Elimination of a Cis-proline-containing loop and turn optimization stabilizes a protein and accelerates its folding

Journal of Molecular Biology

Volumn 399, Issue 2, 2010, Pages 331-346

  Jakob, Roman P ^a   Zierer, Bettina K ^a   Weininger, Ulrich ^b   Hofmann, Stefanie D ^a   Lorenz, Stefan H ^a   Balbach, Jochen ^b   Dobbek, Holger ^a   Schmid, Franz X ^a  

^a UNIVERSITY OF BAYREUTH   (Germany)

^b MARTIN LUTHER UNIVERSITY HALLE WITTENBERG   (Germany)

Author keywords

Folding mechanism; Folding transition state; Protein consensus design; Protein engineering; turn

Indexed keywords

ASPARTIC ACID; MONOMER; PROLINE;

ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; GENETIC HETEROGENEITY; GENETIC VARIABILITY; IN VITRO STUDY; KINETICS; PHASE TRANSITION; PRIORITY JOURNAL; PROCESS OPTIMIZATION; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STABILITY; SEQUENCE ANALYSIS;

ENTEROBACTERIA PHAGE FD;

EID: 77953083362     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.04.007     Document Type: Article

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