Volume and free energy of folding for troponin C C-domain: Linkage to ion binding and N-domain interaction

Biochemistry

Volumn 47, Issue 17, 2008, Pages 5047-5058

  Rocha, Cristiane Barbosa ^a   Suarez, Marisa C ^b   Yu, Aimee ^c,d   Ballard, Lance ^c,e   Sorenson, Martha M ^a   Foguel, Débora ^a   Silva, Jerson L ^a  

^a FEDERAL UNIVERSITY OF RIO DE JANEIRO   (Brazil)

^b Centro Universitario Estadual da Zona Oeste   (Brazil)

^c UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

^d MAYO CLINIC   (United States)

^e BRUKER BIOSPIN CORPORATION   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; BIOMECHANICS; FREE ENERGY; HYDROSTATIC PRESSURE; MOLECULAR INTERACTIONS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; THERMODYNAMIC STABILITY; VOLUME MEASUREMENT;

ACIDIC PROTEINS; ION BINDING; PHYSIOLOGICAL STATES; TERTIARY STRUCTURES; THERMODYNAMIC PARAMETERS;

PROTEINS;

AMINO ACID; CALCIUM; HISTIDINE; MAGNESIUM ION; MUTANT PROTEIN; PHENYLALANINE; TRYPTOPHAN; UREA; MAGNESIUM; TROPONIN C;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; BINDING SITE; ENERGY; FLUORESCENCE; HYDROSTATIC PRESSURE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN TERTIARY STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; THERMODYNAMICS; CHEMISTRY; DRUG EFFECT; METABOLISM; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;

CALCIUM; FLUORESCENCE; HYDROSTATIC PRESSURE; MAGNESIUM; MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN BINDING; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; THERMODYNAMICS; TROPONIN C; TRYPTOPHAN; UREA;

EID: 42449141471     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi702058t     Document Type: Article

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