Transient aggregates in protein folding are easily mistaken for folding intermediates
Open Access
- 10 June 1997
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 94 (12) , 6084-6086
- https://doi.org/10.1073/pnas.94.12.6084
Abstract
It has been questioned recently whether populated intermediates are important for the protein folding process or are artefacts trapped in nonproductive pathways. We report here that the rapidly formed intermediate of the spliceosomal protein U1A is an off-pathway artefact caused by transient aggregation of denatured protein under native conditions. Transient aggregates are easily mistaken for structured monomers and could be a general problem in time-resolved folding studies.Keywords
This publication has 29 references indexed in Scilit:
- Protein Folding Intermediates: Native-State Hydrogen ExchangeScience, 1995
- Fast folding of a prototypic polypeptide: The immunoglobulin binding domain of streptococcal protein GProtein Science, 1994
- Thermodynamic and Kinetic Analysis of the SH3 Domain of Spectrin Shows a Two-State Folding TransitionBiochemistry, 1994
- 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
- Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transitionBiochemistry, 1991
- Transient folding intermediates characterized by protein engineeringNature, 1990
- INTERMEDIATES IN THE FOLDING REACTIONS OF SMALL PROTEINSAnnual Review of Biochemistry, 1990
- Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMRNature, 1988
- NMR evidence for an early framework intermediate on the folding pathway of ribonuclease ANature, 1988