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Article

Folding and aggregation are selectively influenced by the conformational preferences of the alpha-helices of muscle acylphosphatase.

The Journal of biological chemistry - 5 Oct 2001

Taddei N, Capanni C, Chiti F, Stefani M, Dobson C M, Ramponi G

Abstract excerpt

The native state of human muscle acylphosphatase (AcP) presents two alpha-helices. In this study we have investigated folding and aggregation of a number of protein variants having mutations aimed at changing the propensity of these helical regions. Equilibrium and kinetic measurements of folding indicate that only helix-2, spanning residues 55-67, is largely stabilized in the transition state for folding...

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Identifiers

PMID: 11479314
DOI: 10.1074/jbc.M105720200

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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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