Search Results - "Rumbley, J N"

Design and Evaluation of New Analogs of the Sweet Protein Brazzein by Walters, D. Eric, Cragin, Tiffany, Jin, Zheyuan, Rumbley, Jon N., Hellekant, Göran

“…We have previously modeled the interaction of the sweet protein brazzein with the extracellular domains of the sweet taste receptor. Here, we describe the…”
Get full text

Flash photolysis of the carbon monoxide compounds of wild-type and mutant variants of cytochrome bo from Escherichia coli by Brown, S, Rumbley, J N, Moody, A J, Thomas, J W, Gennis, R B, Rich, P R

“…The carbon monoxide compounds of the fully reduced and mixed valence forms of cytochrome bo from Escherichia coli were laser photolysed under anaerobic…”
Get more information

Ligand-binding properties and heterogeneity of cytochrome bo from Escherichia coli by Moody, A J, Rumbley, J N, Gennis, R B, Ingledew, W J, Rich, P R

“…Cyanide and formate induce spectral changes in E. coli cytochrome bo which are similar to those induced in bovine heart cytochrome-c oxidase (cytochrome aa3)…”
Get more information

Uncompetitive Substrate Inhibition and Noncompetitive Inhibition by 5-n-Undecyl-6-hydroxy-4,7-dioxobenzothiazole (UHDBT) and 2-n-Nonyl-4-hydroxyquinoline-N-oxide (NQNO) is Observed for the Cytochrome bo3 Complex:  Implications for a Q(H2)-Loop Proton Translocation Mechanism by MUSSER, Siegfried M., STOWELL, Michael H. B., LEE, Hung Kay, RUMBLEY, Jon N., CHAN, Sunney I.

“…The cytochrome bo3 ubiquinol oxidase complex from Escherichia coli contains two binding sites for ubiquinone(ol) (UQ(H2)). One of these binding sites, the…”
Get full text

Signal transmission between subunits in the hemoglobin T-state by Englander, J J, Rumbley, J N, Englander, S W

“…To study allosteric mechanism in hemoglobin, a hydrogen-exchange method was used to measure ligand-dependent changes in structural free energy at defined…”
Get full text

DNA hydrolysis by monoclonal anti-ssDNA autoantibody BV 04-01: Origins of catalytic activity by Gololobov, Gennady V., Rumbley, Catherine A., Rumbley, Jon N., Schourov, Dmitry V., Makarevich, Oksana I., Gabibov, Alexander G., Voss, Edward W., Scott Rodkey, L.

“…Monoclonal anti-DNA autoantibody BV 04-01 catalyzed hydrolysis of DNA in the presence of Mg2+ ions. DNA hydrolyzing activity was associated with BV 04-01 IgG,…”
Get full text

Flash photolysis of the carbon monoxide compounds of mutant and wild-type cytochrome bo from E. coli by Brown, S, Rumbley, J N, Gennis, R B, Rich, P R

Get more information

Interconversion of Fast and Slow Forms of Cytochrome bo from Escherichia coli by Moody, A. John, Cooper, Chris E, Gennis, Robert B, Rumbley, Jon N, Rich, Peter R

“…The fully oxidized fast form of cytochrome bo from Escherichia coli is shown to convert spontaneously to a slow form when stored at -20 degrees C in 50 mM…”
Get full text

CO recombination as a probe of the Fe/Cu binuclear centre of terminal protonmotive oxidases by Brown, S, Meunier, B, Rumbley, J N, Lemaire, C, Moody, A J, Lemarre, P, Blaiseau, P L, Madgwick, S A, Netter, P, Gennis, R B

Get more information

Cooperative Omega Loops in Cytochrome c: Role in Folding and Function by Krishna, Mallela M.G., Lin, Yan, Rumbley, Jon N., Walter Englander, S.

“…Hydrogen exchange experiments under slow exchange conditions show that an omega loop in cytochrome c (residues 40–57) acts as a cooperative unfolding/refolding…”
Get full text

Protein hydrogen exchange mechanism: Local fluctuations by Maity, Haripada, Lim, Woon Ki, Rumbley, Jon N., Englander, S. Walter

“…Experiments were done to study the dynamic structural motions that determine protein hydrogen exchange (HX) behavior. The replacement of a solvent‐exposed…”
Get full text

Recombinant Equine Cytochrome c in Escherichia coli: High-Level Expression, Characterization, and Folding and Assembly Mutants by Rumbley, Jon N, Hoang, Linh, Englander, S. Walter

“…To promote studies of cytochrome c (Cyt c) ranging from apoptosis to protein folding, a system for facile mutagenesis and high-level expression is desirable…”
Get full text

Submolecular cooperativity produces multi-state protein unfolding and refolding by Englander, S.Walter, Mayne, Leland, Rumbley, Jon N

“…Hydrogen exchange experiments show that cytochrome c and other proteins under native conditions reversibly unfold in a multi-step manner. The step from one…”
Get full text

Uncompetitive substrate inhibition and noncompetitive inhibition by 5-n-undecyl-6-hydroxy-4,7-dioxobenzothiazole (UHDBT) and 2-n-nonyl-4-hydroxyquinoline-N-oxide (NQNO) is observed for the cytochrome bo sub(3) complex: Implications for a Q(H sub(2))-loop proton translocation mechanism by Musser, S M, Stowell, MHB, Lee, H K, Rumbley, J N, Chan, SI

“…The cytochrome bo sub(3) ubiquinol oxidase complex from Escherichia coli contains two binding sites for ubiquinone(ol) (UQ(H sub(2))). One of these binding…”
Get full text

One-step purification of histidine-tagged cytochrome bo3 from Escherichia coli and demonstration that associated quinone is not required for the structural integrity of the oxidase by Rumbley, J N, Furlong Nickels, E, Gennis, R B

“…The cytochrome bo3 ubiquinol oxidase from Escherichia coli is a member of the heme-copper superfamily of proton-pumping respiratory oxidases. An improved…”
Get more information

The reaction of hydrogen peroxide with cytochrome bo from E. coli by Moody, A J, Rumbley, J N, Ingledew, W J, Gennis, R B, Rich, P R

Get more information