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Global analysis of non-specific protein-nucleic interactions by sedimentation equilibrium

Global analysis of non-specific protein-nucleic interactions by sedimentation equilibrium

http://www.wikidata.org/entity/Q34076342

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Structural basis for DNA-mediated allosteric regulation facilitated by the AAA+ module of Lon protease Analytical Ultracentrifugation as a Tool to Study Nonspecific Protein-DNA Interactions The crystal structure and small-angle X-ray analysis of CsdL/TcdA reveal a new tRNA binding motif in the MoeB/E1 superfamily In vivo kinetics of U4/U6·U5 tri-snRNP formation in Cajal bodies.Using Lamm-Equation modeling of sedimentation velocity data to determine the kinetic and thermodynamic properties of macromolecular interactions.Analysis of PKR activation using analytical ultracentrifugation MeCP2 binds cooperatively to its substrate and competes with histone H1 for chromatin binding sites Ionic interactions between PRNA and P protein in Bacillus subtilis RNase P characterized using a magnetocapture-based assay The role of human Dicer-dsRBD in processing small regulatory RNAs Determination of protein complex stoichiometry through multisignal sedimentation velocity experiments.Disconnected Interacting Protein 1 binds with high affinity to pre-tRNA and ADAT.Analysis of high-affinity binding of protein kinase R to double-stranded RNA Mechanism of PKR Activation by dsRNA.Domain stabilities in protein kinase R (PKR): evidence for weak interdomain interactions RNA dimerization promotes PKR dimerization and activation.Domain interactions in adenovirus VAI RNA mediate high-affinity PKR binding.Histidine-tag-directed chromophores for tracer analyses in the analytical ultracentrifuge Analysis of PKR-RNA interactions by sedimentation velocity 5'-triphosphate-dependent activation of PKR by RNAs with short stem-loops.Resolving the contributions of two cooperative mechanisms to the DNA binding of AGT.Electrophoretic mobility shift assay (EMSA) for detecting protein-nucleic acid interactions.Interaction of PKR with single-stranded RNA Functional energetic landscape in the allosteric regulation of muscle pyruvate kinase. 1. Calorimetric study Functional energetic landscape in the allosteric regulation of muscle pyruvate kinase. 2. Fluorescence study.

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Global analysis of non-specific protein-nucleic interactions by sedimentation equilibrium

http://www.wikidata.org/entity/Q34076342

description

2004 nî lūn-bûn

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2004 թուականի Մարտին հրատարակուած գիտական յօդուած

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2004 թվականի մարտին հրատարակված գիտական հոդված

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2004年の論文

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2004年論文

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2004年論文

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2004年論文

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2004年論文

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2004年論文

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2004年论文

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Global analysis of non-specific protein-nucleic interactions by sedimentation equilibrium

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Global analysis of non-specific protein-nucleic interactions by sedimentation equilibrium

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Global analysis of non-specific protein-nucleic interactions by sedimentation equilibrium

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Global analysis of non-specific protein-nucleic interactions by sedimentation equilibrium

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Global analysis of non-specific protein-nucleic interactions by sedimentation equilibrium

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Global analysis of non-specific protein-nucleic interactions by sedimentation equilibrium

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Global analysis of non-specific protein-nucleic interactions by sedimentation equilibrium

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Global analysis of non-specific protein-nucleic interactions by sedimentation equilibrium

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Global analysis of non-specific protein-nucleic interactions by sedimentation equilibrium

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J.BPC.2003.10.033

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Biophysical Chemistry

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Global analysis of non-specific protein-nucleic interactions by sedimentation equilibrium

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James L Cole

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Jason W Ucci

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P2860

A gel electrophoresis method for quantifying the binding of proteins to specific DNA regions: application to components of the Escherichia coli lactose operon regulatory system

Equilibria and kinetics of lac repressor-operator interactions by polyacrylamide gel electrophoresis

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Analytical ultracentrifugation studies of translin: analysis of protein-DNA interactions using a single-stranded fluorogenic oligonucleotide

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Consequences of the non-specific binding of a protein to a linear polymer: reconciliation of stoichiometric and equilibrium titration data for the thrombin-heparin interaction.

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Analytic binding isotherms describing competitive interactions of a protein ligand with specific and nonspecific sites on the same DNA oligomer.

Interaction of the DNA-binding domain of Drosophila heat shock factor with its cognate DNA site: a thermodynamic analysis using analytical ultracentrifugation

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1-3

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