Important role of hydrogen bonds in the structurally polarized transition state for folding of the src SH3 domain.

doi:10.1038/1412

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Article

Important role of hydrogen bonds in the structurally polarized transition state for folding of the src SH3 domain.

Nature structural biology - 1 Aug 1998

Grantcharova V P, Riddle D S, Santiago J V, Baker D

Abstract excerpt

Experimental and theoretical studies on the folding of small proteins such as the chymotrypsin inhibitor 2 (CI-2) and the P22 Arc repressor suggest that the folding transition state is an expanded version of the native state with most interactions partially formed. Here we report that this pictur...

Topics

Flow Injection Analysis
Guanidine
Hydrogen Bonding
Models, Molecular
Mutagenesis, Site-Directed
Mutation
Protein Denaturation
Protein Folding
Protein Structure, Secondary
Proto-Oncogene Proteins pp60(c-src)
src Homology Domains

Source

Open in PubMed

Identifiers

PMID: 9699636
DOI: 10.1038/1412

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-9699636-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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