NMR hydrogen exchange of the OB-fold protein LysN as a function of denaturant: The most conserved elements of structure are the most stable to unfolding

Journal of Molecular Biology

Volumn 289, Issue 4, 1999, Pages 1041-1054

  Alexandrescu, Andrei T ^a   Jaravine, Viktor A ^a   Dames, Sonja A ^a   Lamour, François P ^a  

^a UNIVERSITY OF BASEL   (Switzerland)

Author keywords

Fold families; Lysyl tRNA synthetase; Protein folding; Structural similarity; Two state folding approximation

Indexed keywords

GUANIDINE; HYDROGEN; MUTANT PROTEIN; NUCLEIC ACID BINDING PROTEIN;

ALPHA HELIX; ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; FLUORESCENCE ANALYSIS; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STABILITY; SPECTROPHOTOMETRY;

EID: 0032981587     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2813     Document Type: Article

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