Polymer scaling laws of unfolded and intrinsically disordered proteins quantified with single-molecule spectroscopy - Test2 - elhamkhani - TriplyDB

Polymer scaling laws of unfolded and intrinsically disordered proteins quantified with single-molecule spectroscopy

Polymer scaling laws of unfolded and intrinsically disordered proteins quantified with single-molecule spectroscopy

http://www.wikidata.org/entity/Q36342960

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Cooperative unfolding of compact conformations of the intrinsically disordered protein osteopontin Insights into Coupled Folding and Binding Mechanisms from Kinetic Studies Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)Relating sequence encoded information to form and function of intrinsically disordered proteins Energetically significant networks of coupled interactions within an unfolded protein Effects of Mutations on the Reconfiguration Rate of α-Synuclein Intrinsically disordered proteins drive membrane curvature Microsecond barrier-limited chain collapse observed by time-resolved FRET and SAXS.Collapse of a long axis: single-molecule Förster resonance energy transfer and serpin equilibrium unfolding.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.Probing the average local structure of biomolecules using small-angle scattering and scaling laws.Modulation of frustration in folding by sequence permutation.Hamiltonian Switch Metropolis Monte Carlo Simulations for Improved Conformational Sampling of Intrinsically Disordered Regions Tethered to Ordered Domains of Proteins.Single-molecule spectroscopy reveals chaperone-mediated expansion of substrate protein.Conformations of intrinsically disordered proteins are influenced by linear sequence distributions of oppositely charged residues Quantitative assessments of the distinct contributions of polypeptide backbone amides versus side chain groups to chain expansion via chemical denaturation Balanced Protein-Water Interactions Improve Properties of Disordered Proteins and Non-Specific Protein Association Role of denatured-state properties in chaperonin action probed by single-molecule spectroscopy Force-induced unzipping transitions in an athermal crowded environment.The binding mechanisms of intrinsically disordered proteins.The assembly dynamics of the cytolytic pore toxin ClyA.Intrinsically disordered proteins in cellular signalling and regulation.Random coil negative control reproduces the discrepancy between scattering and FRET measurements of denatured protein dimensions.Force field-dependent solution properties of glycine oligomers Resolution of Two Sub-Populations of Conformers and Their Individual Dynamics by Time Resolved Ensemble Level FRET Measurements.Protein folding guides disulfide bond formation Conformational Dynamics of Two Natively Unfolded Fragment Peptides: Comparison of the AMBER and CHARMM Force Fields.From sequence and forces to structure, function, and evolution of intrinsically disordered proteins Localizing internal friction along the reaction coordinate of protein folding by combining ensemble and single-molecule fluorescence spectroscopy Experiments and simulations show how long-range contacts can form in expanded unfolded proteins with negligible secondary structure Dimensions, energetics, and denaturant effects of the protein unstructured state A quantitative measure for protein conformational heterogeneity Protein Composition Determines the Effect of Crowding on the Properties of Disordered Proteins.Single-molecule FRET reveals the native-state dynamics of the IκBα ankyrin repeat domain Comprehensive structural and dynamical view of an unfolded protein from the combination of single-molecule FRET, NMR, and SAXS.Single-molecule spectroscopy reveals polymer effects of disordered proteins in crowded environments.Temperature-dependent solvation modulates the dimensions of disordered proteins.Deciphering Complexity in Molecular Biophysics with Single-Molecule Resolution.Modulation of Intrinsically Disordered Protein Function by Post-translational Modifications.

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P2860

Polymer scaling laws of unfolded and intrinsically disordered proteins quantified with single-molecule spectroscopy

http://www.wikidata.org/entity/Q36342960

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2012 nî lūn-bûn

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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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Polymer scaling laws of unfold ...... h single-molecule spectroscopy

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Polymer scaling laws of unfold ...... h single-molecule spectroscopy

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Polymer scaling laws of unfold ...... h single-molecule spectroscopy

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Polymer scaling laws of unfold ...... h single-molecule spectroscopy

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Polymer scaling laws of unfold ...... h single-molecule spectroscopy

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Polymer scaling laws of unfold ...... h single-molecule spectroscopy

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

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Polymer scaling laws of unfold ...... h single-molecule spectroscopy

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Alessandro Borgia

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Daniel Nettels

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Hagen Hofmann

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Klaus Gast

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P2860

Shape of unperturbed linear polymers: polypropylene

Why are "natively unfolded" proteins unstructured under physiologic conditions?

Natively unfolded proteins: a point where biology waits for physics

Structure of human cyclophilin and its binding site for cyclosporin A determined by X-ray crystallography and NMR spectroscopy.

Polymer principles in protein structure and stability.

Backbone-driven collapse in unfolded protein chains.

Theory of protein folding: the energy landscape perspective.

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

Fluorescence correlation spectroscopy shows that monomeric polyglutamine molecules form collapsed structures in aqueous solutions

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109

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Benjamin Schuler

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