15N NMR relaxation studies of calcium-loaded parvalbumin show tight dynamics compared to those of other EF-hand proteins

Biochemistry

Volumn 37, Issue 28, 1998, Pages 9964-9975

  Baldellon, Christophe ^a   Alattia, Jean René ^b   Strub, Marie Paule ^a   Pauls, Thomas ^c   Berchtold, Martin W ^d   Cavé, Adrien ^a   Padilla, André ^a  

^a CNRS   (France)

^b UNIVERSITY OF TORONTO   (Canada)

^c UNIVERSITY OF FRIBOURG   (Switzerland)

^d UNIVERSITY OF COPENHAGEN   (Denmark)

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM BINDING PROTEIN; HELIX LOOP HELIX PROTEIN; PARVALBUMIN; AMIDE; NITROGEN; PROTON;

AMINO TERMINAL SEQUENCE; ARTICLE; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; MOLECULAR MODEL; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN TERTIARY STRUCTURE; STRUCTURE ACTIVITY RELATION; ANIMAL; CHEMICAL STRUCTURE; CHEMISTRY; COMPARATIVE STUDY; METABOLISM; NUCLEAR MAGNETIC RESONANCE; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; RAT; THERMODYNAMICS;

AMIDES; ANIMALS; CALCIUM-BINDING PROTEINS; MODELS, MOLECULAR; NITROGEN ISOTOPES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PARVALBUMINS; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTONS; RATS; THERMODYNAMICS;

EID: 0032516410     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi980334p     Document Type: Article

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