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Article

The effect of Ser 128 substitution on the structure and stability of cAMP receptor protein from Escherichia coli.

Journal of protein chemistry - 1 Apr 1998

Małecki J, Wasylewski Z

Abstract excerpt

Kinetic measurements of denaturation and renaturation of two mutants of cAMP receptor protein (CRP) at position 128, namely Ser --> Ala and Ser --> Pro, were performed in order to assess changes introduced by the mutation in the quaternary structure and protein stability. No significant changes were found in the unfolding/refolding reactions. However, small perturbations in the dissociation of CRP dimer can be...

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Identifiers

PMID: 9588945
DOI: 10.1023/a:1022528517129

Genes

CRP

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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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The effect of Ser 128 substitution on the structure and stability of cAMP receptor protein from Escherichia coli.PMID 9588945Read ↗

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Dissection of a surface-exposed portion of the cAMP-CRP complex that mediates transcription activation and repression.Semantic proximity Read ↗

Consequences of cAMP-binding site mutations on the structural stability of the type I regulatory subunit of cAMP-dependent protein kinase.Semantic proximity Read ↗

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Allosteric regulation of the cAMP receptor protein.Semantic proximity Read ↗

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