Thermostability promotes the cooperative function of split adenylate kinases

Protein Engineering, Design and Selection

Volumn 21, Issue 5, 2008, Pages 303-310

  Nguyen, Peter Q ^a   Liu, Shirley ^a   Thompson, Jeremy C ^a   Silberg, Jonathan J ^a  

^a RICE UNIVERSITY   (United States)

Author keywords

Adenylate kinase; Hyperthermophile; Protein design; Protein fragment complementation; Protein thermostability

Indexed keywords

BACTERIOLOGY;

ADENYLATE KINASE; ADENYLATE KINASES; BACILLUS SUBTILIS; FRAGMENT COMPLEMENTATION; HYPERTHERMOPHILE; MESOPHILE; NON-COVALENT INTERACTIONS; PROTEIN DESIGN; PROTEIN FRAGMENT COMPLEMENTATION; PROTEIN FRAGMENTS; PROTEIN THERMOSTABILITY;

CHLORINE COMPOUNDS;

ADENYLATE KINASE; POLYPEPTIDE; ZINC; PROTEIN;

ARTICLE; BACILLUS SUBTILIS; BACTERIAL GROWTH; CATALYSIS; CIRCULAR DICHROISM; ENZYME ACTIVITY; ENZYME STRUCTURE; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PURIFICATION; PROTEIN SECONDARY STRUCTURE; THERMOSTABILITY; THERMOTOGA NEAPOLITANA; BACTERIUM; CHEMICAL STRUCTURE; CHEMISTRY; CONFORMATION; ENZYMOLOGY; GENETIC COMPLEMENTATION; METABOLISM; METHODOLOGY; PROTEIN CONFORMATION; PROTEIN ENGINEERING; TEMPERATURE;

BACILLUS SUBTILIS; ESCHERICHIA COLI; THERMOTOGA NEAPOLITANA;

ADENYLATE KINASE; BACILLUS SUBTILIS; BACTERIA; CATALYSIS; CIRCULAR DICHROISM; ESCHERICHIA COLI; GENETIC COMPLEMENTATION TEST; MODELS, MOLECULAR; MOLECULAR CONFORMATION; PROTEIN CONFORMATION; PROTEIN ENGINEERING; PROTEIN STRUCTURE, SECONDARY; PROTEINS; TEMPERATURE; ZINC;

EID: 48849091618     PISSN: 17410126     EISSN: 17410134     Source Type: Journal    
DOI: 10.1093/protein/gzn005     Document Type: Article

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