Exploring the potential impact of an expanded genetic code on protein function

Proceedings of the National Academy of Sciences of the United States of America

Volumn 112, Issue 22, 2015, Pages 6961-6966

  Xiao, Han ^a   Nasertorabi, Fariborz ^b   Choi, Sei Hyun ^a   Han, Gye Won ^b   Reed, Sean A ^a   Stevens, Raymond C ^b   Schultz, Peter G ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

^b UNIVERSITY OF SOUTHERN CALIFORNIA   (United States)

Author keywords

Beta lactamase; Catalytic activity; Conformational effects; Evolutionary advantage; Noncanonical amino acid

Indexed keywords

4 ACRYLAMIDO PHENYLALANINE; AMINO ACID; BETA LACTAMASE TEM 1; CEFALEXIN; PHENYLALANINE DERIVATIVE; UNCLASSIFIED DRUG; BETA LACTAMASE;

ARTICLE; CATALYTIC EFFICIENCY; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYSTAL STRUCTURE; DEACYLATION; ENERGY; GENETIC CODE; MUTANT; MUTATION; PRIORITY JOURNAL; PROTEIN FUNCTION; WILD TYPE; CATALYSIS; CHEMICAL STRUCTURE; CHEMISTRY; CRYSTALLIZATION; ESCHERICHIA COLI; GENE VECTOR; GENETICS; KINETICS; METABOLISM; MOLECULAR CLONING; MOLECULAR EVOLUTION; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN CONFORMATION; X RAY DIFFRACTION;

AMINO ACIDS; BETA-LACTAMASES; CATALYSIS; CEPHALEXIN; CLONING, MOLECULAR; CRYSTALLIZATION; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ESCHERICHIA COLI; EVOLUTION, MOLECULAR; GENETIC CODE; GENETIC VECTORS; KINETICS; MODELS, MOLECULAR; MOLECULAR STRUCTURE; PROTEIN CONFORMATION; X-RAY DIFFRACTION;

EID: 84930614682     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1507741112     Document Type: Article

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