Zobrazeno 1 - 9
of 9
pro vyhledávání: '"35"'
Autor:
Elodie Point, Karine Moncoq, Marina Casiraghi, Ewen Lescop, Jean-Louis Banères, Marjorie Damian, Daniel Lévy, Eric Guittet, Nelly Morellet, Laurent Catoire, Jacky Marie
Publikováno v:
Journal of the American Chemical Society
Journal of the American Chemical Society, American Chemical Society, 2016, 138 (35), pp.11170-11175. ⟨10.1021/jacs.6b04432⟩
Journal of the American Chemical Society, American Chemical Society, 2016, 138 (35), pp.11170-11175. ⟨10.1021/jacs.6b04432⟩
International audience; Mapping the conformational landscape of G protein-coupled receptors (GPCRs), and in particular how this landscape is modulated by the membrane environment, is required to gain a clear picture of how signaling proceeds. To this
Autor:
Michal Avital-Shmilovici, Kalyaneswar Mandal, Nelson B. Phillips, Michael A. Weiss, Zachary P. Gates, Stephen B. H. Kent
Publikováno v:
Journal of the American Chemical Society. 135:3173-3185
Efficient total synthesis of insulin is important to enable the application of medicinal chemistry to the optimization of the properties of this important protein molecule. Recently we described "ester insulin"--a novel form of insulin in which the f
Publikováno v:
Journal of the American Chemical Society. 133:18420-18432
Escherichia coli ribonucleotide reductase is an α2β2 complex that catalyzes the conversion of nucleotides to deoxynucleotides using a diferric tyrosyl radical (Y(122)(•)) cofactor in β2 to initiate catalysis in α2. Each turnover requires revers
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:
Jan Vávra, Filip Teplý, Lucie Bednárová, Petr Štěpánek, Ján Tarábek, Lubomír Pospíšil, Petr Slavíček, Helena Dlouhá, Magdaléna Hromadová
Publikováno v:
Journal of the American Chemical Society. 136(31)
Two-step redox switching in enantiopure helquat system [P-1](2+) ⇌ [P-1](•+) ⇌ [P-1](0) is demonstrated. The viologen-type electroactive unit embedded directly in the helical scaffold of 1 is responsible for the prominent chiroptical switching
Publikováno v:
Journal of the American Chemical Society. 119:12192-12200
The two available crystallographic structures of cobalamin dependent enzymes, the 27 kDa fragment of the methylcobalamin-dependent enzyme, methionine synthase, from Escherichia coli [Drennan, C. L. et al. Science 1994, 266, 1669] and the 5‘-deoxyad
Autor:
Robert G. Griffin, Sylwia Kacprzak, Brian Hoffman, Erin Artin, JoAnne Stubbe, Hendrik Zipse, Debora Marcela Martino, Nicholas Lees, Martin Kaupp, Gregory J. S. Lohman, Marina Bennati, Stanislaw F. Wnuk
Publikováno v:
Journal of the American Chemical Society
The Escherichia coli ribonucleotide reductase (RNR) catalyzes the conversion of nucleoside diphosphates to deoxynucleotides and requires a diferric-tyrosyl radical cofactor for catalysis. RNR is composed of a 1:1 complex of two homodimeric subunits:
Publikováno v:
Journal of the American Chemical Society. 123(25)
Concise syntheses of the Ergot alkaloids rugulovasine A (3a), rugulovasine B (3b), and setoclavine (2) have been completed by strategies that feature inter- and intramolecular vinylogous Mannich reactions as the key steps. Thus, the first synthesis o
Autor:
Don S. Martin, John W. Reishus
Publikováno v:
Journal of the American Chemical Society. 83:2457-2462
The acid hydrolysis of cis-STAPt(NH/sub 3/)/sub 2/Cl/sub 2/! was studied at 25 and 35 deg . For the first acid hydrolysis, cis-STAPt(NH/sub 3/)/sub 2/Cl! + H/sub 2/O yields cis-STAPt(NH/sub 3/)/sub 2/Cl(H/sub 2/O)!/sup +/ + Cl/sup -/ , the equilibriu