Zobrazeno 1 - 10
of 68
pro vyhledávání: '"David W. Hoffman"'
Autor:
David W. Hoffman, Cornelia Rasmussen
Publikováno v:
Analytical Chemistry. 94:5240-5247
Autor:
Cornelia Rasmussen, David W. Hoffman
Publikováno v:
Analytical chemistry. 94(43)
We introduce a novel nuclear magnetic resonance (NMR) tool for determining position-specific carbon (
Autor:
David W. Hoffman, Cornelia Rasmussen
Publikováno v:
Amino Acids. 52:955-964
Carbon stable isotope analysis can provide information about the origin and synthetic pathways that produce organic molecules, with applications in chemical, medical and (bio)geochemical sciences. The 13C/12C isotope ratios of organics such as amino
Autor:
Cornelia, Rasmussen, David W, Hoffman
Publikováno v:
Amino acids. 52(6-7)
Carbon stable isotope analysis can provide information about the origin and synthetic pathways that produce organic molecules, with applications in chemical, medical and (bio)geochemical sciences. The
Publikováno v:
Archives of Biochemistry and Biophysics. 537:113-124
Methylibium petroleiphilum strain PM1 uses various petroleum products including the fuel additive methyl tert-butyl ether and straight chain and aromatic hydrocarbons as sole carbon and energy sources. It has two operons, dmpI and dmpII, that code fo
Autor:
Jianting Zheng, Borries Demeler, David W. Hoffman, Adrian T. Keatinge-Clay, Christopher D. Fage
Publikováno v:
ACS Chemical Biology. 8:1263-1270
The dimerization of multimodular polyketide synthases is essential for their function. Motifs that supplement the contacts made by dimeric polyketide synthase enzymes have previously been characterized outside the boundaries of modules, at the N- and
Publikováno v:
Biochemistry. 48:12202-12212
The RNA recognition motif (or RRM) is a ubiquitous RNA-binding module present in approximately two percent of the proteins encoded in the human genome. This work characterizes an expanded RRM, which is present in the Drosophila Bruno protein, and tar
Autor:
David W. Hoffman, Wei Li
Publikováno v:
Protein Science. 10:2426-2438
Translation initiation factor 1A (aIF-1A) from the archaeon Methanococcus jannaschii was expressed in Escherichia coli, purified, and characterized in terms of its structure and dynamics using multidimensional NMR methods. The protein was found to be
Autor:
Jennifer H. Sadow, Anirvan Dutt-Chaudhuri, Angeline Lyon, Jon D. Robertus, Karen S. Browning, David W. Hoffman, Simrit Dhaliwal, Arthur F. Monzingo
Publikováno v:
Plant Physiology. 143:1504-1518
Eukaryotic translation initiation factor-4E (eIF4E) recognizes and binds the m(7) guanosine nucleotide at the 5' end of eukaryotic messenger RNAs; this protein-RNA interaction is an essential step in the initiation of protein synthesis. The structure
Publikováno v:
Journal of the American Chemical Society. 129:1304-1311
NMR spectroscopy was used to explore the sequence-specific interaction of DNA with a new threading bisintercalator (C1) consisting of two intercalating 1,4,5,8-naphthalenetetracarboxylic diimide (NDI) units connected by a rigid, tricyclic spiro linke