Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Hugh K. Haddox"'
Autor:
Tamuka M. Chidyausiku, Soraia R. Mendes, Jason C. Klima, Marta Nadal, Ulrich Eckhard, Jorge Roel-Touris, Scott Houliston, Tibisay Guevara, Hugh K. Haddox, Adam Moyer, Cheryl H. Arrowsmith, F. Xavier Gomis-Rüth, David Baker, Enrique Marcos
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-14 (2022)
The immunoglobulin domain framework of antibodies has been a long standing design challenge. Here, the authors describe design rules for tailoring these domains and show they can be accurately designed, de novo, with high stability and the ability to
Externí odkaz:
https://doaj.org/article/97a8dd6f14d04e56ae09b84b09e5515d
Autor:
Jedediah M. Singer, Scott Novotney, Devin Strickland, Hugh K. Haddox, Nicholas Leiby, Gabriel J. Rocklin, Cameron M. Chow, Anindya Roy, Asim K. Bera, Francis C. Motta, Longxing Cao, Eva-Maria Strauch, Tamuka M. Chidyausiku, Alex Ford, Ethan Ho, Alexander Zaitzeff, Craig O. Mackenzie, Hamed Eramian, Frank DiMaio, Gevorg Grigoryan, Matthew Vaughn, Lance J. Stewart, David Baker, Eric Klavins
Publikováno v:
PLoS ONE, Vol 17, Iss 3 (2022)
Engineered proteins generally must possess a stable structure in order to achieve their designed function. Stable designs, however, are astronomically rare within the space of all possible amino acid sequences. As a consequence, many designs must be
Externí odkaz:
https://doaj.org/article/6bc977c80731465da8bb65f2719bfb0c
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:
Tae-Eun Kim, Kotaro Tsuboyama, Scott Houliston, Cydney M. Martell, Claire M. Phoumyvong, Alexander Lemak, Hugh K. Haddox, Cheryl H. Arrowsmith, Gabriel J. Rocklin
Publikováno v:
Proceedings of the National Academy of Sciences. 119
Designing entirely new protein structures remains challenging because we do not fully understand the biophysical determinants of folding stability. Yet some protein folds are easier to design than others. Previous work identified the 43-residue □β
Autor:
Jan D. Estrada Pabón, Greg Van Aken, Jedediah M. Singer, Hugh K. Haddox, Ian M. Pendleton, Joshua Schrier, Hamed Eramian
Publikováno v:
The Journal of Physical Chemistry B. 125:3057-3065
Predicting protein stability is a challenge due to the many competing thermodynamic effects. Through de novo protein design, one begins with a target structure and searches for a sequence that will fold into it. Previous work by Rocklin et al. introd
Autor:
David F Thieker, Eric Klavins, Surya V.S.R.K. Pulavarti, Frank DiMaio, Jermel R. Griffin, David Baker, Matthew Cummins, Thomas Szyperski, Hugh K. Haddox, Devin Strickland, Brian Coventry, Brian Kuhlman, Samer Halabiya, Jack Maguire
Publikováno v:
Proteins
The FastDesign protocol in the molecular modeling program Rosetta iterates between sequence optimization and structure refinement to stabilize de novo designed protein structures and complexes. FastDesign has been used previously to design novel prot
Autor:
Jedediah M. Singer, Scott Novotney, Devin Strickland, Hugh K. Haddox, Nicholas Leiby, Gabriel J. Rocklin, Cameron M. Chow, Anindya Roy, Asim K. Bera, Francis C. Motta, Longxing Cao, Eva-Maria Strauch, Tamuka M. Chidyausiku, Alex Ford, Ethan Ho, Alexander Zaitzeff, Craig O. Mackenzie, Hamed Eramian, Frank DiMaio, Gevorg Grigoryan, Matthew Vaughn, Lance J. Stewart, David Baker, Eric Klavins
Publikováno v:
PloS one. 17(3)
Engineered proteins generally must possess a stable structure in order to achieve their designed function. Stable designs, however, are astronomically rare within the space of all possible amino acid sequences. As a consequence, many designs must be
Autor:
Devin Strickland, Alex Ford, Tamuka M. Chidyausiku, Francis C. Motta, Hamed Eramian, Gabriel J. Rocklin, Jedediah M. Singer, Longxing Cao, Ethan Ho, Anindya Roy, Gevorg Grigoryan, Scott Novotney, Asim K. Bera, Eva-Maria Strauch, Nicholas Leiby, Cameron M. Chow, Hugh K. Haddox, David Baker, Lance Stewart, Matthew W. Vaughn, Craig O. Mackenzie, Frank DiMaio, Eric Klavins
Engineered proteins generally must possess a stable structure in order to achieve their designed function. Stable designs, however, are astronomically rare within the space of all possible amino acid sequences. As a consequence, many designs must be
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1e9365315f7ac752b3e51cd28d482387
https://doi.org/10.1101/2021.03.12.435185
https://doi.org/10.1101/2021.03.12.435185
Autor:
Jermel R. Griffin, Samer Halabiya, Brian Coventry, Frank DiMaio, Hugh K. Haddox, Devin Strickland, S. Pulavarti, David Baker, Thomas Szyperski, Jack Maguire, Brian Kuhlman, Eric Klavins, Matthew Cummins, David F Thieker
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::87189a7806962908b25419ef1f025608
https://doi.org/10.1002/prot.26030/v2/response1
https://doi.org/10.1002/prot.26030/v2/response1
Autor:
Frank DiMaio, Brian Coventry, Samer Halabiya, Matthew Cummins, David Baker, Brian Kuhlman, Jack Maguire, David F Thieker, Devin Strickland, Eric Klavins, Hugh K. Haddox
The FastDesign protocol in the molecular modeling program Rosetta iterates between sequence optimization and structure refinement to stabilize de novo designed protein structures and complexes. FastDesign has been used previously to design novel prot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3264767860e3f1803c8791f2b55f24f1
https://doi.org/10.22541/au.158986804.41133682
https://doi.org/10.22541/au.158986804.41133682