Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Erte Xi"'
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/
Publikováno v:
Macromolecules
Macromolecules, 2021, Vol.54(6), pp.2763-2773 [Peer Reviewed Journal]
Macromolecules, 2021, Vol.54(6), pp.2763-2773 [Peer Reviewed Journal]
In this work, we calculate Flory-Huggins phase diagrams for correlated random copolymers. We achieve it in two steps. At first, we derive a distribution function of two-letter A, B copolymer chains depending on the fraction of A-segments and ABduplet
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e457f05b6f939212d9218f65baaf3682
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
Publikováno v:
Proceedings of the National Academy of Sciences. 113:5508-5513
Rough or textured hydrophobic surfaces are dubbed superhydrophobic due to their numerous desirable properties, such as water repellency and interfacial slip. Superhydrophobicity stems from an aversion for water to wet the surface texture, so that a w
Publikováno v:
Journal of Chemical Theory and Computation. 12:706-713
The free energetics of water density fluctuations near a surface, and the rare low-density fluctuations in particular, serve as reliable indicators of surface hydrophobicity; the easier it is to displace the interfacial waters, the more hydrophobic t
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
Publikováno v:
The journal of physical chemistry. B. 122(13)
The solubility of proteins and other macromolecular solutes plays an important role in numerous biological, chemical, and medicinal processes. An important determinant of protein solubility is the solvation free energy of the protein, which quantifie
Autor:
Amish J. Patel, Erte Xi, Srivathsan Vembanur, Richard C. Remsing, Sumit Sharma, Shekhar Garde, Pablo G. Debenedetti
Liquid water can become metastable with respect to its vapor in hydrophobic confinement. The resulting dewetting transitions are often impeded by large kinetic barriers. According to macroscopic theory, such barriers arise from the free energy requir
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4337123133543240473f1d4fb340ecee
http://arxiv.org/abs/1502.05436
http://arxiv.org/abs/1502.05436
Autor:
Remsing, Richard C., Erte Xi, Vembanur, Srivathsan, Sharma, Sumit, Debenedetti, Pablo G., Garde, Shekhar, Patel, Amish J.
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America; 7/7/2015, Vol. 112 Issue 27, p8181-8186, 6p