WW: An isolated three-stranded antiparallel β-sheet domain that unfolds and refolds reversibly; evidence for a structured hydrophobic cluster in urea and GdnHCl and a disordered thermal unfolded state

Protein Science

Volumn 8, Issue 4, 1999, Pages 841-853

  Koepf, Edward K ^a   Petrassi, H Michael ^a   Sudol, Marius ^b   Kelly, Jeffery W ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

^b MOUNT SINAI SCHOOL OF MEDICINE   (United States)

Author keywords

Hydrophobic cluster; Reversible folding; WW; sheet folding

Indexed keywords

GUANIDINE; UREA;

ARTICLE; DISSOCIATION CONSTANT; ENZYME RECONSTITUTION; HYDROPHOBICITY; LIGAND BINDING; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DENATURATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN STABILITY; PROTON NUCLEAR MAGNETIC RESONANCE; STRUCTURE ANALYSIS; THERMOSTABILITY; ULTRACENTRIFUGATION;

EID: 0032939806     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.8.4.841     Document Type: Article

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