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Article

A hierarchy of functionally important relaxations within myoglobin based on solvent effects, mutations and kinetic model.

Biochimica et biophysica acta - 1 Jun 2005

Dantsker David, Samuni Uri, Friedman Joel M, Agmon Noam

Abstract excerpt

Geminate CO rebinding in myoglobin is studied for two viscous solvents, trehalose and sol-gel (bathed in 100% glycerol) at several temperatures. Mutations in key distal hemepocket residues are used to eliminate or enhance specific relaxation modes. The time-resolved data are analyzed with a modified Agmon-Hopfield model which is capable of providing excellent fits in cases where a single relaxation mode is...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 15914102
DOI: 10.1016/j.bbapap.2005.04.002

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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