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Article

Conformational switching between protein substates studied with 2D IR vibrational echo spectroscopy and molecular dynamics simulations.

The journal of physical chemistry. B - 30 Dec 2010

Bagchi Sayan, Thorpe Dayton G, Thorpe Ian F, Voth Gregory A, Fayer M D

Abstract excerpt

Myoglobin is an important protein for the study of structure and dynamics. Three conformational substates have been identified for the carbonmonoxy form of myoglobin (MbCO). These are manifested as distinct peaks in the IR absorption spectrum of the CO stretching mode. Ultrafast 2D IR vibrational echo chemical exchange experiments are used to observed switching between two of these substates, A(1) and A(3), on a...

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Identifiers

PMID: 21128650
DOI: 10.1021/jp109203b
PMCID: PMC3033731

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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