Zobrazeno 41 - 46
of 46
pro vyhledávání: '"35"'
Autor:
Geert van den Bogaart, Victor V. Krasnikov, J. Antoinette Killian, Sivaramakrishnan Ramadurai, Andrea Holt, Berend Poolman
Publikováno v:
Journal of the American Chemical Society, 131(35), 12650-12656. AMER CHEMICAL SOC
We measured the lateral mobility of integral membrane proteins reconstituted in giant unilamellar vesicles (GUVs), using fluorescence correlation spectroscopy. Receptor, channel, and transporter proteins with 1-36 transmembrane segments (lateral radi
Publikováno v:
Journal of the American Chemical Society. 125:14728-14732
The description of reaction regulation in enzymes responsible for activating and catalyzing small molecules (O(2), NO) requires identification of ligand movement into the binding site and out of the enzyme through specific channels and docking sites.
Publikováno v:
Journal of the American Chemical Society. 124:6449-6460
In the previous paper in this issue we have demonstrated that it is possible to measure the five different relaxation rates of a deuteron in (13)CH(2)D methyl groups of (13)C-labeled, fractionally deuterated proteins. The extensive set of data acquir
Publikováno v:
Journal of the American Chemical Society. 131(31)
A MerR family metalloregulatory protein CupR selectively responds to gold stress in Ralstonia metallidurans. A distorted trigonal geometry appears to be used by CupR to achieve the highly sensitive (K(d) approximately 10(-35) M) and selective recogni
Publikováno v:
Journal of the American Chemical Society. 127(23)
FosA is a manganese metalloglutathione transferase that confers resistance to the broad-spectrum antibiotic fosfomycin, which contains a phosphonate group. The active site of this enzyme consists of a high-spin Mn(2+) ion coordinated by endogenous li
Autor:
Richard N. Armstrong, Christopher L. Rife, Stoyan K. Smoukov, Joshua Telser, Brian M. Hoffman, Bryan A Bernat
Publikováno v:
Journal of the American Chemical Society. 124(10)
FosA is a manganese metalloglutathione transferase that confers resistance to the broad-spectrum antibiotic fosfomycin, (1R,2S)-epoxypropylphosphonic acid. The reaction catalyzed by FosA involves the attack by glutathione on fosfomycin to yield the p