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Article

Sampling unfolding intermediates in calmodulin by single-molecule spectroscopy.

Journal of the American Chemical Society - 31 Aug 2005

Slaughter Brian D, Unruh Jay R, Price E Shane, Huynh Jason L, Bieber Urbauer Ramona J, Johnson Carey K

Abstract excerpt

We used single-pair fluorescence resonance energy transfer (spFRET) measurements to characterize denatured and partially denatured states of the multidomain calcium signaling protein calmodulin (CaM) in both its apo and Ca(2+)-bound forms. The results demonstrate the existence of an unfolding intermediate. A CaM mutant (CaM-T34C-T110C) was doubly labeled with fluorescent probes AlexaFlour 488 and Texas Red at...

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Identifiers

PMID: 16117552
DOI: 10.1021/ja0526315

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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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