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Article

In vitro folding of phage P22 coat protein with amino acid substitutions that confer in vivo temperature sensitivity.

Biochemistry - 23 May 1995

Teschke C M, King J

Abstract excerpt

The coat protein that forms the icosahedral shell of phage P22 can be efficiently refolded in vitro [Teschke, C. M., & King, J. (1993) Biochemistry 32, 10839-10847]. Temperature-sensitive mutants of coat protein interfere with folding or assembly in vivo [Gordon, C. L., & King, J. (1993) J. Biol. Chem. 268, 9358-9368]. The folding of a set of phage P22 coat proteins carrying the temperature-sensitive for folding...

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Identifiers

PMID: 7756313
DOI: 10.1021/bi00020a028

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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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In vitro folding of phage P22 coat protein with amino acid substitutions that confer in vivo temperature sensitivity.PMID 7756313Read ↗

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GroEL binds a late folding intermediate of phage P22 coat protein.Semantic proximity Read ↗

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Selective in vivo rescue by GroEL/ES of thermolabile folding intermediates to phage P22 structural proteins.Semantic proximity Read ↗

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