Intrinsic fluorescence as a probe of structure-function relationships in Ca(2+)-transport ATPases.
Applications of intrinsic fluorescence measurements in the study of Ca(2+)-transport ATPases are reviewed. Since the initial reports showing that the fluorescence emission was sensitive to Ca2+ binding, a substantial amount of work has focused on the use of both steady-state and time-resolved fluorescence spectroscopy to investigate structure-function relationships in sarcoplasmic reticulum and plasma membrane Ca(2+)-ATPases. These studies have revealed ligand-induced conformational changes, as well as provided information on protein-protein, protein-solvent and/or protein-lipid interactions in different functional states of these proteins. The main results of these studies, as well as possible future prospects are discussed.
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Departamento de Bioquímica Médica, Universidade Federal do Rio de Janeiro, Brazil.
Coelho-Sampaio
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D000818:Animals; D000252:Calcium-Transporting ATPases / Q000737:chemistry*; D005453:Fluorescence; D006801:Humans; D008024:Ligands; D011487:Protein Conformation; D013329:Structure-Activity Relationship
D008024:Ligands; D000252:Calcium-Transporting ATPases