Search Results - "Horowitz, Paul M"

High Hydrostatic Pressure Can Reverse Aggregation of Protein Folding Intermediates and Facilitate Acquisition of Native Structure by Gorovits, Boris M, Horowitz, Paul M

“…The present work demonstrates that high hydrostatic pressure can increase protein folding by reducing nonspecific aggregation. Protein aggregation is one of…”
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Single synonymous codon substitution eliminates pausing during chloramphenicol acetyl transferase synthesis on Escherichia coli ribosomes in vitro by Ramachandiran, Vasanthi, Kramer, Gisela, Horowitz, Paul M, Hardesty, Boyd

“…The coding sequence for chloramphenicol acetyl transferase (CAT) contains several rare codons; three of them are ATA encoding isoleucine in positions 13, 84…”
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Active Rhodanese Lacking Nonessential Sulfhydryl Groups Contains an Unstable C-terminal Domain and Can Be Bound, Inactivated, and Reactivated by GroEL by Ybarra, Jesse, Bhattacharyya, Anusri Mitra, Panda, Markandeswar, Horowitz, Paul M.

“…Mutation of all nonessential cysteine residues in rhodanese turns the enzyme into a form (C3S) that is fully active but less stable than wild type (WT). This…”
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GroES in the asymmetric GroEL14–GroES7 complex exchanges via an associative mechanism by Horowitz, P M, Lorimer, G H, Ybarra, J

“…The interaction of the chaperonin GroEL 14 with its cochaperonin GroES 7 is dynamic, involving stable, asymmetric 1:1 complexes (GroES 7 ⋅GroEL 7 –GroEL 7 )…”
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Dissociation of the Single-Ring Chaperonin GroEL by High Hydrostatic Pressure by Panda, Markandeswar, Ybarra, Jesse, Horowitz, Paul M

“…We investigated the dissociation of single-ring heptameric GroEL (SR1) by high hydrostatic pressure in the range of 1−2.5 kbar. The kinetics of the…”
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The Binding of Bis-ANS to the Isolated GroEL Apical Domain Fragment Induces the Formation of a Folding Intermediate with Increased Hydrophobic Surface Not Observed in Tetradecameric GroEL by Smoot, Alison L, Panda, Markandeswar, Brazil, Bill T, Buckle, Ashley M, Fersht, Alan R, Horowitz, Paul M

“…The extent of hydrophobic exposure upon bis-ANS binding to the functional apical domain fragment of GroEL, or minichaperone (residues 191−345), was…”
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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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Conformational Heterogeneity Is Revealed in the Dissociation of the Oligomeric Chaperonin GroEL by High Hydrostatic Pressure by Panda, Markandeswar, Horowitz, Paul M

“…We investigated the dissociation of tetradecameric GroEL by high hydrostatic pressure in the range of 1−2.5 kbar. Kinetics of the dissociation of GroEL in the…”
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High Hydrostatic Pressure Can Probe the Effects of Functionally Related Ligands on the Quaternary Structures of the Chaperonins GroEL and GroES by Panda, Markandeswar, Ybarra, Jesse, Horowitz, Paul M.

“…We investigated the effects of high hydrostatic pressure in the range of 1–3 kilobars on tetradecameric GroEL, heptameric GroES, and the GroEL-GroES complex…”
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Productive and Nonproductive Intermediates in the Folding of Denatured Rhodanese by Panda, M, Gorovits, B M, Horowitz, P M

“…The competition between protein aggregation and folding has been investigated using rhodanese (thiosulfate:cyanide sulfurtransferase, EC 2.8.1.1 ) as a model…”
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Active rhodanese lacking nonessential sulfhydryl groups has increased hydrophobic exposure not observed in wild-type enzyme by Kaur, Yogeet, Ybarra, Jesse, Horowitz, Paul M

“…Mutation of all nonessential cysteine residues to serines in rhodanese turns the enzyme into a form (C3S) that is fully active but less stable than wild type…”
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Rhodanese Can Partially Refold in Its GroEL−GroES−ADP Complex and Can Be Released to Give a Homogeneous Product by Bhattacharyya, Anusri Mitra, Horowitz, Paul M

“…Molecular chaperones GroEL and GroES facilitate reactivation of denatured rhodanese which folds poorly unless the process is assisted. The present work tests…”
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The Aggregation State of Rhodanese during Folding Influences the Ability of GroEL to Assist Reactivation by Bhattacharyya, A M, Horowitz, P M

“…The in vitro folding of rhodanese involves a competition between formation of properly folded enzyme and off-pathway inactive species. Co-solvents like…”
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The molecular chaperone DnaK is not recruited to translating ribosomes that lack trigger factor by Kramer, Gisela, Ramachandiran, Vasanthi, Horowitz, Paul M, Hardesty, Boyd

“…The molecular chaperone DnaK and trigger factor (TF), a ribosome-associated protein with folding activity, have been implicated in assisting nascent…”
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Isolation and Characterization of Rhodanese Intermediates during Thermal Inactivation and Their Implications for the Mechanism of Protein Aggregation by Bhattacharyya, Anusri Mitra, Horowitz, Paul M

“…The initial steps of heat-induced inactivation and aggregation of the enzyme rhodanese have been studied and found to involve the early formation of modified…”
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GroEL and GroES increase the specific enzymic activity of newly-synthesized rhodanese if present during in vitro transcription/translation by Tsalkova, Tamara, Zardeneta, Gustavo, Kudlicki, Wieslaw, Kramer, Gisela, Horowitz, Paul M, Hardesty, Boyd

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Prodan fluorescence mimics the GroEL folding cycle by Kaur, Yogeet, Horowitz, Paul M

“…The non-covalent fluorescent probe 6-propionyl-2-(dimethylamino) naphthalene sulfonate (prodan) binds to hydrophobic surfaces exposed on the surface of GroEL…”
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Activation parameters for the spontaneous and pressure-induced phases of the dissociation of single-ring GroEL (SR1) chaperonin by Panda, Markandeswar, Horowitz, Paul M

“…We investigated the dissociation of single-ring heptameric GroEL (SR1) by high hydrostatic pressure in the range 0.5-3.0 kbar. The kinetics were studied as a…”
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Hydrophobic Surfaces That Are Hidden in Chaperonin Cpn60 Can Be Exposed by Formation of Assembly-Competent Monomers or by Ionic Perturbation of the Oligomer (∗) by Horowitz, Paul M., Hua, Su, Gibbons, Don L.

“…The oligomeric form (14-mer) of the chaperonin protein, Cpn60 (GroEL) from Eschericia coli, displays restricted hydrophobic surfaces and binds tightly one to…”
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Refolding and Reassembly of Active Chaperonin GroEL After Denaturation (∗) by Ybarra, Jesse, Horowitz, Paul M.

“…Conditions are reported that, for the first time, permit the folding and assembly of active chaperonin, GroEL, following denaturation in 8 M urea. The folding…”
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