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Article

Conformational and dynamic characterization of the molten globule state of an apomyoglobin mutant with an altered folding pathway.

Biochemistry - 4 Dec 2001

Cavagnero S, Nishimura C, Schwarzinger S, Dyson H J, Wright P E

Abstract excerpt

Kinetic and equilibrium studies of apomyoglobin folding pathways and intermediates have provided important insights into the mechanism of protein folding. To investigate the role of intrinsic helical propensities in the apomyoglobin folding process, a mutant has been prepared in which Asn132 and Glu136 have been substituted with glycine to destabilize the H helix. The structure and dynamics of the equilibrium...

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PMID: 11724558
DOI: 10.1021/bi011500n

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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