SCOPUS 정보 검색 플랫폼

Volumn 12, Issue 10, 2011, Pages 1559-1573

Fine Tuning of a Biological Machine: DnaK Gains Improved Chaperone Activity by Altered Allosteric Communication and Substrate Binding

(5) Schweizer, Regina S a Aponte, Raphael A a,b Zimmermann, Sabine a Weber, Annika a Reinstein, Jochen a

a MAX PLANCK INSTITUTE FOR MEDICAL RESEARCH (Germany)

b BASF SE (Germany)

Author keywords

Chaperones; Directed evolution; Protein engineering; Protein folding; Transient kinetics

Indexed keywords

ADENOSINE TRIPHOSPHATE; ALANINE; FIREFLY LUCIFERASE; GLYCINE; MUTANT PROTEIN; PROTEIN DNAK;

ALLOSTERISM; AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; BIOCHEMISTRY; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; DISSOCIATION CONSTANT; ENZYME ACTIVITY; ENZYME BINDING; ENZYME SUBSTRATE COMPLEX; HINGE REGION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN DETERMINATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN MOTIF; PROTEIN SECRETION; PROTEIN VARIANT; WILD TYPE;

ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; AMINO ACID SUBSTITUTION; ANIMALS; DIRECTED MOLECULAR EVOLUTION; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; FIREFLIES; HSP70 HEAT-SHOCK PROTEINS; LUCIFERASES, FIREFLY; MODELS, MOLECULAR; MUTATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN REFOLDING;

EID: 79959685900 PISSN: 14394227 EISSN: 14397633 Source Type: Journal
DOI: 10.1002/cbic.201000786 Document Type: Article

Times cited : (13)

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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.