Phenylalanine fluorescence studies of calcium binding to N-domain fragments ofParameciumcalmodulin mutants show increased calcium affinity correlates with increased disorder
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چکیده
منابع مشابه
Calcium binding to calmodulin mutants monitored by domain-specific intrinsic phenylalanine and tyrosine fluorescence.
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(...
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ژورنال
عنوان ژورنال: Protein Science
سال: 2001
ISSN: 0961-8368,1469-896X
DOI: 10.1110/ps.11601