Zobrazeno 1 - 10
of 17
pro vyhledávání: '"T. J. Brunette"'
Autor:
Yang Hsia, Rubul Mout, William Sheffler, Natasha I. Edman, Ivan Vulovic, Young-Jun Park, Rachel L. Redler, Matthew J. Bick, Asim K. Bera, Alexis Courbet, Alex Kang, T. J. Brunette, Una Nattermann, Evelyn Tsai, Ayesha Saleem, Cameron M. Chow, Damian Ekiert, Gira Bhabha, David Veesler, David Baker
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-10 (2021)
De novo design of self-assembling protein nanostructures and materials is of significant interest, however design of complex, multi-component assemblies is challenging. Here, the authors present a stepwise hierarchical approach to build such assembli
Externí odkaz:
https://doaj.org/article/8bb80e33cedb4e58856a97a798a217fd
Autor:
Kejia Wu, Hua Bai, Ya-Ting Chang, Rachel Redler, Kerrie E. McNally, William Sheffler, T. J. Brunette, Derrick R. Hicks, Tomos E. Morgan, Tim J. Stevens, Adam Broerman, Inna Goreshnik, Michelle DeWitt, Cameron M. Chow, Yihang Shen, Lance Stewart, Emmanuel Derivery, Daniel Adriano Silva, Gira Bhabha, Damian C. Ekiert, David Baker
Publikováno v:
Nature. 616:581-589
General approaches for designing sequence-specific peptide-binding proteins would have wide utility in proteomics and synthetic biology. However, designing peptide-binding proteins is challenging, as most peptides do not have defined structures in is
Autor:
Sherry Bermeo, Andrew Favor, Ya-Ting Chang, Andrew Norris, Scott E. Boyken, Yang Hsia, Hugh K. Haddox, Chunfu Xu, T. J. Brunette, Vicki H. Wysocki, Gira Bhabha, Damian C. Ekiert, David Baker
Publikováno v:
Nature Structural & Molecular Biology. 29:1266-1276
The de novo design of three protein chains that associate to form a heterotrimer (but not any of the possible two-chain heterodimers) and that can drive the assembly of higher-order branching structures is an important challenge for protein design. W
Autor:
Derrick R. Hicks, Madison A. Kennedy, Kirsten A. Thompson, Michelle DeWitt, Brian Coventry, Alex Kang, Asim K. Bera, T. J. Brunette, Banumathi Sankaran, Barry Stoddard, David Baker
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 119(30)
Function follows form in biology, and the binding of small molecules requires proteins with pockets that match the shape of the ligand. For design of binding to symmetric ligands, protein homo-oligomers with matching symmetry are advantageous as each
Autor:
William A. Catterall, Qi Xu, Daohua Jiang, Atsuko Uyeda, Jiayi Dou, Tamer M. Gamal El-Din, Tomoaki Matsuura, Yang Hsia, David Baker, Dan Ma, Matthew J. Bick, T. J. Brunette, Justin M. Kollman, Chunfu Xu, Hua Bai, Eric M. Lynch, Po-Ssu Huang, Gabriella Reggiano, Peilong Lu, Scott E. Boyken, Matthew C. Johnson, Xue Y. Pei, Frank DiMaio, Lance Stewart, Ben F. Luisi
Publikováno v:
Nature
Transmembrane channels and pores have key roles in fundamental biological processes1 and in biotechnological applications such as DNA nanopore sequencing2-4, resulting in considerable interest in the design of pore-containing proteins. Synthetic amph
Autor:
T. J. Brunette, Matthew J. Bick, Justin M. Kollman, Jesse M Hansen, David Baker, Cameron M. Chow
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Significance The ability to robustly control macromolecular shape on the nanometer length scale is important for a wide range of biomedical and materials applications. DNA nanotechnology has achieved considerable success in building up complex struct
Autor:
Glenna Wink Foight, Per Jr Greisen, Cindy T. Wei, Dustin J. Maly, David Baker, Zhizhi Wang, William Sheffler, T. J. Brunette, Daniel Cunningham-Bryant, Keunwan Park, Katrina M Warner
Publikováno v:
Nature biotechnology
Chemical and optogenetic methods for post-translationally controlling protein function have enabled new discoveries and the engineering of synthetic cellular functions. However, most of these methods only confer single-input, single-output control. T
Autor:
Mengxuan Jia, David Flores-Solis, David Baker, Scott E. Boyken, Zibo Chen, T. J. Brunette, Matthew J. Bick, Sherry Bermeo, Aniruddha Sahasrabuddhe, Frank DiMaio, Vicki H. Wysocki, Peilong Lu, Nikolaos G. Sgourakis, Florian Busch, Robert A. Langan, Vikram Khipple Mulligan, Lauren Carter, Zachary L. VanAernum
Publikováno v:
Nature. 565:106-111
Heterodimeric interaction specificity between two DNA strands, and between protein and DNA, is often achieved by varying side chains or bases coming off the protein or DNA backbone -- for example, the bases participating in Watson-Crick base pairing
Autor:
Ivan Vulovic, Cameron M. Chow, Natasha I. Edman, Evelyn Tsai, Yang Hsia, Matthew J. Bick, Alex Kang, Alexis Courbet, William Sheffler, Rubul Mout, Gira Bhabha, Rachel L. Redler, Young-Jun Park, David Veesler, David Baker, Una Nattermann, Damian C. Ekiert, Ayesha Saleem, Asim K. Bera, T. J. Brunette
Publikováno v:
Nature Communications
Nature Communications, Vol 12, Iss 1, Pp 1-10 (2021)
Nature Communications, Vol 12, Iss 1, Pp 1-10 (2021)
A systematic and robust approach to generating complex protein nanomaterials would have broad utility. We develop a hierarchical approach to designing multi-component protein assemblies from two classes of modular building blocks: designed helical re
Autor:
Damian C. Ekiert, John A. Tainer, David Baker, Fabio Parmeggiani, Po-Ssu Huang, T. J. Brunette, Susan E. Tsutakawa, Greg L. Hura, Gira Bhabha
Publikováno v:
Nature
A central question in protein evolution is the extent to which naturally occurring proteins sample the space of folded structures accessible to the polypeptide chain. Repeat proteins composed of multiple tandem copies of a modular structure unit are