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Article

Unfolding of bacteriophage P22 tailspike protein: enhanced thermal stability of an N-terminal fusion mutant.

FEBS letters - 7 Aug 1998

Carbonell X, Villaverde A

Abstract excerpt

The tailspike protein (TSP) of bacteriophage P22 is a homotrimeric multifunctional protein responsible for cell attachment and hydrolysis of the Salmonella typhimurium host cell receptor. Despite the folding of TSP involves the formation of thermolabile intermediates, the mature protein is extremely resistant to heat and detergent denaturation. We have analyzed the thermal resistance and unfolding pathway of two...

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Identifiers

PMID: 9720930
DOI: 10.1016/s0014-5793(98)00876-x

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SDS

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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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Unfolding of bacteriophage P22 tailspike protein: enhanced thermal stability of an N-terminal fusion mutant.PMID 9720930Read ↗

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Conformational stability of P22 tailspike proteins carrying temperature-sensitive folding mutations.Semantic proximity Read ↗

Pressure dissociation studies provide insight into oligomerization competence of temperature-sensitive folding mutants of P22 tailspike.Semantic proximity Read ↗

Side-chain specificity at three temperature-sensitive folding mutation sites of P22 tailspike protein.Semantic proximity Read ↗

Interaction of Salmonella phage P22 with its O-antigen receptor studied by X-ray crystallography.Semantic proximity Read ↗

Thermally induced structural changes of intrinsically disordered small heat shock protein Hsp22.Semantic proximity Read ↗

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