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Article

Native protein sequences are designed to destabilize folding intermediates.

Biochemistry - 28 Feb 2006

Isogai Yasuhiro

Abstract excerpt

Hydrophobic core mutants of sperm whale apomyoglobin were constructed to investigate the amino acid sequence features that determine the folding properties. Replacements of all of the Ile residues with Leu and of all of the Ile and Val residues with Leu decreased the thermodynamic stability of the folded states against the unfolded states but increased the stability of the folding intermediates against the...

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Identifiers

PMID: 16489741
DOI: 10.1021/bi0523714

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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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