Full distance-resolved folding energy landscape of one single protein molecule.
about
Diverse metastable structures formed by small oligomers of α-synuclein probed by force spectroscopyMechanical unzipping and rezipping of a single SNARE complex reveals hysteresis as a force-generating mechanismWhen fast is better: protein folding fundamentals and mechanisms from ultrafast approachesDirect observation of a force-induced switch in the anisotropic mechanical unfolding pathway of a protein.Electric-field-stimulated protein mechanics.Deconvolution of dynamic mechanical networksProtein folding at single-molecule resolution.High-resolution optical tweezers for single-molecule manipulation.Optical trapping with high forces reveals unexpected behaviors of prion fibrils.Denaturant-dependent folding of GFPRapid internal contraction boosts DNA friction.Protein folding and unfolding under forceSequence-resolved free energy profiles of stress-bearing vimentin intermediate filaments.Free-energy inference from partial work measurements in small systems.The complex folding network of single calmodulin molecules.Direct observation of multiple misfolding pathways in a single prion protein moleculeSingle reconstituted neuronal SNARE complexes zipper in three distinct stages.Free energy profiles from single-molecule pulling experiments.Practical axial optical trappingDirect single-molecule observation of calcium-dependent misfolding in human neuronal calcium sensor-1From mechanical folding trajectories to intrinsic energy landscapes of biopolymers.Connecting thermal and mechanical protein (un)folding landscapes.Collapse kinetics and chevron plots from simulations of denaturant-dependent folding of globular proteins.Fast-folding alpha-helices as reversible strain absorbers in the muscle protein myomesinMechano-transduction: from molecules to tissuesCommunication: Does force spectroscopy of biomolecules probe their intrinsic dynamic properties?Spring-loaded unraveling of a single SNARE complex by NSF in one round of ATP turnoverReconstructing folding energy landscapes from splitting probability analysis of single-molecule trajectories.Single-molecule observation of helix staggering, sliding, and coiled coil misfolding.Structural basis of histidine kinase autophosphorylation deduced by integrating genomics, molecular dynamics, and mutagenesisReconstructing folding energy landscapes by single-molecule force spectroscopy.Energy landscape analysis of native folding of the prion protein yields the diffusion constant, transition path time, and ratesLimitations of constant-force-feedback experiments.Calcium-dependent folding of single calmodulin molecules.Dynamic force sensing of filamin revealed in single-molecule experiments.Transition paths, diffusive processes, and preequilibria of protein folding.Structure-Based Derivation of Protein Folding Intermediates and Energies from Optical TweezersHelices 2 and 3 are the initiation sites in the PrP(C) → PrP(SC) transitionSingle-Molecule Chemo-Mechanical Spectroscopy Provides Structural Identity of Folding Intermediates.Highly anisotropic stability and folding kinetics of a single coiled coil protein under mechanical tension.
P2860
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P2860
Full distance-resolved folding energy landscape of one single protein molecule.
description
2010 nî lūn-bûn
@nan
2010 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Full distance-resolved folding energy landscape of one single protein molecule.
@ast
Full distance-resolved folding energy landscape of one single protein molecule.
@en
type
label
Full distance-resolved folding energy landscape of one single protein molecule.
@ast
Full distance-resolved folding energy landscape of one single protein molecule.
@en
prefLabel
Full distance-resolved folding energy landscape of one single protein molecule.
@ast
Full distance-resolved folding energy landscape of one single protein molecule.
@en
P2860
P356
P1476
Full distance-resolved folding energy landscape of one single protein molecule.
@en
P2093
J Christof M Gebhardt
Matthias Rief
P2860
P304
P356
10.1073/PNAS.0909854107
P407
P577
2010-01-19T00:00:00Z