Zobrazeno 1 - 10
of 28
pro vyhledávání: '"William B. O'Dell"'
Autor:
Tsega L. Solomon, Kinlin Chao, Genevieve Gingras, Yves Aubin, William B. O’Dell, John P. Marino, Robert G. Brinson
Publikováno v:
Biomolecular NMR Assignments. 17:75-81
Publikováno v:
Chemical science. 13(45)
Metalloproteins perform a diverse array of redox-related reactions facilitated by the increased chemical functionality afforded by their metallocofactors. Lytic polysaccharide monooxygenases (LPMOs) are a class of copper-dependent enzymes that are re
Autor:
Gloria E. O. Borgstahl, William B. O’Dell, Martin Egli, Jan F. Kern, Andrey Kovalevsky, Jiao Y. Y. Lin, Dean Myles, Mark A. Wilson, Wen Zhang, Petrus Zwart, Leighton Coates
Publikováno v:
The Review of scientific instruments. 93(6)
Revealing the positions of all the atoms in large macromolecules is powerful but only possible with neutron macromolecular crystallography (NMC). Neutrons provide a sensitive and gentle probe for the direct detection of protonation states at near-phy
Autor:
Colleen McClung, William B. O'Dell, Christina Bergonzo, Zvi Kelman, Erik M. Leith, Robert G. Brinson, Mehmet Berkmen, Na Ke
Publikováno v:
Journal of Biological Chemistry. 294:18046-18056
Monoclonal antibodies (mAbs) represent an important platform for the development of biotherapeutic products. Most mAbs are produced in mammalian cells, but several mAbs are made in Escherichia coli, including therapeutic fragments. The NISTmAb is a w
Autor:
Zvi Kelman, William B. O'Dell
Publikováno v:
Methods in enzymology. 659
Autor:
Prasad T, Reddy, William B, O'Dell
Publikováno v:
Methods in enzymology. 659
A protocol for increasing soluble protein expression by fusing the chaperone GroEL apical domain with a gene of interest is described herein. GroEL apical domain, the minichaperone that functions independently of GroES and ATP in protein folding, is
Autor:
William B. O’Dell, Zvi Kelman
Publikováno v:
Methods in enzymology. 660
Publikováno v:
Acta Crystallogr F Struct Biol Commun
Lytic polysaccharide monooxygenases (LPMOs) are copper-center enzymes that are involved in the oxidative cleavage of the glycosidic bond in crystalline cellulose and other polysaccharides. The LPMO reaction is initiated by the addition of a reductant
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7953e0c19a1ab49b14cf33fa15501ac2
https://europepmc.org/articles/PMC8034432/
https://europepmc.org/articles/PMC8034432/
Autor:
Prasad T. Reddy, William B. O'Dell
Publikováno v:
Recombinant Protein Expression: Prokaryotic Hosts and Cell-Free Systems ISBN: 9780323901468
A protocol for increasing soluble protein expression by fusing the chaperone GroEL apical domain with a gene of interest is described herein. GroEL apical domain, the minichaperone that functions independently of GroES and ATP in protein folding, is
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d822cc5dfe16d986df302a26867bc3b3
https://doi.org/10.1016/bs.mie.2021.09.002
https://doi.org/10.1016/bs.mie.2021.09.002
Publikováno v:
J Bacteriol
Replicative DNA helicases are essential cellular enzymes that unwind duplex DNA in front of the replication fork during chromosomal DNA replication. Replicative helicases were discovered, beginning in the 1970s, in bacteria, bacteriophages, viruses,