Search Results - "Pielak, G J"

Macromolecular Crowding in the Escherichia coli Periplasm Maintains α-Synuclein Disorder by McNulty, Brian C., Young, Gregory B., Pielak, Gary J.

“…The natively disordered protein α-synuclein is the primary component of Lewy bodies, the cellular hallmark of Parkinson's disease. Most studies of this protein…”
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Interactions between Yeast Iso-1-cytochrome c and Its Peroxidase by Pielak, Gary J, Wang, Xuming

“…Isothermal titration calorimetry was used to study the formation of 19 complexes involving yeast iso-1-ferricytochrome c (Cc) and ferricytochrome c peroxidase…”
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Baseline length and automated fitting of denaturation data by Allen, Devon L., Pielak, Gary J.

“…To understand relationships between protein sequence and stability, we often compare data from proteins that differ by the substitution of one amino acid…”
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Effects of Crowding by Mono-, Di-, and Tetrasaccharides on Cytochrome c−Cytochrome c Peroxidase Binding:  Comparing Experiment to Theory by Morar, Artemiza S, Wang, Xuming, Pielak, Gary J

“…In cells, protein−protein interactions occur in an environment that is crowded with other molecules, but in vitro studies are almost exclusively performed in…”
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Stability of yeast iso‐1‐ferricytochrome c as a function of pH and temperature by Cohen, David S., Pielak, Gary J.

“…Absorbance‐detected thermal denaturation studies of the C102T variant of Saccharomyces cerevisiae iso‐1‐ferricytochrome c were performed between pH 3 and 5…”
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FlgM Gains Structure in Living Cells by Dedmon, Matthew M., Patel, Chetan N., Young, Gregory B., Pielak, Gary J.

“…Intrinsically disordered proteins such as FlgM play important roles in biology, but little is known about their structure in cells. We use NMR to show that…”
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Solvent‐induced collapse of α‐synuclein and acid‐denatured cytochrome c by Morar, Artemiza S., Olteanu, Alina, Young, Gregory B., Pielak, Gary J.

“…The effects of solution conditions on protein collapse were studied by measuring the hydrodynamic radii of two unfolded proteins, α‐synuclein and…”
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Introduction of a disulfide bond into cytochrome c stabilizes a compact denatured state by Betz, Stephen F, Pielak, Gary J

“…We introduced a novel disulfide bond, modeled on that of bullfrog cytochrome c, into yeast iso-1-cytochrome c. The disulfide spontaneously forms upon…”
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Yeast cytochrome c with phenylalanine or tyrosine at position 87 transfers electrons to (zinc cytochrome c peroxidase)+ at a rate ten thousand times that of the serine-87 or glycine-87 variants by Liang, N, Pielak, G.J, Mauk, A.G, Smith, M, Hoffman, B.M

“…Of the many factors known to influence the rate of electron transfer between two metalloproteins, it is particularly difficult to assess the role of the…”
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Comparison of reduced and oxidized yeast iso-1-cytochrome c using proton paramagnetic shifts by Gao, Yuan, Boyd, Jonathan, Pielak, Gary J, Williams, Robert J. P

“…Dipolar paramagnetic shifts for protons of yeast iso-1-cytochrome c have been calculated by using an optimized g-tensor and the X-ray crystallographic…”
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Site-directed mutagenesis of cytochrome c shows that an invariant Phe is not essential for function by Pielak, Gary J, Mauk, A. Grant, Smith, Michael

“…Phenylalanine 87 of yeast iso-1-cytochrome c (Phe 82 in horse heart and bonito) is phylogenetically conserved and occurs near the surface of the protein. It…”
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Amide proton exchange rates of oxidized and reduced saccharomyces cerevisiae iso‐1‐cytochrome c by Marmorino, Jennifer L., Auld, Douglas S., Betz, Stephen F., Doyle, Donald F., Young, Gregory B., Pielak, Gary J.

“…Proton NMR spectroscopy was used to determine the rate constant, kobs, for exchange of labile protons in both oxidized (Fe(III)) and reduced (Fe(II))…”
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Regulation of interprotein electron transfer by residue 82 of yeast cytochrome c by Liang, N, Mauk, A.G, Pielak, G.J, Johnson, J.A, Smith, M, Hoffman, B.M

“…Yeast iso-1-cytochrome c (Cc) mutants have been constructed with Phe, Tyr, Gly, Ser, Leu, and Ile at position 82, each with Thr substituted for Cys at position…”
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Intracomplex electron transfer between ruthenium-65-cytochrome b5 and position-82 variants of yeast iso-1-cytochrome c by Willie, Anne, McLean, Mark, Liu, Rui Qin, Hilgen-Willis, Sharon, Saunders, Aleister J, Pielak, Gary J, Sligar, Stephen G, Durham, Bill, Millett, Francis

“…We tested the idea that the aromatic ring on the invariant residue Phe-82 in cytochrome c acts as an electron-transfer bridge between cytochrome c and…”
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Replacement of cysteine-107 of Saccharomyces cerevisiae iso-1-cytochrome c with threonine: improved stability of the mutant protein by Cutler, R L, Pielak, G J, Mauk, A G, Smith, M

“…Site-directed mutagenesis has been used to change the codon for cysteine-107 of Saccharomyces cerevisiae iso-1-cytochrome c to a threonine codon. The resulting…”
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Stability and apoptotic activity of recombinant human cytochrome c by Olteanu, Alina, Patel, Chetan N, Dedmon, Matthew M, Kennedy, Scott, Linhoff, Michael W, Minder, Camille M, Potts, Patrick R, Deshmukh, Mohanish, Pielak, Gary J

“…An efficient system for producing human cytochrome c variants is important to help us understand the roles of this protein in biological processes relevant to…”
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The function of the Saccharomyces cerevisiae iso-1-cytochrome c gene is independent of the codon at invariant residue Phe82 when the gene is present on a low-copy-number vector by Hilgen, S E, Pielak, G J

“…Phe82 is the most studied invariant residue of cytochrome c. However, the physiological relevance of amino acid substitutions at this position is unclear…”
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Role of phenylalanine-82 in yeast iso-1-cytochrome c and remote conformational changes induced by a serine residue at this position by Louie, Gordon V, Pielak, Gary J, Smith, Michael, Brayer, Gary D

“…A three-dimensional structural analysis of the reduced form of the Ser-82 mutant protein of yeast iso-1-cytochrome c has been completed to 2.8-A resolution…”
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Dramatic stabilization of ferricytochrome c upon reduction by Hilgen-Willis, S, Bowden, E F, Pielak, G J

“…By combining measurements of the free energy of denaturation of the C102T variant of Saccharomyces cerevisiae iso-1-ferricytochrome c with determination of the…”
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Polarity of disulfide bonds by Saunders, Aleister J., Young, Gregory B., Pielak, Gary J.

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