Replacing 32 proline residues by a noncanonical amino acid results in a highly active DNA polymerase

Journal of the American Chemical Society

Volumn 132, Issue 44, 2010, Pages 15708-15713

  Holzberger, Bastian ^a   Marx, Andreas ^a  

^a UNIVERSITY OF KONSTANZ   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYTIC CYCLES; COMPUTATIONAL PROTEIN DESIGN; CONFORMATIONAL STATE; DIRECTED EVOLUTION; DNA POLYMERASE; DNA SYNTHESISS; HIGH MOLECULAR WEIGHT; NATURAL AMINO ACIDS; PCR ASSAY; PRIMER EXTENSION; PROLINE RESIDUES; PROTEIN ENGINEERING; RATIONAL DESIGN; WILD-TYPE ENZYMES;

AMINO ACIDS; BIOCHEMICAL ENGINEERING; CARBOXYLIC ACIDS; DNA; ENZYMES; GENETIC ENGINEERING; LAKES; POLYMERS;

POLYMERASE CHAIN REACTION;

DNA POLYMERASE; IMINO ACID; PROLINE;

AMINO ACID SUBSTITUTION; ARTICLE; CONFORMATIONAL TRANSITION; DNA SYNTHESIS; DNA TEMPLATE; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME STABILITY; FLUORINATION; MOLECULAR WEIGHT; POLYMERASE CHAIN REACTION; THERMOSTABILITY; WILD TYPE;

AMINO ACID SEQUENCE; DNA-DIRECTED DNA POLYMERASE; MASS SPECTROMETRY; MODELS, MOLECULAR; PROLINE;

EID: 78149239484     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja106525y     Document Type: Article

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