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Article

Analysis of the factors that stabilize a designed two-stranded antiparallel beta-sheet.

Protein science : a publication of the Protein Society - 1 Jun 2002

Espinosa Juan F, Syud Faisal A, Gellman Samuel H

Abstract excerpt

Autonomously folding beta-hairpins (two-strand antiparallel beta-sheets) have become increasingly valuable tools for probing the forces that control peptide and protein conformational preferences. We examine the effects of variations in sequence and solvent on the stability of a previously designed 12-residue peptide (1). This peptide adopts a beta-hairpin conformation containing a two-residue loop (D-Pro-Gly)...

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Identifiers

PMID: 12021448
DOI: 10.1110/ps.4140102
PMCID: PMC2373626

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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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