Heat and cold denatured states of monomeric λ represser are thermodynamically and conformationally equivalen

Biochemistry

Volumn 35, Issue 20, 1996, Pages

  Huang, Guewha S ^a,c   Oas, Terrence G ^a,b  

^a DUKE UNIVERSITY MEDICAL CENTER   (United States)

^b Box 3711 ^*

^c INSTITUTE OF BIOMEDICAL SCIENCES   (Taiwan)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO TERMINAL SEQUENCE; ARTICLE; DENATURATION; NUCLEAR MAGNETIC RESONANCE; NUCLEAR OVERHAUSER EFFECT; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; SPECTROSCOPY; THERMAL CONDUCTIVITY; THERMODYNAMICS;

CIRCULAR DICHROISM; COLD; DNA-BINDING PROTEINS; HEAT; KINETICS; MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; RECOMBINANT PROTEINS; REPRESSOR PROTEINS; THERMODYNAMICS; UREA; VIRAL PROTEINS;

EID: 0029934661     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

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