Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Lucas G. Nivón"'
Autor:
Gustav Oberdorfer, Santrupti Nerli, David Baker, Lauren Carter, Konstantinos Tripsianes, Nikolaos G. Sgourakis, Andrew C. McShan, Lucas G. Nivón, Enrique Marcos, Tamuka M. Chidyausiku, Audrey Davis, Thomas Evangelidis
Publikováno v:
Nature structural & molecular biology
β-sheet proteins carry out critical functions in biology, and hence are attractive scaffolds for computational protein design. Despite this potential, de novo design of all-β-sheet proteins from first principles lags far behind the design of all-α
Autor:
Lucas G. Nivón, Eugene I. Shakhnovich
Publikováno v:
Journal of Molecular Biology. 344:29-45
We report a detailed all-atom simulation of the folding of the GCAA RNA tetraloop. The GCAA tetraloop motif is a very common and thermodynamically stable secondary structure in natural RNAs. We use our simulation methods to study the folding behavior
Publikováno v:
Gene. 341:249-253
A new determination of the house cat (Felis catus) prion protein gene sequence (fPrnp), which has so far been subject of controversy, is reported. The newly determined fPrnp sequence is similar to dog (Canis familiaris) and mink (Mustela putorius) Pr
Publikováno v:
Hippocampus. 12:245-257
Chronic stress causes atrophy of the apical dendrites of CA3 pyramidal neurons and deficits in spatial memory. We investigated the effects of chronic stress on hippocampal physiology and long-term potentiation (LTP) in the CA3 and dentate gyrus (DG).
Autor:
Catherine L. Drennan, Lucas G. Nivón, Florian Richter, Anne Z. Ye, Douglas S. Richardson, David Baker, Peter Goldman, Jennifer Z. Yao, Daniel S. Liu, Mark H. Ellisman, William S. Phipps, Thomas J. Deerinck, Alice Y. Ting
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America, vol 111, iss 43
Proceedings of the National Academy of Sciences of the United States of America, vol 111, iss 43
Chemical fluorophores offer tremendous size and photophysical advantages over fluorescent proteins but are much more challenging to target to specific cellular proteins. Here, we used Rosetta-based computation to design a fluorophore ligase that acce
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8c7f221ac3b138fc989a3f46a3939c51
https://hdl.handle.net/11858/00-001M-0000-0024-4092-A11858/00-001M-0000-0024-408F-311858/00-001M-0000-0024-4091-C
https://hdl.handle.net/11858/00-001M-0000-0024-4092-A11858/00-001M-0000-0024-408F-311858/00-001M-0000-0024-4091-C
Publikováno v:
Proteins. 82(5)
In the design of new enzymes and binding proteins, human intuition is often used to modify computationally designed amino acid sequences prior to experimental characterization. The manual sequence changes involve both reversions of amino acid mutatio
Autor:
Sinisa Bjelic, Forrest E. Michael, David Baker, Scott Lew, Gert Kiss, Jasmine L. Gallaher, Helena M. Lovick, John F. Hunt, Gaetano T. Montelione, Erica L. Ingalls, Lucas G. Nivón, Kendall N. Houk, Nihan Çelebi-Ölçüm, Jayaraman Seetharaman, Carolyn F. Rosewall
The Morita-Baylis-Hillman reaction forms a carbon-carbon bond between the alpha carbon of a conjugated carbonyl compound and a carbon electrophile. The reaction mechanism involves Michael addition of a nucleophile catalyst at the carbonyl beta carbon
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fec4d63de181fde4358467b377a9b20f
https://europepmc.org/articles/PMC3647451/
https://europepmc.org/articles/PMC3647451/
Autor:
Lucas G. Nivón, Eugene I. Shakhnovich
We report a set of atomistic folding/unfolding simulations for the hairpin ribozyme using a Monte Carlo algorithm. The hairpin ribozyme folds in solution and catalyzes self-cleavage or ligation via a specific two-domain structure. The minimal active
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::30ccf299c97cbddb6ff9694332ff098f
https://europepmc.org/articles/PMC3508787/
https://europepmc.org/articles/PMC3508787/
Autor:
Minh Hong, Xiaowei Zhuang, Shixin Liu, Gregory Bokinsky, Geqing Chai, Kevin M. Weeks, Lucas G. Nivón
Like most cellular RNA enzymes, the bI5 group I intron requires binding by a protein cofactor to fold correctly. Here, we use single-molecule approaches to monitor the structural dynamics of the bI5 RNA in real time as it assembles with its CBP2 prot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::31167185f42247404c2fe8bacd5409f9
Autor:
Christine von Schroetter, Barbara Christen, Vicent Esteve-Moya, Christian Schorn, Dominikus A. Lysek, Lucas G. Nivón, Torsten Herrmann, Luigi Calzolai, Francesco Fiorito, Peter Güntert, Kurt Wüthrich
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 102(3)
The NMR structures of the recombinant cellular form of the prion proteins (PrP C ) of the cat ( Felis catus ), dog ( Canis familiaris ), and pig ( Sus scrofa ), and of two polymorphic forms of the prion protein from sheep ( Ovis aries ) are presented