Microscopic stability of cold shock protein a examined by NMR native state hydrogen exchange as a function of urea and trimethylamine N-oxide

Protein Science

Volumn 9, Issue 2, 2000, Pages 290-301

  Jaravine, Victor A ^a   Rathgeb Szabo, Klara ^a   Alexandrescu, Andrei T ^a,b  

^a UNIVERSITY OF BASEL   (Switzerland)

^b UNIVERSITY OF CONNECTICUT   (United States)

Author keywords

Hydrogen bonding; Hydrogen exchange; OB fold; Osmolyte; Protein folding; Protein stabilization; Sequence hydrophobicity; Two state folding approximation

Indexed keywords

COLD SHOCK PROTEIN; SOLVENT; TRIMETHYLAMINE OXIDE; UREA;

ARTICLE; CIRCULAR DICHROISM; ESCHERICHIA COLI; HYDROGEN BOND; HYDROPHOBICITY; MOLECULAR INTERACTION; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE;

BACTERIAL PROTEINS; CIRCULAR DICHROISM; DRUG STABILITY; HYDROGEN; HYDROGEN BONDING; MAGNETIC RESONANCE SPECTROSCOPY; METHYLAMINES; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN STRUCTURE, SECONDARY; THERMODYNAMICS; UREA;

ESCHERICHIA COLI;

EID: 0034003742     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.9.2.290     Document Type: Article

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