Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Jonathan Cuthbertson"'
Publikováno v:
Magnetic Resonance in Medicine. 81:2176-2183
PURPOSE: An innovative radio-frequency (RF) coil design that allows RF currents both at the Larmor frequency and in a wireless communication band to flow on the same coil is proposed to enable simultaneous MRI signal reception and wireless data trans
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4f5a62db8ea098d69435d7893da9b27c
https://doi.org/10.1002/mrm.27513
https://doi.org/10.1002/mrm.27513
The in vitro study of membrane proteins for the purpose of physicochemical analysis or structure determination often relies upon successful reconstitution into detergent micelles. Moreover, a number of biological processes such as membrane protein fo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c00c16912ae02c119b251ea5a2c2cd79
https://doi.org/10.1021/ja044819e
https://doi.org/10.1021/ja044819e
The prediction of transmembrane (TM) helices plays an important role in the study of membrane proteins, given the relatively small number (approximately 0.5% of the PDB) of high-resolution structures for such proteins. We used two datasets (one redun
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::26e9a45b053319e27571d9044524e6c4
https://ora.ox.ac.uk/objects/uuid:5116691e-edeb-45e6-988e-cf1ef9e97824
https://ora.ox.ac.uk/objects/uuid:5116691e-edeb-45e6-988e-cf1ef9e97824
Autor:
George Patargias, Mark S.P. Sansom, Carmen Domene, José D. Faraldo-Gómez, Peter J. Bond, Jonathan Cuthbertson, Lucy R. Forrest, Marc Baaden
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 57:783-791
In the current report, we provide a quantitative analysis of the convergence of the sampling of conformational space accomplished in molecular dynamics simulations of membrane proteins of duration in the order of 10 nanoseconds. A set of proteins of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::415035b7a3220fc68cd019ac874222d6
https://doi.org/10.1002/prot.20257
https://doi.org/10.1002/prot.20257
Autor:
Jonathan Cuthbertson, Mark S.P. Sansom
Publikováno v:
The Biochemist. 26:25-28
Membrane proteins account for approximately 25% of all genes, and constitute approximately 50% of potential drug targets. The steady increase in the number of three-dimensional structures for membrane proteins means that the twin disciplines of struc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::dbde727eb0ad0dce589b5b4b0d8f0d13
https://doi.org/10.1042/bio02604025
https://doi.org/10.1042/bio02604025
Autor:
Jonathan Cuthbertson, Jennifer M. Johnston, Mark S.P. Sansom, Lucy R. Forrest, Sundeep S. Deol, Peter J. Bond, George Patargias
Publikováno v:
New Algorithms for Macromolecular Simulation ISBN: 3540255427
Molecular dynamics simulations of membrane proteins are reviewed, with especial attention to exploration of the interactions between membrane proteins and their environment. Environments of membrane proteins that have been studied include: (i) solven
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f0ee898cb57b7c314f10d119bfb10960
https://doi.org/10.1007/3-540-31618-3_1
https://doi.org/10.1007/3-540-31618-3_1
Publikováno v:
Biochemical Society transactions. 33(Pt 5)
Interactions between membrane proteins and detergents are important in biophysical and structural studies and are also biologically relevant in the context of folding and transport. Despite a paucity of high-resolution data on protein–detergent int
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2bbd126e68683a0c9c1dd26203458cb0
https://pubmed.ncbi.nlm.nih.gov/16246008
https://pubmed.ncbi.nlm.nih.gov/16246008
Autor:
Declan A. Doyle, Anling Kuo, Takayuki Ezaki, Frances M. Ashcroft, Jacqueline M. Gulbis, Edward D. Lowe, Jochen Zimmer, Jennifer F. Antcliff, Tahmina Rahman, Jonathan Cuthbertson
Publikováno v:
Science (New York, N.Y.). 300(5627)
The KirBac1.1 channel belongs to the inward-rectifier family of potassium channels. Here we report the structure of the entire prokaryotic Kir channel assembly, in the closed state, refined to a resolution of 3.65 angstroms. We identify the main acti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::08a47f76234c7a2468cf749d4a006ddb
https://pubmed.ncbi.nlm.nih.gov/12738871
https://pubmed.ncbi.nlm.nih.gov/12738871