Single-molecule spectroscopy of the temperature-induced collapse of unfolded proteins. - Wikidata - wikimedia - TriplyDB

Single-molecule spectroscopy of the temperature-induced collapse of unfolded proteins.

Single-molecule spectroscopy of the temperature-induced collapse of unfolded proteins.

http://www.wikidata.org/entity/Q37469603

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Learning To Fold Proteins Using Energy Landscape Theory.Protein folding at single-molecule resolution.Compaction properties of an intrinsically disordered protein: Sic1 and its kinase-inhibitor domain.Single-molecule fluorescence coincidence spectroscopy and its application to resonance energy transfer.Fast protein folding kinetics A microfluidic approach for investigating the temperature dependence of biomolecular activity with single-molecule resolution.Describing sequence-ensemble relationships for intrinsically disordered proteins.The origin of nonmonotonic complex behavior and the effects of nonnative interactions on the diffusive properties of protein folding From the Cover: Charge interactions can dominate the dimensions of intrinsically disordered proteins.Modest influence of FRET chromophores on the properties of unfolded proteins.A preformed binding interface in the unbound ensemble of an intrinsically disordered protein: evidence from molecular simulations.Conformations of intrinsically disordered proteins are influenced by linear sequence distributions of oppositely charged residues Free-energy landscape of the GB1 hairpin in all-atom explicit solvent simulations with different force fields: Similarities and differences Balanced Protein-Water Interactions Improve Properties of Disordered Proteins and Non-Specific Protein Association Temperature dependent equilibrium native to unfolded protein dynamics and properties observed with IR absorption and 2D IR vibrational echo experiments.Structural basis of folding cooperativity in model proteins: insights from a microcanonical perspective.Single-molecule fluorescence reveals sequence-specific misfolding in multidomain 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.Dynamic Protein Interaction Networks and New Structural Paradigms in Signaling.The inverted free energy landscape of an intrinsically disordered peptide by simulations and experiments.Intramolecular three-colour single pair FRET of intrinsically disordered proteins with increased dynamic range Conformational dynamics and self-association of intrinsically disordered Huntingtin exon 1 in cells.Transient misfolding dominates multidomain protein folding Polymer scaling laws of unfolded and intrinsically disordered proteins quantified with single-molecule spectroscopy Conformational Dynamics of Two Natively Unfolded Fragment Peptides: Comparison of the AMBER and CHARMM Force Fields.Quantifying internal friction in unfolded and intrinsically disordered proteins with single-molecule spectroscopy.Dimensions, energetics, and denaturant effects of the protein unstructured state Comprehensive structural and dynamical view of an unfolded protein from the combination of single-molecule FRET, NMR, and SAXS.Measuring ultrafast protein folding rates from photon-by-photon analysis of single molecule fluorescence trajectories.Shedding light on protein folding landscapes by single-molecule fluorescence.Temperature-dependent solvation modulates the dimensions of disordered proteins.The folding of single domain proteins--have we reached a consensus?Role of solvation effects in protein denaturation: from thermodynamics to single molecules and back.How, when and why proteins collapse: the relation to folding.Single molecule study of the intrinsically disordered FG-repeat nucleoporin 153.Thermal compaction of the intrinsically disordered protein tau: entropic, structural, and hydrophobic factors.A J-modulated protonless NMR experiment characterizes the conformational ensemble of the intrinsically disordered protein WIP.Exploring the role of internal friction in the dynamics of unfolded proteins using simple polymer models.Substrate dynamics in enzyme action: rotations of monosaccharide subunits in the binding groove are essential for pectin methylesterase processivity.

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P2860

Single-molecule spectroscopy of the temperature-induced collapse of unfolded proteins.

http://www.wikidata.org/entity/Q37469603

description

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2009年学术文章

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2009年学术文章

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2009年学术文章

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2009年學術文章

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2009年學術文章

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2009年學術文章

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name

Single-molecule spectroscopy of the temperature-induced collapse of unfolded proteins.

@en

Single-molecule spectroscopy of the temperature-induced collapse of unfolded proteins.

@nl

type

label

Single-molecule spectroscopy of the temperature-induced collapse of unfolded proteins.

@en

Single-molecule spectroscopy of the temperature-induced collapse of unfolded proteins.

@nl

prefLabel

Single-molecule spectroscopy of the temperature-induced collapse of unfolded proteins.

@en

Single-molecule spectroscopy of the temperature-induced collapse of unfolded proteins.

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PNAS.0900622106

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

P1476

Single-molecule spectroscopy of the temperature-induced collapse of unfolded proteins.

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Armin Hoffmann

http://www.w3.org/2001/XMLSchema#string

Benjamin Heinz

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Daniel Nettels

http://www.w3.org/2001/XMLSchema#string

Dominik Haenni

http://www.w3.org/2001/XMLSchema#string

Frank Küster

http://www.w3.org/2001/XMLSchema#string

Hagen Hofmann

http://www.w3.org/2001/XMLSchema#string

Jan Kubelka

http://www.w3.org/2001/XMLSchema#string

Klaus Gast

http://www.w3.org/2001/XMLSchema#string

Luc Reymond

http://www.w3.org/2001/XMLSchema#string

Sonja Müller-Späth

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P2860

Comparison of simple potential functions for simulating liquid water

Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features

Development of an improved four-site water model for biomolecular simulations: TIP4P-Ew

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

Dominant forces in protein folding

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

Structure and energetics of the hydrogen-bonded backbone in protein folding.

Polymer principles in protein structure and stability.

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

How fast is protein hydrophobic collapse?

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20740-20745

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scholarly article

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10.1073/PNAS.0900622106

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106

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Benjamin Schuler

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2009-11-20T00:00:00Z

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40026692

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2791578

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