Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Nabil F. Faruk"'
Publikováno v:
PLoS Computational Biology, Vol 14, Iss 12, p e1006342 (2018)
To address the large gap between time scales that can be easily reached by molecular simulations and those required to understand protein dynamics, we present a rapid self-consistent approximation of the side chain free energy at every integration st
Externí odkaz:
https://doaj.org/article/acc06078665e4c9c936a64fc59eefd0b
Publikováno v:
PLoS Computational Biology, Vol 14, Iss 12, p e1006578 (2018)
An ongoing challenge in protein chemistry is to identify the underlying interaction energies that capture protein dynamics. The traditional trade-off in biomolecular simulation between accuracy and computational efficiency is predicated on the assump
Externí odkaz:
https://doaj.org/article/77024e231a02488287694c95dea0776d
Publikováno v:
Journal of Chemical Theory and Computation. 18:2016-2032
Predicting protein binding is a core problem of computational biophysics. That this objective can be partly achieved with some amount of success using docking algorithms based on rigid protein models is remarkable, although going further requires all
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f3bb6d95d14ac3810b99a9797079c954
https://doi.org/10.1021/acs.jctc.1c01255
https://doi.org/10.1021/acs.jctc.1c01255
Publikováno v:
International Journal of Molecular Sciences
Volume 24
Issue 3
Pages: 2654
Volume 24
Issue 3
Pages: 2654
Single-molecule force spectroscopy methods, such as AFM and magnetic tweezers, have proved extremely beneficial in elucidating folding pathways for soluble and membrane proteins. To identify factors that determine the force rupture levels in force-in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d44cc97a5aa521cbec2228da7c00b4b3
Publikováno v:
Biophysical Journal. 122:304a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7f69f431c20cf910819ab5c2207d4f79
https://doi.org/10.1016/j.bpj.2022.11.1711
https://doi.org/10.1016/j.bpj.2022.11.1711
Autor:
Tobin R. Sosnick, Kristen A. Gaffney, Ruiqiong Guo, Michael D. Bridges, Daoyang Chen, Fathima Shaima MuhammedNazaar, Miyeon Kim, Zhongyu Yang, Anthony L. Schilmiller, Nabil F. Faruk, Xiangda Peng, A.D. Jones, Liangliang Sun, Wayne L. Hubbell, Heedeok Hong
Publikováno v:
Biophysical Journal. 121:469a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::179face4b33827341af811019321f077
https://doi.org/10.1016/j.bpj.2021.11.428
https://doi.org/10.1016/j.bpj.2021.11.428
Publikováno v:
PLoS Computational Biology, Vol 14, Iss 12, p e1006342 (2018)
PLoS Computational Biology
PLoS Computational Biology
To address the large gap between time scales that can be easily reached by molecular simulations and those required to understand protein dynamics, we present a rapid self-consistent approximation of the side chain free energy at every integration st
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d71e4f3e90b1ee8576c51bca239623fb
https://doaj.org/article/acc06078665e4c9c936a64fc59eefd0b
https://doaj.org/article/acc06078665e4c9c936a64fc59eefd0b
Autor:
Karl F. Freed, Nabil F. Faruk, Scott Houliston, Cheryl H. Arrowsmith, Michael C. Baxa, Gabriel J. Rocklin, Xiangda Peng, Tobin R. Sosnick
Publikováno v:
Biophysical Journal. 120:116a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ff9f58788760a7c0a295e35af001c584
https://doi.org/10.1016/j.bpj.2020.11.917
https://doi.org/10.1016/j.bpj.2020.11.917
Publikováno v:
Biophysical Journal. 118:353a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e4e1362616660df0cbbbbecd85e44cbc
https://doi.org/10.1016/j.bpj.2019.11.2034
https://doi.org/10.1016/j.bpj.2019.11.2034
Publikováno v:
Computer Physics Communications. 191:203-208
In this work, we provide an interface developed to link the Molecular Modelling toolkit (MMTK) with OpenMM in order to take advantage of the fast evaluation techniques of OpenMM. This interface allows MMTK scripts using the Langevin dynamics integrat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::38ac926159623bb4815a7b11fb15a2e7
https://doi.org/10.1016/j.cpc.2015.01.025
https://doi.org/10.1016/j.cpc.2015.01.025