Zobrazeno 1 - 2
of 2
pro vyhledávání: '"Linda K.M. Meekels"'
Autor:
Ana Toplak, Eduardo F. Teixeira de Oliveira, Marcel Schmidt, Henriëtte J. Rozeboom, Hein J. Wijma, Linda K.M. Meekels, Rowin de Visser, Dick B. Janssen, Timo Nuijens
Publikováno v:
Computational and Structural Biotechnology Journal, Vol 19, Iss , Pp 1277-1287 (2021)
Omniligase-1 is a broadly applicable enzyme for peptide bond formation between an activated acyl donor peptide and a non-protected acyl acceptor peptide. The enzyme is derived from an earlier subtilisin variant called peptiligase by several rounds of
Externí odkaz:
https://doaj.org/article/6a85ba9608194f52a918b9a4228a5b84
Autor:
Hein J. Wijma, Ana Toplak, Timo Nuijens, Rowin de Visser, Dick B. Janssen, Henriëtte J. Rozeboom, Marcel Schmidt, Linda K.M. Meekels, Eduardo F. Teixeira de Oliveira
Publikováno v:
Computational and Structural Biotechnology Journal, Vol 19, Iss, Pp 1277-1287 (2021)
Computational and Structural Biotechnology Journal
Computational and Structural Biotechnology Journal, 19, 1277-1287. Elsevier Bedrijfsinformatie b.v.
Computational and Structural Biotechnology Journal
Computational and Structural Biotechnology Journal, 19, 1277-1287. Elsevier Bedrijfsinformatie b.v.
Graphical abstract
Omniligase-1 is a broadly applicable enzyme for peptide bond formation between an activated acyl donor peptide and a non-protected acyl acceptor peptide. The enzyme is derived from an earlier subtilisin variant called peptilig
Omniligase-1 is a broadly applicable enzyme for peptide bond formation between an activated acyl donor peptide and a non-protected acyl acceptor peptide. The enzyme is derived from an earlier subtilisin variant called peptilig
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ea8ebcabf304d2ff08d475d9a857fe9c
https://doi.org/10.1016/j.csbj.2021.02.002
https://doi.org/10.1016/j.csbj.2021.02.002