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Article

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

Biophysical chemistry - 1 May 2009

Reich Lothar, Becker Marion, Seckler Robert, Weikl Thomas R

Abstract excerpt

Parallel beta-helices are among the simplest repetitive structural elements in proteins. The folding behavior of beta-helix proteins has been studied intensively, also to gain insight on the formation of amyloid fibrils, which share the parallel beta-helix as a central structural motif. An important system for investigating beta-helix folding is the tailspike protein from the Salmonella bacteriophage P22. The...

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Identifiers

PMID: 19254821
DOI: 10.1016/j.bpc.2009.01.015

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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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Invivo folding efficiencies for mutants of the P22 tailspike beta-helix protein correlate with predicted stability changes.PMID 19254821Read ↗

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