Nonprolyl cis peptide bonds in unfolded proteins cause complex folding kinetics

Nature Structural Biology

Volumn 8, Issue 5, 2001, Pages 452-458

  Pappenberger, Günter ^a,b   Aygün, Hüseyin ^c   Engels, Joachim W ^c   Reimer, Ulf ^c,d   Fischer, Gunter ^d   Kiefhaber, Thomas ^a  

^a UNIVERSITY OF BASEL   (Switzerland)

^b INSTITUTE OF CANCER RESEARCH   (United Kingdom)

^c GOETHE UNIVERSITY   (Germany)

^d MAX PLANCK RESEARCH UNIT FOR ENZYMOLOGY OF PROTEIN FOLDING   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLASE; LITHIUM CHLORIDE; PROLINE DERIVATIVE; TENDAMISTAT;

ARTICLE; CHEMICAL BOND; CHEMICAL REACTION; CIS TRANS ISOMERISM; KINETICS; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; TEMPERATURE DEPENDENCE;

ALPHA-AMYLASE; AMINO ACID SUBSTITUTION; BACTERIAL PROTEINS; ISOMERISM; KINETICS; LITHIUM CHLORIDE; MAGNETIC RESONANCE SPECTROSCOPY; PEPTIDES; PROLINE; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN RENATURATION; TEMPERATURE; THERMODYNAMICS;

EID: 0035032155     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/87624     Document Type: Article

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