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Article

Dramatic stabilization of an SH3 domain by a single substitution: roles of the folded and unfolded states.

Journal of molecular biology - 30 Mar 2001

Mok Y K, Elisseeva E L, Davidson A R, Forman-Kay J D

Abstract excerpt

The N-terminal SH3 domain of the Drosophila drk protein (drkN SH3) exists in equilibrium between folded and unfolded states under non-denaturing buffer conditions. In order to examine the origins of this instability, we have made mutations in the domain and characterized the thermodynamics and ki...

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Identifiers

PMID: 11273710
DOI: 10.1006/jmbi.2001.4521

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-11273710-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

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Dramatic stabilization of an SH3 domain by a single substitution: roles of the folded and unfolded states.PMID 11273710Read ↗

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