Methionine oxidation of monomeric l repressor: The denatured state ensemble under nondenaturing conditions

Protein Science

Volumn 15, Issue 3, 2006, Pages 533-542

  Chugha, Preeti ^a   Sage, Harvey J ^a   Oas, Terrence G ^a,b  

^a DUKE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b DUKE UNIVERSITY MEDICAL CENTER   (United States)

Author keywords

Circular dichroism; Denatured state ensemble; Heteronuclear NMR; Hydrodynamic radius; Methionine oxidation; New methods; NMR spectroscopy; Protein structure folding; Repressor proteins

Indexed keywords

BUFFER; METHIONINE; MONOMER; REPRESSOR PROTEIN;

ARTICLE; CIRCULAR DICHROISM; CONFORMATION; DENATURATION; MOLECULAR INTERACTION; OXIDATION; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN STABILITY; SEDIMENTATION RATE; ULTRACENTRIFUGATION; ULTRAVIOLET SPECTROSCOPY;

CIRCULAR DICHROISM; DNA-BINDING PROTEINS; KINETICS; METHIONINE; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; OXIDATION-REDUCTION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; REPRESSOR PROTEINS; VIRAL PROTEINS;

EID: 33644514666     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.051856406     Document Type: Article

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