Accuracy of current all-atom force-fields in modeling protein disordered states.
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Principles and Overview of Sampling Methods for Modeling Macromolecular Structure and DynamicsIntegrating atomistic molecular dynamics simulations, experiments, and network analysis to study protein dynamics: strength in unity.Experimental conformational energy maps of proteins and peptides.ff14IDPs force field improving the conformation sampling of intrinsically disordered proteins.Assessing the potential of atomistic molecular dynamics simulations to probe reversible protein-protein recognition and binding.Force field-dependent solution properties of glycine oligomersSynergy between NMR measurements and MD simulations of protein/RNA complexes: application to the RRMs, the most common RNA recognition motifs.Methods of probing the interactions between small molecules and disordered proteins.Solving protein structures using short-distance cross-linking constraints as a guide for discrete molecular dynamics simulations.Metadynamic metainference: Convergence towards force field independent structural ensembles of a disordered peptide.Optimization of the GBMV2 implicit solvent force field for accurate simulation of protein conformational equilibria.Disentangling polydispersity in the PCNA-p15PAF complex, a disordered, transient and multivalent macromolecular assembly.Molecular Dynamics Simulation of Tau Peptides for the Investigation of Conformational Changes Induced by Specific Phosphorylation Patterns.Comparison of force fields for Alzheimer's A β42: A case study for intrinsically disordered proteins.Crowding in Cellular Environments at an Atomistic Level from Computer Simulations.Testing the transferability of a coarse-grained model to intrinsically disordered proteins.Structural Characterization of Highly Flexible Proteins by Small-Angle Scattering.An Efficient Method for Estimating the Hydrodynamic Radius of Disordered Protein Conformations.Conformational flexibility of the complete catalytic domain of Cdc25B phosphatases.Communication: Role of explicit water models in the helix folding/unfolding processes.Atomistic Peptide Folding Simulations Reveal Interplay of Entropy and Long-Range Interactions in Folding Cooperativity
P2860
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P2860
Accuracy of current all-atom force-fields in modeling protein disordered states.
description
2014 nî lūn-bûn
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2014年の論文
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2014年論文
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2014年論文
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2014年論文
@zh-hk
2014年論文
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2014年論文
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2014年论文
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2014年论文
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2014年论文
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name
Accuracy of current all-atom force-fields in modeling protein disordered states.
@en
type
label
Accuracy of current all-atom force-fields in modeling protein disordered states.
@en
prefLabel
Accuracy of current all-atom force-fields in modeling protein disordered states.
@en
P356
P1476
Accuracy of current all-atom force-fields in modeling protein disordered states.
@en
P2093
Ferruccio Palazzesi
Meher K Prakash
P356
10.1021/CT500718S
P577
2014-12-18T00:00:00Z