Search Results - "Kurzban, Gary"

Noncooperativity of Biotin Binding to Tetrameric Streptavidin by Jones, M. Lisa, Kurzban, Gary P

“…Streptavidin tetramers have been separated according to their biotin content by anion exchange chromatography. Biotin-free and biotin-saturated streptavidin…”
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Core Sugar Residues of the N-Linked Oligosaccharides of Russell's Viper Venom Factor X-Activator Maintain Functionally Active Polypeptide Structure by Gowda, D. Channe, Jackson, Craig M, Kurzban, Gary P, McPhie, Peter, Davidson, Eugene A

“…We previously showed that the factor X activator of Russell's viper venom (RVV-X) contains six N-linked oligosaccharide chains:  four in the heavy chain and…”
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Cystalysin, a 46-kDa L-Cysteine Desulfhydrase from Treponema denticola: Biochemical and Biophysical Characterization by Chu, Lianrui, Ebersole, Jeffery L., Kurzban, Gary P., Holt, Stanley C.

“…A 46-kDa hemolytic protein referred to as cystalysin, from Treponema denticola ATCC 35404, was characterized and overexpressed in Escherichia coli LC-67…”
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Shielding of tryptophan residues of avidin by the binding of biotin by Kurzban, Gary P, Gitlin, Gerry, Bayer, Edward A, Wilchek, Meir, Horowitz, Paul M

“…The binding of biotin to tetrameric avidin changes the environment of tryptophan residues. Binding reduces the total tryptophan fluorescence by 34%, shifts the…”
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In Vitro Antimalarial Activity of Chalcones and Their Derivatives by Li, Rongshi, Kenyon, George L, Cohen, Fred E, Chen, Xiaowu, Gong, Baoqing, Dominguez, Jose N, Davidson, Eugene, Kurzban, Gary, Miller, Robert E, Nuzum, Edwin O, Rosenthal, Philip J, McKerrow, James H

“…A series of chalcones and their derivatives have been synthesized and identified as novel potential antimalarials using both molecular modeling and in vitro…”
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Structure-based design of parasitic protease inhibitors by Li, Rongshi, Chen, Xiaowu, Gong, Baoqing, Selzer, Paul M., Li, Zhe, Davidson, Eugene, Kurzban, Gary, Miller, Robert E., Nuzum, Edwin O., McKerrow, James H., Fletterick, Robert J., Gillmor, Sarah A., Craik, Charles S., Kuntz, Irwin D., Cohen, Fred E., Kenyon, George L.

“…To streamline the preclinical phase of pharmaceutical development, we have explored the utility of structural data on the molecular target and synergy between…”
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Giant polypeptides of skeletal muscle titin: sedimentation equilibrium in guanidine hydrochloride by Kurzban, G P, Wang, K

“…Titin has been purified from rabbit skeletal myofibrils in guanidine hydrochloride by gel filtration on Sephacryl S-1000. The sedimentation coefficients of…”
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The quaternary structure of streptavidin in urea by KURZBAN, G. P, BAYER, E. A, WILCHEK, M, HOROWITZ, P. M

“…We report on the interactions of urea and guanidinium salts with streptavidin. Gel filtration chromatography in 0, 4, 6, and 7 M urea indicates that the…”
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Purification of bovine liver rhodanese by low-pH column chromatography by Kurzban, G P, Horowitz, P M

“…We report a purification of bovine liver rhodanese (thiosulfate:cyanide sulfurtransferase, EC 2.8.1.1) using column chromatography under conditions that take…”
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NADPH-cytochrome P-450 reductase. Physical properties and redox behavior in the absence of the FAD moiety by KURZBAN, G. P, HOWARTH, J, PALMER, G, STROBEL, H. W

“…NADPH-cytochrome P-450 reductase contains one molecule each of FMN and FAD. The FAD moiety has been selectively removed, producing the FMN reductase. The FMN…”
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PREPARATION AND CHARACTERIZATION OF FAD DEPENDENT NADPH CYTOCHROME P-450 REDUCTASE (FLAVOPROTEINS, APOFLAVOPROTEIN) by KURZBAN, GARY PAUL

“…NADPH cytochrome P-450 reductase releases FMN and FAD upon dilution into slightly acidic potassium bromide. The flavins are released with positive…”
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Recombinant bovine rhodanese: purification and comparison with bovine liver rhodanese by Miller, D M, Kurzban, G P, Mendoza, J A, Chirgwin, J M, Hardies, S C, Horowitz, P M

“…Recombinant bovine rhodanese (thiosulfate: cyanide sulfurtransferase, EC 2.8.1.1) has been purified to homogeneity from Escherichia coli BL21(DE3) by…”
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Cytochromes P-450 and the activation and inactivation of mutagens and carcinogens by Strobel, H W, Fang, W F, Takazawa, R S, Stralka, D J, Newaz, S N, Kurzban, G P, Nelson, D R, Beyer, R S

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Biotin binding changes the conformation and decreases tryptophan accessibility of streptavidin by Kurzban, G P, Gitlin, G, Bayer, E A, Wilchek, M, Horowitz, P M

“…Biotin binding reduces the tryptophan fluorescence emissions of streptavidin by 39%, blue shifts the emission peak from 333 to 329 nm, and reduces the…”
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