Ligand-dependent equilibrium fluctuations of single calmodulin molecules.
about
A nanoscale force probe for gauging intermolecular interactionsSingle-molecule force spectroscopy distinguishes target binding modes of calmodulinInsights into Protein-Ligand Interactions: Mechanisms, Models, and MethodsOptimizing 1-μs-Resolution Single-Molecule Force Spectroscopy on a Commercial Atomic Force Microscope.The role of dynamic conformational ensembles in biomolecular recognitionPresynaptic Calmodulin targets: lessons from structural proteomics.Deconvolution of dynamic mechanical networksProtein folding at single-molecule resolution.Counteracting chemical chaperone effects on the single-molecule α-synuclein structural landscape.Nanomechanics of the cadherin ectodomain: "canalization" by Ca2+ binding results in a new mechanical element.High-resolution optical tweezers for single-molecule manipulation.Full reconstruction of a vectorial protein folding pathway by atomic force microscopy and molecular dynamics simulations.Atomic force microscopy with sub-picoNewton force stability for biological applications.Photothermal cantilever actuation for fast single-molecule force spectroscopy.Equilibrium sampling for biomolecules under mechanical tensionData-driven approach to decomposing complex enzyme kinetics with surrogate models.Sampling protein form and function with the atomic force microscope.Full distance-resolved folding energy landscape of one single protein molecule.Photounbinding of calmodulin from a family of CaM binding peptidesProtein folding and unfolding under forceFast and forceful refolding of stretched alpha-helical solenoid proteins.Energy landscape views for interplays among folding, binding, and allostery of calmodulin domains.The complex folding network of single calmodulin molecules.Single molecule force spectroscopy using polyproteins.Single reconstituted neuronal SNARE complexes zipper in three distinct stages.The Ca(2+) influence on calmodulin unfolding pathway: a steered molecular dynamics simulation study.Induced fit, conformational selection and independent dynamic segments: an extended view of binding eventsSingle-molecule dissection of the high-affinity cohesin-dockerin complex.Inhibitor binding increases the mechanical stability of staphylococcal nucleaseTowards design principles for determining the mechanical stability of proteins.P-SPLINES USING DERIVATIVE INFORMATION.Extension of a three-helix bundle domain of myosin VI and key role of calmodulins.Ca2+ binding enhanced mechanical stability of an archaeal crystallin.Ultrastable atomic force microscopy: improved force and positional stability.Fast-folding alpha-helices as reversible strain absorbers in the muscle protein myomesinDifferential mechanical stability of filamin A rod segments.Optimizing the calculation of energy landscape parameters from single-molecule protein unfolding experiments.Identifying sequential substrate binding at the single-molecule level by enzyme mechanical stabilizationMechanical anisotropy of ankyrin repeatsLow folding cooperativity of HP35 revealed by single-molecule force spectroscopy and molecular dynamics simulation
P2860
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P2860
Ligand-dependent equilibrium fluctuations of single calmodulin molecules.
description
2009 nî lūn-bûn
@nan
2009 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Ligand-dependent equilibrium fluctuations of single calmodulin molecules.
@ast
Ligand-dependent equilibrium fluctuations of single calmodulin molecules.
@en
type
label
Ligand-dependent equilibrium fluctuations of single calmodulin molecules.
@ast
Ligand-dependent equilibrium fluctuations of single calmodulin molecules.
@en
prefLabel
Ligand-dependent equilibrium fluctuations of single calmodulin molecules.
@ast
Ligand-dependent equilibrium fluctuations of single calmodulin molecules.
@en
P2860
P356
P1433
P1476
Ligand-dependent equilibrium fluctuations of single calmodulin molecules.
@en
P2093
Fabian Ziegler
Matthias Rief
P2860
P304
P356
10.1126/SCIENCE.1166191
P407
P577
2009-01-01T00:00:00Z