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Article

Calcium binding to calmodulin mutants monitored by domain-specific intrinsic phenylalanine and tyrosine fluorescence.

Biophysical journal - 1 Nov 2002

VanScyoc Wendy S, Sorensen Brenda R, Rusinova Elena, Laws William R, Ross J B Alexander, Shea Madeline A

Abstract excerpt

Cooperative calcium binding to the two homologous domains of calmodulin (CaM) induces conformational changes that regulate its association with and activation of numerous cellular target proteins. Calcium binding to the pair of high-affinity sites (III and IV in the C-domain) can be monitored by observing calcium-dependent changes in intrinsic tyrosine fluorescence intensity (lambda(ex)/lambda(em) of 277/320 nm)....

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Identifiers

PMID: 12414709
DOI: 10.1016/S0006-3495(02)75286-7
PMCID: PMC1302361

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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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