folding of hen lysozyme involves partially structured intermediates and multiple pathwaysNature, 1992
- Early hydrogen-bonding events in the folding reaction of ubiquitin.Proceedings of the National Academy of Sciences, 1992
- Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transitionBiochemistry, 1991
- Early folding intermediate of ribonuclease A.Proceedings of the National Academy of Sciences, 1990
- Intermediates In The Folding Reactions Of Small ProteinsAnnual Review of Biochemistry, 1990
- The molten globule state as a clue for understanding the folding and cooperativity of globular‐protein structureProteins-Structure Function and Bioinformatics, 1989