Zobrazeno 41 - 50
of 57
pro vyhledávání: '"35"'
Autor:
Aneel K. Aggarwal, Nicolas Bolik-Coulon, Fabien Ferrage, Ludovic Carlier, Philippe Pelupessy, Guillaume Bouvignies, Cyril Charlier, Sandrine Sagan, Rodrigue Marquant, Mikhail Kozlov, Astrid Walrant, Pablo De Ioannes, Patricia Cortes
Publikováno v:
Journal of the American Chemical Society
Journal of the American Chemical Society, 2017, 139 (35), pp.12219-12227. ⟨10.1021/jacs.7b05823⟩
Journal of the American Chemical Society, American Chemical Society, 2017, 139 (35), pp.12219-12227. ⟨10.1021/jacs.7b05823⟩
Journal of the American Chemical Society, 2017, 139 (35), pp.12219-12227. ⟨10.1021/jacs.7b05823⟩
Journal of the American Chemical Society, American Chemical Society, 2017, 139 (35), pp.12219-12227. ⟨10.1021/jacs.7b05823⟩
International audience; Many intrinsically disordered proteins (IDPs) and protein regions (IDRs) engage in transient, yet specific, interactions with a variety of protein partners. Often, if not always, interactions with a protein partner lead to par
Autor:
Klaus Gawrisch, Ivan V. Polozov, Nadukkudy V. Eldho, Scott E. Feller, Stephanie Tristram-Nagle
Publikováno v:
Journal of the American Chemical Society. 125:6409-6421
Insufficient supply to the developing brain of docosahexaenoic acid (22:6n3, DHA), or its omega-3 fatty acid precursors, results in replacement of DHA with docosapentaenoic acid (22:5n6, DPA), an omega-6 fatty acid that is lacking a double bond near
Publikováno v:
J Am Chem Soc
Huntingtin polypeptides (htt(ex1)), encoded by exon 1 of the htt gene and containing an expanded polyglutamine tract, form fibrils that accumulate within neuronal inclusion bodies, resulting in the fatal neurodegenerative condition known as Huntingto
Autor:
Ann E. McDermott, Justin L. Lorieau
Publikováno v:
Journal of the American Chemical Society. 128:11505-11512
The majority of protein structures are determined in the crystalline state, yet few methods exist for the characterization of dynamics for crystalline biomolecules. Solid-state NMR can be used to probe detailed dynamic information in crystalline biom
Publikováno v:
Journal of the American Chemical Society. 128:2121-2134
The results of a detailed systematic chlorine solid-state NMR study of several hydrochloride salts of amino acids implicated in chloride ion transport channel selectivity are reported. (35)Cl and (37)Cl NMR spectra have been obtained for stationary a
Autor:
Koichiro Ishimori, Isao Morishima, Takehiko Tosha, Shiro Yoshioka, Hiroshi Hori, Satoshi Takahashi
Publikováno v:
Journal of the American Chemical Society. 124:14571-14579
Structural and functional roles of the hydrogen bonding network that surrounds the heme-thiolate coordination of P450(cam) from Pseudomonas putida were investigated. A hydrogen bond between the side chain amide of Gln360 and the carbonyl oxygen of th
Publikováno v:
Journal of the American Chemical Society. 124:6449-6460
In the previous paper in this issue we have demonstrated that it is possible to measure the five different relaxation rates of a deuteron in (13)CH(2)D methyl groups of (13)C-labeled, fractionally deuterated proteins. The extensive set of data acquir
Autor:
Stoyan K. Smoukov, Brian M. Hoffman, Stephen J. Lippard, Daniel A. Kopp, Roman Davydov, Ann M. Valentine
Publikováno v:
Journal of the American Chemical Society. 124:2657-2663
The binding of ethanol and 1,1,1-trifluoroethanol (TFE) to both the H(mv) and H(ox) forms of soluble methane monooxygenase (sMMO) in solution has been studied by Q-band (35 GHz) CW and pulsed ENDOR spectroscopy of (1)H, (2)H and (19)F nuclei of exoge
Autor:
Fiala, R., Spackova, N., Foldynová-Trantírková, S., Sponer, J., Sklenár, V., Trantirek, L., Cellular Protein Chemistry, Sub Cellular Protein Chemistry
Publikováno v:
Journal of the American Chemical Society, 133(35), 13790. American Chemical Society
In this work, a novel NMR method for the identification of preferential coordination sites between physiologically relevant counterions and nucleic acid bases is demonstrated. In this approach, the NMR cross-correlated relaxation rates between the ar
Publikováno v:
Journal of the American Chemical Society. 131(22)
NMR-based drug screening methods provide the most reliable characterization of binding propensities of ligands to their target proteins. Unique to NMR is its capability to detect weak microM-mM bindings. NMR assays are, however, one of the least effe