Molecular dynamics of calmodulin as monitored by fluorescence anisotropy
Copyright policy )Molecular dynamics of calmodulin as monitored by fluorescence anisotropy
Abstract Static and dynamic measurements of fluorescence anisotropy have been made for calmodulin, employing both the intrinsic fluorescence of Tyr-99 and Tyr-138 and the fluorescence of dansyl and fluorescein groups attached to Tyr-99, as well as AEDANS groups attached to methionines. All approaches indicate the presence of a significant internal mobility involving the probe for calmodulin in the absence of Ca2+. This is diminished in the presence of Ca2+. 2
- University of Maryland, Baltimore United States
- University System of Maryland at Hagerstown United States
- University of Maryland, Baltimore County United States
Male, Binding Sites, Protein Conformation, Viscosity, Calcium-Binding Proteins, Fluorescence Polarization, Kinetics, Calmodulin, Testis, Animals, Tyrosine, Calcium, Cattle, Egtazic Acid, Fluorescent Dyes, Protein Binding
Male, Binding Sites, Protein Conformation, Viscosity, Calcium-Binding Proteins, Fluorescence Polarization, Kinetics, Calmodulin, Testis, Animals, Tyrosine, Calcium, Cattle, Egtazic Acid, Fluorescent Dyes, Protein Binding
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