Zobrazeno 1 - 4
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pro vyhledávání: '"Si Naftaly"'
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-10 (2018)
Characterizing the binding selectivity landscape of interacting proteins is crucial in protein engineering. Here the authors use multi-target selective library screening and in silico next-generation sequencing to map the binding landscape of protein
Externí odkaz:
https://doaj.org/article/ac5f05fbac774e239f296d3fd917c27a
Publikováno v:
ProteinsREFERENCES. 90(1)
Deep mutational scanning provides unprecedented wealth of quantitative data regarding the functional outcome of mutations in proteins. A single experiment may measure properties (eg, structural stability) of numerous protein variants. Leveraging the
Publikováno v:
Biochemical Journal. 475:1335-1352
High structural and sequence similarity within protein families can pose significant challenges to the development of selective inhibitors, especially toward proteolytic enzymes. Such enzymes usually belong to large families of closely similar protea
Publikováno v:
Nature Communications
Nature Communications, Vol 9, Iss 1, Pp 1-10 (2018)
'Nature Communications ', vol: 9, pages: 3935-1-3935-10 (2018)
Nature Communications, Vol 9, Iss 1, Pp 1-10 (2018)
'Nature Communications ', vol: 9, pages: 3935-1-3935-10 (2018)
Characterizing the binding selectivity landscape of interacting proteins is crucial both for elucidating the underlying mechanisms of their interaction and for developing selective inhibitors. However, current mapping methods are laborious and cannot