Finding the right fold
- PMID: 10542081
- DOI: 10.1038/14866
Finding the right fold
Abstract
Using mutational analysis, three groups have compared the transition states for the folding of two pairs of homologous proteins. The results of these studies suggest that protein folding mechanisms are conserved and are defined primarily by the overall topology of the native structures, as opposed to specific details of the interactions stabilizing these structures.
Comment on
-
Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding.Nat Struct Biol. 1999 Nov;6(11):1005-9. doi: 10.1038/14890. Nat Struct Biol. 1999. PMID: 10542090
-
The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved.Nat Struct Biol. 1999 Nov;6(11):1010-6. doi: 10.1038/14896. Nat Struct Biol. 1999. PMID: 10542091
-
Experiment and theory highlight role of native state topology in SH3 folding.Nat Struct Biol. 1999 Nov;6(11):1016-24. doi: 10.1038/14901. Nat Struct Biol. 1999. PMID: 10542092