The rate-limiting step in the folding of the cis-Pro167Thr mutant of TEM-1 β-lactamase is the trans to cis isomerization of a non-proline peptide bond

Proteins: Structure, Function and Genetics

Volumn 25, Issue 1, 1996, Pages 104-111

  Vanhove, Marc ^a   Raquet, Xavier ^a   Palzkill, Timothy ^b   Pain, Roger H ^c   Frère, Jean Marie ^a  

^a UNIVERSITY OF LIÈGE   (Belgium)

^b STANFORD UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c JO EF STEFAN INSTITUTE   (Slovenia)

Author keywords

cis non proline amino acid; cis proline mutant; cis trans isomerization; Folding unfolding kinetics; Guanidine hydrochloride denaturation; Protein folding

Indexed keywords

BETA LACTAMASE; GUANIDINE; PROLINE;

ARTICLE; ENZYME STRUCTURE; HYDROGEN BOND; ISOMERISM; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STABILITY; THERMODYNAMICS;

ANTI-BACTERIAL AGENTS; BETA-LACTAMASES; BETA-LACTAMS; ENZYME STABILITY; GUANIDINE; GUANIDINES; ISOMERISM; KINETICS; MODELS, MOLECULAR; MUTATION; PROLINE; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; SPECTROMETRY, FLUORESCENCE; THERMODYNAMICS;

EID: 0029888845     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(199605)25:1<104::AID-PROT8>3.3.CO;2-H     Document Type: Article

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