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Article

Dramatic acceleration of protein folding by stabilization of a nonnative backbone conformation.

Proceedings of the National Academy of Sciences of the United States of America - 25 May 2004

Di Nardo Ariel A, Korzhnev Dmitry M, Stogios Peter J, Zarrine-Afsar Arash, Kay Lewis E, Davidson Alan R

Abstract excerpt

Through a mutagenic investigation of Gly-48, a highly conserved position in the Src homology 3 domain, we have discovered a series of amino acid substitutions that are highly destabilizing, yet dramatically accelerate protein folding, some up to 10-fold compared with the wild-type rate. The unique folding properties of these mutants allowed for accurate measurement of their folding and unfolding rates in water...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Identifiers

PMID: 15148398
DOI: 10.1073/pnas.0400550101
PMCID: PMC419538

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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