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Article

Enhanced hairpin stability through loop design: the case of the protein G B1 domain hairpin.

Journal of the American Chemical Society - 16 Jun 2004

Fesinmeyer R Matthew, Hudson F Michael, Andersen Niels H

Abstract excerpt

A mutational study of the peptide corresponding to the second hairpin of the protein G B1 domain (GB1p) provided a series of mutants with significantly increased fold stability. Mutations focused on improvement of the direction-reversing loop and the addition of favorable Coulombic interactions at the sequence termini. The loop optimization was based on a database search for residues that occur with the greatest...

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Identifiers

PMID: 15186161
DOI: 10.1021/ja0379520

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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