Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Declan Evans"'
Autor:
Andy Hsien-Wei Yeh, Christoffer Norn, Yakov Kipnis, Doug Tischer, Samuel J. Pellock, Declan Evans, Pengchen Ma, Gyu Rie Lee, Jason Z. Zhang, Ivan Anishchenko, Brian Coventry, Longxing Cao, Justas Dauparas, Samer Halabiya, Michelle DeWitt, Lauren Carter, K. N. Houk, David Baker
Publikováno v:
Nature, vol 614, iss 7949
De novo enzyme design has sought to introduce active sites and substrate-binding pockets that are predicted to catalyse a reaction of interest into geometrically compatible native scaffolds1,2, but has been limited by a lack of suitable protein struc
Autor:
Mary C. Andorfer, Declan Evans, Song Yang, Cyndi Qixin He, Anna M. Girlich, Jaylie Vergara-Coll, Narayanasami Sukumar, K.N. Houk, Jared C. Lewis
Publikováno v:
Chem Catalysis. 2:2658-2674
Flavin-dependent halogenases catalyze selective halogenation of electron-rich aromatic compounds without the need for harsh oxidants required by conventional oxidative halogenation reactions. Predictive models for halogenase site selectivity would gr
Autor:
Isaac Benavides, Eric D. Raftery, Alexandra G. Bell, Declan Evans, Wendell A. Scott, K. N. Houk, Timothy J. Deming
Publikováno v:
Journal of the American Chemical Society. 144(9)
Via the design of a new, soluble poly(
Autor:
Wen-Tao Li, Qi-Lin Zhou, Mao-Lin Li, Shou-Fei Zhu, Liang-Liang Yang, Bin Xu, K. N. Houk, Declan Evans
Publikováno v:
J Am Chem Soc
Journal of the American Chemical Society, vol 142, iss 28
Journal of the American Chemical Society, vol 142, iss 28
Catalytic enantioselection usually depends on differences in steric interactions between prochiral substrates and a chiral catalyst. We have discovered a carbene Si-H insertion in which the enantioselectivity depends primarily on the electronic chara
Autor:
Kevin A. Murray, Declan Evans, Michael P. Hughes, Michael R. Sawaya, Carolyn J. Hu, Kendall N. Houk, David Eisenberg
The assembly of proteins into fibrillar amyloid structures was once considered to be pathologic and essentially irreversible. Recent studies reveal amyloid-like structures that form reversibly, derived from protein low-complexity domains which functi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::126b6a33ecd475f197e71cbaacf00817
https://resolver.caltech.edu/CaltechAUTHORS:20220208-948240000
https://resolver.caltech.edu/CaltechAUTHORS:20220208-948240000
Publikováno v:
Biophysical Journal. 110:2610-2617
Protein-nucleic acid interactions are central to a variety of biological processes, many of which involve large-scale conformational changes that lead to bending of the nucleic acid helix. Here, we focus on the nonsequence-specific protein TRBP, whos