Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Deok Cheon Yeh"'
Publikováno v:
Biochemistry. 44:14055-14061
We describe here the solution NMR structures of two IgG binding domains with highly homologous sequences but different three-dimensional structures. The proteins, G311 and A219, are derived from the IgG binding domains of their wild-type counterparts
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 54:375-383
The solution structure of the acidic protein HI1450 from Haemophilus influenzae has been determined by NMR spectroscopy. HI1450 has homologues in ten other bacterial species including Escherichia coli, Vibrio cholerae, and Yersinia pestis but there a
Autor:
Gerd N. La Mar, Karine Auclair, Anbanandam Asokan, Paul R. Ortiz de Montellano, Bryan Espiritu, Deok Cheon Yeh
Publikováno v:
Journal of Biological Chemistry. 276:15676-15687
The majority of the active site residues of cyanide-inhibited, substrate-bound human heme oxygenase have been assigned on the basis of two-dimensional NMR using the crystal structure of the water-ligated substrate complex as a guide (Schuller, D. J.,
Publikováno v:
Biochemistry. 39:1389-1399
The globin from the cyanobacterium Nostoc commune, abbreviated GlbN, which appears to serve as a part of a terminal oxidase rather than as a respiratory pigment, displays relatively normal O2 binding properties, despite the highly abbreviated polypep
Publikováno v:
Journal of the American Chemical Society. 121:208-217
Comprehensive 1H NMR assignments of the heme cavity proton resonances of sperm whale metmyoglobin cyanide have provided the dipolar shifts for nonligated residues which, together with the crystal c...
The solution structure of the 154-residue conserved hypothetical protein HI0004 has been determined using multidimensional heteronuclear NMR spectroscopy. HI0004 has sequence homologs in many organisms ranging from bacteria to humans and is believed
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b5f8454877bef29887354a0fb974ec1d
https://europepmc.org/articles/PMC2253416/
https://europepmc.org/articles/PMC2253416/
Publikováno v:
Journal of biomolecular NMR. 29(2)
Autor:
Eugene Melamud, Edward Eisenstein, Osnat Herzberg, Aleksandra Tempczyk, Narmada Thanki, Galina Obmolova, Maria Tordova, Nicklas Bonander, Deok Cheon Yeh, John Moult, James F. Parsons, Wojciech W. Krajewski, Hong Zhang, Kap Lim, Jane E. Ladner, Gary L. Gilliland, John Orban, J. Toedt, Andrew Howard, Prasad T. Reddy, Alexey Teplyakov, C. V. Rao, Kui Huang, Lisa Parsons, Zhong Li, Kathryn E. Fisher
Publikováno v:
Europe PubMed Central
The three-dimensional structures of Haemophilus influenzae proteins whose biological functions are unknown are being determined as part of a structural genomics project to ask whether structural information can assist in assigning the functions of pr
Publikováno v:
Journal of Biomolecular NMR. 29:213-214
Publikováno v:
Journal of Biomolecular NMR. 29:101-102