Structural uncoupling between opposing domains of oxidized calmodulin underlies the enhanced binding affinity and inhibition of the plasma membrane Ca-ATPase

Biochemistry

Volumn 44, Issue 12, 2005, Pages 4737-4747

  Chen, Baowei ^a   Mayer, M Uljana ^a   Squier, Thomas C ^a  

^a PACIFIC NORTHWEST NATIONAL LABORATORY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINETRIPHOSPHATE; AMINO ACIDS; BINDING ENERGY; BIOLOGICAL MEMBRANES; FLUORESCENCE; OXIDATION; OXYGEN; STABILIZATION;

FREQUENCY DOMAIN FLUOERSCENCE ANISOTROPY; METHIONINES OXIDATION; PROTIEN CALMODULIN (CAM); STRUCTURAL UNOUPLING;

ENZYMES;

ADENOSINE TRIPHOSPHATASE (CALCIUM); CALMODULIN; FLUORESCENT DYE; MEMBRANE ENZYME; METHIONINE;

AMINO TERMINAL SEQUENCE; ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; CELL MEMBRANE; ENZYME INHIBITION; OXIDATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN IMMOBILIZATION; PROTEIN STABILITY; PROTEIN STRUCTURE;

AMINO ACID SEQUENCE; CALCIUM-TRANSPORTING ATPASES; CALMODULIN; CELL MEMBRANE; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ELECTROPHORETIC MOBILITY SHIFT ASSAY; FLUORESCEINS; FLUORESCENCE POLARIZATION; MEMBRANE PROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; ORGANOMETALLIC COMPOUNDS; OXIDATION-REDUCTION; PEPTIDE FRAGMENTS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SOLVENTS; SPECTROMETRY, FLUORESCENCE;

EID: 15444381327     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0474113     Document Type: Article

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