Phosphorylation of serine residues affects the conformation of the calmodulin binding domain of human protein 4.1

European Journal of Biochemistry

Volumn 268, Issue 15, 2001, Pages 4292-4299

  Vetter, Stefan W ^a,b   Leclerc, Estelle ^a  

^a ETH ZURICH   (Switzerland)

^b SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

Calmodulin binding domain; Peptide conformation; Protein p4.1; Serine phosphorylation

Indexed keywords

CALMODULIN; ERYTHROCYTE BAND 4.1 PROTEIN; LEUCINE; PEPTIDE; PHENYLALANINE; PHOSPHATE; SERINE;

ANALYTIC METHOD; ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; FLUORESCENCE SPECTROSCOPY; HUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN PHOSPHORYLATION;

ARGININE; BINDING SITES; CALMODULIN; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CIRCULAR DICHROISM; CYTOSKELETAL PROTEINS; HUMANS; MEMBRANE PROTEINS; MODELS, MOLECULAR; MODELS, THEORETICAL; NEUROPEPTIDES; PEPTIDE BIOSYNTHESIS; PEPTIDES; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN ISOFORMS; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SERINE; SPECTROMETRY, FLUORESCENCE;

EID: 0034833014     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.2001.02347.x     Document Type: Article

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