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Article

Mutations improving the folding of phage P22 tailspike protein affect its receptor binding activity.

Journal of molecular biology - 29 Oct 1999

Baxa U, Steinbacher S, Weintraub A, Huber R, Seckler R

Abstract excerpt

Four previously isolated mutations in Salmonella phage P22 tailspike protein were used to study the relationship between protein stability, folding, and function. Tailspike protein binds and hydrolyzes the repetitive O-antigen structure in Salmonella lipopolysaccharide. Four mutations (V331G, V331A, A334V, A334I) are known to increase the folding efficiency, and two of them (at position 331) also increase the...

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Identifiers

PMID: 10543960
DOI: 10.1006/jmbi.1999.3165

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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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