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Article

Conformational stability of P22 tailspike proteins carrying temperature-sensitive folding mutations.

Biochemistry - 1 May 1990

Thomas G J, Becka R, Sargent D, Yu M H, King J

Abstract excerpt

The thermostable tailspike endorhamnosidase of Salmonella phage P22 provides a model system for comparing the role of amino acid sequences in determining the intracellular folding pathway with their role in stabilizing the mature structural protein. Complete Raman band assignments are given here for the native form of the tailspike trimer in aqueous solution. Once correctly folded and assembled, the wild-type and...

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Identifiers

PMID: 2141794
DOI: 10.1021/bi00469a022

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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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Conformational stability of P22 tailspike proteins carrying temperature-sensitive folding mutations.PMID 2141794Read ↗

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Mutations improving the folding of phage P22 tailspike protein affect its receptor binding activity.Semantic proximity Read ↗

P22 tailspike folding mutants revisited: effects on the thermodynamic stability of the isolated beta-helix domain.Semantic proximity Read ↗

Folding and assembly of phage P22 tailspike endorhamnosidase lacking the N-terminal, head-binding domain.Semantic proximity Read ↗

Stability of wild-type and temperature-sensitive protein subunits of the phage P22 capsid.Semantic proximity Read ↗

Distinct cysteine sulfhydryl environments detected by analysis of Raman S-hh markers of Cys-->Ser mutant proteins.Semantic proximity Read ↗

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

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

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

Buried hydrophobic side-chains essential for the folding of the parallel beta-helix domains of the P22 tailspike.Semantic proximity Read ↗

Isolation of suppressors of temperature-sensitive folding mutations.Semantic proximity Read ↗

Invivo folding efficiencies for mutants of the P22 tailspike beta-helix protein correlate with predicted stability changes.Semantic proximity Read ↗

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