Nuclear magnetic resonance spectroscopy with the stringent substrate rhodanese bound to the single-ring variant SR1 of the E. coli chaperonin GroEL

Protein Science

Volumn 20, Issue 8, 2011, Pages 1380-1386

  Koculi, Eda ^a   Horst, Reto ^a   Horwich, Arthur L ^a,b   Wüthrich, Kurt ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

^b YALE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Coherence transfer; CRINEPT; Protein folding; Substrate protein chaperonin crosslinking; TROSY

Indexed keywords

CHAPERONIN; PROTEIN SR 1; THIOSULFATE SULFURTRANSFERASE; UNCLASSIFIED DRUG;

ARTICLE; ESCHERICHIA COLI; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; POLARIZATION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN STRUCTURE; PROTEIN VARIANT; SPECTROSCOPY; TRANSVERSE RELAXATION OPTIMIZED SPECTROSCOPY;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CHAPERONIN 60; ESCHERICHIA COLI; HUMANS; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN FOLDING; THIOSULFATE SULFURTRANSFERASE;

EID: 79960684196     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.665     Document Type: Article

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