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Article

Propagated Perturbations from a Peripheral Mutation Show Interactions Supporting WW Domain Thermostability.

Structure (London, England : 1993) - 6 Nov 2018

Zhang Meiling, Case David A, Peng Jeffrey W

Abstract excerpt

Inter-residue interactions stabilize protein folds and facilitate allosteric communication. Predicting which interactions are crucial and understanding why remain challenging. We highlight this through studies of a single peripheral mutation (Q33E) on the surface of the Pin1 WW domain that causes an unexpected loss of thermostability. Nuclear magnetic resonance studies attribute the loss to reorganizations of...

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Identifiers

PMID: 30197038
DOI: 10.1016/j.str.2018.07.014

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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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