Zobrazeno 81 - 90
of 121
pro vyhledávání: '"35"'
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. 133(34)
Concise and protecting-group-free total syntheses of the marine oxylipins hybridalactone (1) and three members of the ecklonialactone family (2-4) were developed. They deliver these targets in optically pure form in 14 or 13 steps, respectively, in t
Autor:
Takao Saito, Kiyoto Hori, Noboru Sayo, Noriyoshi Arai, Kazuhiko Hiratsuka-shi Matsumura, Takeshi Ohkuma
Publikováno v:
Journal of the American Chemical Society. 133(28)
A novel ruthenabicyclic complex with base shows excellent catalytic activity in the asymmetric hydrogenation of ketones. The turnover frequency of the hydrogenation of acetophenone reaches about 35 000 min–1 in the best case, affording 1-phenyletha
Publikováno v:
Journal of the American Chemical Society. 115:2260-2267
An efficient and convenient synthetic route to glycosyl phosphites and phosphates has been developed that uses dibenzyl N,N-diethylphosphoramidite as a phosphitylating reagent. Glycosyl phosphites and phosphates of 2-acetamido-2-deoxy-D-galactose (Ga
Publikováno v:
Journal of the American Chemical Society. 132(43)
Escherichia coli ribonucleotide reductase is an α2β2 complex that catalyzes the conversion of nucleotides to deoxynucleotides and requires a diferric-tyrosyl radical (Y(•)) cofactor to initiate catalysis. The initiation process requires long-rang
Publikováno v:
Journal of the American Chemical Society. 132(24)
E. coli ribonucleotide reductase catalyzes the reduction of nucleoside 5'-diphosphates into 2'-deoxynucleotides and is composed of two subunits: alpha2 and beta2. During turnover, a stable tyrosyl radical (Y*) at Y(122)-beta2 reversibly oxidizes C(43
Autor:
Isabel Saura-Llamas, John A. Gladysz
Publikováno v:
Journal of the American Chemical Society. 114:2136-2144
Diastereomerically pure secondary alcohols epimerize to mixtures of diasteromers in C{sub 6}H{sub 5}R at 65-90 {degrees}C in the presence of 10 mol% ({eta}{sup 5}C{sub 5}R{sub 5})Re(NO)(PPh{sub 3})(OCH{sub 3}) (1; R = H, Me). The methoxide ligand of
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. 131(3)
Unlike most ordered molecular systems, globular proteins exhibit a temperature of maximum stability, implying that the structure can be disrupted by cooling. This cold denaturation phenomenon is usually linked to the temperature-dependent hydrophobic
Publikováno v:
Journal of the American Chemical Society. 112:6768-6771
A molecular dynamics (MD) simulation was performed on the hydrated decapeptide Ala 10 .550H 2 O under periodic boundary conditions. The initial configuration of the peptide was a canonical right-handed α-helix. Over the course of the MD trajectory,