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Article

Modulation of the structural integrity of helix F in apomyoglobin by single amino acid replacements.

Protein science : a publication of the Protein Society - 1 Jun 2004

Picotti Paola, Marabotti Anna, Negro Alessandro, Musi Valeria, Spolaore Barbara, Zambonin Marcello, Fontana Angelo

Abstract excerpt

The conformational features of native and mutant forms of sperm-whale apomyoglobin (apoMb) at neutral pH were probed by limited proteolysis experiments utilizing up to eight proteases of different substrate specificities. It was shown that all proteases selectively cleave apoMb at the level of chain segment 82-94 (HEAELKPLAQSHA), encompassing helix F in the X-ray structure of the holo form of the native protein;...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 15152090
DOI: 10.1110/ps.04635304
PMCID: PMC2279989

Provenance

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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