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Article

A tale of two secondary structure elements: when a beta-hairpin becomes an alpha-helix.

Journal of molecular biology - 17 Sept 1999

Cregut D, Civera C, Macias M J, Wallon G, Serrano L

Abstract excerpt

In this work, we have analyzed the relative importance of secondary versus tertiary interactions in stabilizing and guiding protein folding. For this purpose, we have designed four different mutants to replace the alpha-helix of the GB1 domain by a sequence with strong beta-hairpin propensity in isolation. In particular, we have chosen the sequence of the second beta-hairpin of the GB1 domain, which populates the...

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Identifiers

PMID: 10493883
DOI: 10.1006/jmbi.1999.2966

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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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