Quantifying internal friction in unfolded and intrinsically disordered proteins with single-molecule spectroscopy. - Wikidata - wikimedia - TriplyDB

Quantifying internal friction in unfolded and intrinsically disordered proteins with single-molecule spectroscopy.

Quantifying internal friction in unfolded and intrinsically disordered proteins with single-molecule spectroscopy.

http://www.wikidata.org/entity/Q36398007

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Insights into Coupled Folding and Binding Mechanisms from Kinetic Studies Relating sequence encoded information to form and function of intrinsically disordered proteins Detection of correlated conformational fluctuations in intrinsically disordered proteins through paramagnetic relaxation interference.Single-molecule FRET of protein structure and dynamics - a primer.Average conformations determined from PRE data provide high-resolution maps of transient tertiary interactions in disordered proteins.Understanding the mechanism of proteasome 20S core particle gating.Single-molecule fluorescence probes dynamics of barrier crossing.Discriminating binding mechanisms of an intrinsically disordered protein via a multi-state coarse-grained model.Theoretical and computational validation of the Kuhn barrier friction mechanism in unfolded proteins.Hamiltonian Switch Metropolis Monte Carlo Simulations for Improved Conformational Sampling of Intrinsically Disordered Regions Tethered to Ordered Domains of Proteins.Molecular origins of internal friction effects on protein-folding rates.Fast single-molecule FRET spectroscopy: theory and experiment Single-molecule spectroscopy reveals chaperone-mediated expansion of substrate protein.Balanced Protein-Water Interactions Improve Properties of Disordered Proteins and Non-Specific Protein Association Single molecule unfolding and stretching of protein domains inside a solid-state nanopore by electric field.Role of denatured-state properties in chaperonin action probed by single-molecule spectroscopy A disorder-induced domino-like destabilization mechanism governs the folding and functional dynamics of the repeat protein IκBα Probing protein disorder and complexity at single-molecule resolution.Dependence of internal friction on folding mechanism.Quantifying the role of chaperones in protein translocation by computational modeling.Native contact density and nonnative hydrophobic effects in the folding of bacterial immunity proteins.Extracting intrinsic dynamic parameters of biomolecular folding from single-molecule force spectroscopy experiments.Quantitative interpretation of FRET experiments via molecular simulation: force field and validation.Reconstructing folding energy landscapes from splitting probability analysis of single-molecule trajectories.Slowdown of Interhelical Motions Induces a Glass Transition in RNA Protein misfolding occurs by slow diffusion across multiple barriers in a rough energy landscape.Polymer scaling laws of unfolded and intrinsically disordered proteins quantified with single-molecule spectroscopy Localizing internal friction along the reaction coordinate of protein folding by combining ensemble and single-molecule fluorescence spectroscopy Load-dependent destabilization of the γ-rotor shaft in FOF1 ATP synthase revealed by hydrogen/deuterium-exchange mass spectrometry.Elasticity, structure, and relaxation of extended proteins under force.Microsecond folding experiments and simulations: a match is made.Sequence and temperature dependence of the end-to-end collision dynamics of single-stranded DNA Infrared and Fluorescence Assessment of Protein Dynamics: From Folding to Function.Simple method to enhance the photostability of the fluorescence reporter R6G for prolonged single-molecule studies.A quantitative measure for protein conformational heterogeneity Meandering Down the Energy Landscape of Protein Folding: Are We There Yet?Single-Molecule Analysis of Cytochrome c Folding by Monitoring the Lifetime of an Attached Fluorescent Probe.How kinetics within the unfolded state affects protein folding: an analysis based on markov state models and an ultra-long MD trajectory Comprehensive structural and dynamical view of an unfolded protein from the combination of single-molecule FRET, NMR, and SAXS.Folding of a large protein at high structural resolution.

P2860

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P2860

Quantifying internal friction in unfolded and intrinsically disordered proteins with single-molecule spectroscopy.

http://www.wikidata.org/entity/Q36398007

description

2012 nî lūn-bûn

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2012年の論文

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2012年学术文章

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2012年学术文章

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2012年学术文章

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2012年学术文章

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2012年学术文章

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2012年學術文章

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2012年學術文章

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2012年學術文章

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name

Quantifying internal friction ...... single-molecule spectroscopy.

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Quantifying internal friction ...... single-molecule spectroscopy.

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type

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Quantifying internal friction ...... single-molecule spectroscopy.

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Quantifying internal friction ...... single-molecule spectroscopy.

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Quantifying internal friction ...... single-molecule spectroscopy.

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Quantifying internal friction ...... single-molecule spectroscopy.

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PNAS.1117368109

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Proceedings of the National Academy of Sciences of the United States of America

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Quantifying internal friction ...... h single-molecule spectroscopy

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P2093

Armin Hoffmann

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Brigitte Buchli

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Daniel Nettels

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Dmitrii E Makarov

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Everett A Lipman

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Ryan R Cheng

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Shawn H Pfeil

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Sonja Müller-Späth

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P2860

Function and structure of inherently disordered proteins

Funnels, pathways, and the energy landscape of protein folding: a synthesis

Mapping protein collapse with single-molecule fluorescence and kinetic synchrotron radiation circular dichroism spectroscopy.

Experimental evidence for a frustrated energy landscape in a three-helix-bundle protein family

The role of solvent viscosity in the dynamics of protein conformational changes.

Relaxation rate for an ultrafast folding protein is independent of chemical denaturant concentration.

Measuring internal friction of an ultrafast-folding protein

Diffusion in a rough potential

Coordinate-dependent diffusion in protein folding.

Net charge per residue modulates conformational ensembles of intrinsically disordered proteins

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17800-17806

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scholarly article

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10.1073/PNAS.1117368109

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44

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109

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Benjamin Schuler

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2012-04-06T00:00:00Z

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235616793

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22492978

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3497802

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