Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Nicholas B. Rego"'
Autor:
Amish J. Patel, Nicholas B. Rego
Publikováno v:
Annual Review of Condensed Matter Physics. 13:303-324
The aversion of hydrophobic solutes for water drives diverse interactions and assemblies across materials science, biology and beyond. % Here, we review the theoretical, computational and experimental developments which underpin a contemporary unders
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::75cf9b0afb76725e5063567ae5cb4275
https://doi.org/10.1146/annurev-conmatphys-040220-045516
https://doi.org/10.1146/annurev-conmatphys-040220-045516
Publikováno v:
Proc Natl Acad Sci U S A
Interactions between proteins lie at the heart of numerous biological processes and are essential for the proper functioning of the cell. Although the importance of hydrophobic residues in driving protein interactions is universally accepted, a chara
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9977fc25b9554240623d935fe8ed90c4
https://europepmc.org/articles/PMC8018078/
https://europepmc.org/articles/PMC8018078/
Autor:
Erte Xi, Vasudevan Venkateshwaran, Nicholas B. Rego, Amish J. Patel, Lijuan Li, Shekhar Garde
Publikováno v:
Proceedings of the National Academy of Sciences. 114:13345-13350
Hydrophobic interactions drive many important biomolecular self-assembly phenomena. However, characterizing hydrophobicity at the nanoscale has remained a challenge due to its nontrivial dependence on the chemistry and topography of biomolecular surf
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f73dbe1b862761a80fd3742523d03359
https://doi.org/10.1073/pnas.1700092114
https://doi.org/10.1073/pnas.1700092114
Publikováno v:
The journal of physical chemistry. B. 123(7)
Hydrophobic effects drive diverse aqueous assemblies, such as micelle formation or protein folding, wherein the solvent plays an important role. Consequently, characterizing the free energetics of solvent density fluctuations can lead to important in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a2ac6c7fff7122bfeaac8472596bfee9
https://pubmed.ncbi.nlm.nih.gov/30682885
https://pubmed.ncbi.nlm.nih.gov/30682885
The interactions of a protein, its phase behavior, and ultimately, its ability to function, are all influenced by the interactions between the protein and its hydration waters. Here we study proteins with a variety of sizes, shapes, chemistries, and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ce89f540af99875dd2054b5fc32fd861
http://arxiv.org/abs/1811.02678
http://arxiv.org/abs/1811.02678
Autor:
Nicholas B. Rego, Adam J. Pratt, Kim F. Wong, Joshua L. Adelman, Lillian T. Chong, Matthew C. Zwier, Steven Lettieri, Michael Grabe, Daniel M. Zuckerman, David W. Wang, Ernesto Suárez, Joseph W. Kaus
Publikováno v:
Journal of Chemical Theory and Computation. 11:800-809
The weighted ensemble (WE) path sampling approach orchestrates an ensemble of parallel calculations with intermittent communication to enhance the sampling of rare events, such as molecular associations or conformational changes in proteins or peptid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::99f113f19343032d6128b260d120ef91
https://doi.org/10.1021/ct5010615
https://doi.org/10.1021/ct5010615