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of 8
pro vyhledávání: '"Ashley B. Daugherty"'
Autor:
Fei Chen, Yuan Zhang, Ashley B Daugherty, Zunyi Yang, Ryan Shaw, Mengxing Dong, Stefan Lutz, Steven A Benner
Publikováno v:
PLoS ONE, Vol 12, Iss 3, p e0174163 (2017)
One research goal for unnatural base pair (UBP) is to replicate, transcribe and translate them in vivo. Accordingly, the corresponding unnatural nucleoside triphosphates must be available at sufficient concentrations within the cell. To achieve this
Externí odkaz:
https://doaj.org/article/fe74bec01f5a4997b06753a97f93b3a1
Publikováno v:
ACS Catalysis
Circular permutation of the NADPH-dependent oxidoreductase Old Yellow Enzyme from Saccharomyces pastorianus (OYE1) can significantly enhance the enzyme’s catalytic performance. Termini relocation into four regions of the protein (sectors I–IV) ne
Autor:
Fei Chen, Myong-Jung Kim, Myong-Sang Kim, Jennifer D. Moses, Mariko F. Matsuura, Ashley B. Daugherty, Patricia Moussatche, Steven A. Benner, Stefan Lutz, Ryan W. Shaw, Christian B. Winiger
Publikováno v:
ACS Synthetic Biology
Deoxynucleoside kinase from D. melanogaster (DmdNK) has broad specificity; although it catalyzes the phosphorylation of natural pyrimidine more efficiently than natural purine nucleosides, it accepts all four 2'-deoxynucleosides and many analogues, u
Autor:
Ashley B. Daugherty, Yuan Zhang, Fei Chen, Mengxing Dong, Steven A. Benner, Ryan Shaw, Zunyi Yang, Stefan Lutz
Publikováno v:
PLoS ONE
PLoS ONE, Vol 12, Iss 3, p e0174163 (2017)
PLoS ONE, Vol 12, Iss 3, p e0174163 (2017)
One research goal for unnatural base pair (UBP) is to replicate, transcribe and translate them in vivo. Accordingly, the corresponding unnatural nucleoside triphosphates must be available at sufficient concentrations within the cell. To achieve this
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 1179
Protein engineering by random circular permutation is an effective tool for tailoring protein topology with potential functional benefits including improved catalytic activity. This method involves covalently connecting the native protein termini wit
Publikováno v:
Methods in Molecular Biology ISBN: 9781493910526
Protein engineering by random circular permutation is an effective tool for tailoring protein topology with potential functional benefits including improved catalytic activity. This method involves covalently connecting the native protein termini wit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e502e6b745b3b5452daca7e62a777e64
https://doi.org/10.1007/978-1-4939-1053-3_17
https://doi.org/10.1007/978-1-4939-1053-3_17
Publikováno v:
Journal of the American Chemical Society. 135(38)
Members of the old yellow enzyme (OYE) family are widely used, effective biocatalysts for the stereoselective trans-hydrogenation of activated alkenes. To further expand their substrate scope and improve catalytic performance, we have applied a prote
Publikováno v:
Biochemistry. 51(41)
The propeptide domain of subtilisin BPN' functions as a molecular chaperone for its cognate protease yet quickly assumes a predominantly unfolded structure following cleavage by the mature protease. In contrast, structural stabilization of the propep