Zobrazeno 1 - 10
of 85
pro vyhledávání: '"Kathleen G. Valentine"'
Publikováno v:
Biophysical Reports, Vol 3, Iss 1, Pp 100098- (2023)
The thermodynamics of molecular recognition by proteins is a central determinant of complex biochemistry. For over a half-century, detailed cryogenic structures have provided deep insight into the energetic contributions to ligand binding by proteins
Externí odkaz:
https://doaj.org/article/69eae41ec89b401abf3ade8765988f6c
Autor:
A. Joshua Wand, Nathaniel V. Nucci, Matthew A. Stetz, Kathleen G. Valentine, Bryan S. Marques, Christine Jorge
Publikováno v:
Scientific Reports
Scientific Reports, Vol 10, Iss 1, Pp 1-8 (2020)
Scientific Reports, Vol 10, Iss 1, Pp 1-8 (2020)
Conformational entropy can be an important element of the thermodynamics of protein functions such as the binding of ligands. The observed role for conformational entropy in modulating molecular recognition by proteins is in opposition to an often-in
Autor:
A. Joshua Wand, Brian Fuglestad, Bryan S. Marques, Nicole E. Kerstetter, Kathleen G. Valentine, Christine Jorge
Publikováno v:
Methods in enzymology. 615
Reverse micelle (RM) encapsulation of proteins for NMR spectroscopy has many advantages over standard NMR methods such as enhanced tumbling and improved sensitivity. It has opened many otherwise difficult lines of investigation including the study of
Autor:
Bryan S. Marques, Sravya Kotaru, Jose A. Caro, A. Joshua Wand, Xuejun Yao, Kathleen G. Valentine, Matthew A. Stetz
Recent studies suggest that the fast timescale motion of methyl-bearing side chains may play an important role in mediating protein activity. These motions have been shown to encapsulate the residual conformational entropy of the folded state that ca
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::44f906d3cf274c911946a55b6fc61cc7
https://doi.org/10.1016/bs.mie.2018.09.010
https://doi.org/10.1016/bs.mie.2018.09.010
Protein hydration is a critical aspect of protein stability, folding, and function and yet remains difficult to characterize experimentally. Solution NMR offers a route to a site-resolved view of the dynamics of protein-water interactions through the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::39b355ee7866e040c122e6fee5920f53
https://doi.org/10.1016/bs.mie.2018.09.040
https://doi.org/10.1016/bs.mie.2018.09.040
Autor:
Jakob Dogan, Sabrina Bédard, Vignesh Kasinath, A. Joshua Wand, Veronica R. Moorman, Kathleen G. Valentine, Fiona Love
Publikováno v:
Journal of Molecular Biology. 426:3520-3538
Human cell division cycle protein 42 (Cdc42Hs) is a small, Rho-type guanosine triphosphatase involved in multiple cellular processes through its interactions with downstream effectors. The binding domain of one such effector, the actin cytoskeleton-r
Autor:
Kyle W. Harpole, Jackwee Lim, A. Joshua Wand, Jeffrey M. Granja, Vignesh Kasinath, Kim A. Sharp, Jose A. Caro, Kathleen G. Valentine
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 114(25)
Molecular recognition by proteins is fundamental to molecular biology. Dissection of the thermodynamic energy terms governing protein-ligand interactions has proven difficult, with determination of entropic contributions being particularly elusive. N
Publikováno v:
Journal of Magnetic Resonance. 241:137-147
High-resolution multi-dimensional solution NMR is unique as a biophysical and biochemical tool in its ability to examine both the structure and dynamics of macromolecules at atomic resolution. Conventional solution NMR approaches, however, are largel
Autor:
Gurnimrat K. Sidhu, A. Joshua Wand, Arthur Pardi, Igor Dodevski, Nathaniel V. Nucci, Kathleen G. Valentine, Evan S. O'Brien
Publikováno v:
Journal of the American Chemical Society
An optimized reverse micelle surfactant system has been developed for solution nuclear magnetic resonance studies of encapsulated proteins and nucleic acids dissolved in low viscosity fluids. Comprising the nonionic 1-decanoyl-rac-glycerol and the zw
Autor:
Robert G. Griffin, Guinevere Mathies, Thach V. Can, Sabrina Bédard, Kathleen G. Valentine, Matthew A. Stetz, A. Joshua Wand, Nathaniel V. Nucci, Igor Dodevski
Publikováno v:
Journal of the American Chemical Society
Despite tremendous advances in recent years, solution NMR remains fundamentally restricted due to its inherent insensitivity. Dynamic nuclear polarization (DNP) potentially offers significant improvements in this respect. The basic DNP strategy is to