Zobrazeno 1 - 10
of 12
pro vyhledávání: '"35"'
Publikováno v:
Journal of the American Chemical Society. 141:10821-10829
High fidelity human mitochondrial DNA polymerase (Pol γ) contains two active sites, a DNA polymerization site (pol) and a 3′−5′ exonuclease site (exo) for proofreading. Although separated by 35 Å, coordination between the pol and exo sites is
Publikováno v:
Journal of the American Chemical Society. 140:15744-15752
Class Ia ribonucleotide reductase (RNR) of Escherichia coli contains an unusually stable tyrosyl radical cofactor in the β2 subunit (Y122•) necessary for nucleotide reductase activity. Upon binding the cognate α2 subunit, loaded with nucleoside d
Autor:
Brandon Q. Mercado, Scott J. Miller, Nadia C. Abascal, Eric K. Paulson, Anthony J. Metrano, Anna E. Hurtley
Publikováno v:
Journal of the American Chemical Society
X-ray crystallography has been applied to the structural analysis of a series of tetrapeptides that were previously assessed for catalytic activity in an atroposelective bromination reaction. Common to the series is a central Pro-Xaa sequence, where
Publikováno v:
Journal of the American Chemical Society, vol 137, iss 35
Optical modulation of proteins provides superior spatiotemporal resolution for understanding biological processes, and photoswitches built on light-sensitive proteins have been significantly advancing neuronal and cellular studies. Small molecule pho
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:
Mohammad R. Seyedsayamdost, Tomislav Argirević, JoAnne Stubbe, Ellen Catherine Minnihan, Marina Bennati
Publikováno v:
Journal of the American Chemical Society
E. coli ribonucleotide reductase (RNR) catalyzes the conversion of nucleotides to deoxynucleotides, a process that requires long-range radical transfer over 35 A from a tyrosyl radical (Y(122)*) within the beta2 subunit to a cysteine residue (C(439))
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, 125(35), 10570-10579. AMER CHEMICAL SOC
The binding of a series of p-alkylbenzamidinium chloride inhibitors to the serine proteinase trypsin over a range of temperatures has been studied using isothermal titration (micro)calorimetry and molecular dynamics simulation techniques. The inhibit
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. 125(47)
Conformational changes occurring on the microsecond-millisecond time scale in basic pancreatic trypsin inhibitor (BPTI) are investigated using nuclear magnetic resonance spectroscopy. The rczz CPMG experiment (Wang, C.; Grey, M. J.; Palmer, A. G. J.