Accumulation of partly folded in the equilibrium unfolding of the pneumococcal choline-binding module C-LytA

Biochemical Journal

Volumn 387, Issue 2, 2005, Pages 479-488

  Maestro, Beatriz ^a   Sanz, Jesús M ^a  

^a MIGUEL HERNÁNDEZ UNIVERSITY   (Spain)

Author keywords

Solenoid; Affinity tag; C LytA; Choline binding module; Partly folded state; Protein folding

Indexed keywords

CELL MEMBRANES; CHEMICAL BONDS; CHLORINE COMPOUNDS; DIMERIZATION; FLUORESCENCE; FREE ENERGY; MICROORGANISMS; THERMAL EFFECTS;

CHOLINES; DENATURATION; THERMAL EQUILIBRIUM; VIRULENCE FACTORS;

PROTEINS;

BACTERIAL PROTEIN; CHOLINE; GUANIDINE; PROTEIN C LYTA; UNCLASSIFIED DRUG;

ARTICLE; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; DENATURATION; FLUORESCENCE; GEL FILTRATION CHROMATOGRAPHY; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN LIPID INTERACTION; PROTEIN STABILITY; PROTEIN TERTIARY STRUCTURE; STREPTOCOCCUS PNEUMONIAE;

CHOLINE; ENZYME STABILITY; MODELS, MOLECULAR; N-ACETYLMURAMOYL-L-ALANINE AMIDASE; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; STREPTOCOCCUS PNEUMONIAE; THERMODYNAMICS;

EID: 17644413572     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20041194     Document Type: Article

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