Single-molecule spectroscopy of the temperature-induced collapse of unfolded proteins.
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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 kineticsA 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 foldingFrom 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 residuesFree-energy landscape of the GB1 hairpin in all-atom explicit solvent simulations with different force fields: Similarities and differencesBalanced Protein-Water Interactions Improve Properties of Disordered Proteins and Non-Specific Protein AssociationTemperature 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 proteinsExtracting 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 rangeConformational dynamics and self-association of intrinsically disordered Huntingtin exon 1 in cells.Transient misfolding dominates multidomain protein foldingPolymer scaling laws of unfolded and intrinsically disordered proteins quantified with single-molecule spectroscopyConformational 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 stateComprehensive 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.
P2860
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P2860
Single-molecule spectroscopy of the temperature-induced collapse of unfolded proteins.
description
2009 nî lūn-bûn
@nan
2009年の論文
@ja
2009年学术文章
@wuu
2009年学术文章
@zh-cn
2009年学术文章
@zh-hans
2009年学术文章
@zh-my
2009年学术文章
@zh-sg
2009年學術文章
@yue
2009年學術文章
@zh
2009年學術文章
@zh-hant
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.
@nl
P2093
P2860
P356
P1476
Single-molecule spectroscopy of the temperature-induced collapse of unfolded proteins.
@en
P2093
Armin Hoffmann
Benjamin Heinz
Daniel Nettels
Dominik Haenni
Frank Küster
Hagen Hofmann
Jan Kubelka
Klaus Gast
Luc Reymond
Sonja Müller-Späth
P2860
P304
20740-20745
P356
10.1073/PNAS.0900622106
P407
P577
2009-11-20T00:00:00Z