Thermodynamic characterization of the osmolyte- and ligand-folded states of Bacillus subtilis ribonuclease P protein

Biochemistry

Volumn 44, Issue 39, 2005, Pages 13014-13026

  Henkels, Christopher H ^a   Oas, Terrence G ^a  

^a DUKE UNIVERSITY MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

NEGATIVE IONS; PH EFFECTS; PROTEINS; THERMODYNAMICS;

DISSOCIATION CONSTANTS; NONCATALYTIC COMPONENTS;

BIOCHEMISTRY;

LIGAND; RIBONUCLEASE P; SULFATE; TRIMETHYLAMINE OXIDE;

ARTICLE; BACILLUS SUBTILIS; CIRCULAR DICHROISM; DISSOCIATION CONSTANT; ENERGY; ENZYME ACTIVITY; ENZYME BINDING; ENZYME CONFORMATION; ENZYME DENATURATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; SOLVATION; STOICHIOMETRY; THERMODYNAMICS;

BACILLUS SUBTILIS; CIRCULAR DICHROISM; HEAT; LIGANDS; METHYLAMINES; OSMOLAR CONCENTRATION; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; RIBONUCLEASE P; SULFATES; THERMODYNAMICS;

BACILLUS SUBTILIS;

EID: 25444472330     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0504613     Document Type: Article

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