A preformed binding interface in the unbound ensemble of an intrinsically disordered protein: evidence from molecular simulations.
about
Efficient Atomistic Simulation of Pathways and Calculation of Rate Constants for a Protein-Peptide Binding Process: Application to the MDM2 Protein and an Intrinsically Disordered p53 Peptide.Analytical methods for structural ensembles and dynamics of intrinsically disordered proteinsInvestigating the Role of Large-Scale Domain Dynamics in Protein-Protein InteractionsLigand clouds around protein clouds: a scenario of ligand binding with intrinsically disordered proteinsModulation of the disordered conformational ensembles of the p53 transactivation domain by cancer-associated mutationsAdvantages of proteins being disordered.Integrating atomistic molecular dynamics simulations, experiments, and network analysis to study protein dynamics: strength in unity.The transition state structure for coupled binding and folding of disordered protein domains.Discriminating binding mechanisms of an intrinsically disordered protein via a multi-state coarse-grained model.Comparison of structure determination methods for intrinsically disordered amyloid-β peptides.Recognition of the HIV capsid by the TRIM5α restriction factor is mediated by a subset of pre-existing conformations of the TRIM5α SPRY domain.Quantifying the Sources of Kinetic Frustration in Folding Simulations of Small Proteins.Hamiltonian Switch Metropolis Monte Carlo Simulations for Improved Conformational Sampling of Intrinsically Disordered Regions Tethered to Ordered Domains of Proteins.Modest influence of FRET chromophores on the properties of unfolded proteins.p15PAF is an intrinsically disordered protein with nonrandom structural preferences at sites of interaction with other proteins.A relationship between the transient structure in the monomeric state and the aggregation propensities of α-synuclein and β-synucleinBalanced Protein-Water Interactions Improve Properties of Disordered Proteins and Non-Specific Protein AssociationDisorder in cholesterol-binding functionality of CRAC peptides: a molecular dynamics study.Dynamic conformational change regulates the protein-DNA recognition: an investigation on binding of a Y-family polymerase to its target DNA.Binding cavities and druggability of intrinsically disordered proteins.The Differential Response of Proteins to Macromolecular CrowdingThe inverted free energy landscape of an intrinsically disordered peptide by simulations and experiments.Disorder-to-Order Transition of an Active-Site Loop Mediates the Allosteric Activation of Sortase A.The metastasis suppressor KISS1 is an intrinsically disordered protein slightly more extended than a random coil.Inherent relationships among different biophysical prediction methods for intrinsically disordered proteins.Role of Intrinsic Protein Disorder in the Function and Interactions of the Transcriptional Coactivators CREB-binding Protein (CBP) and p300Dimensions, energetics, and denaturant effects of the protein unstructured stateMechanism and rate constants of the Cdc42 GTPase binding with intrinsically disordered effectors.Multiscaled exploration of coupled folding and binding of an intrinsically disordered molecular recognition element in measles virus nucleoprotein.Effects of Macromolecular Crowding on the Conformational Ensembles of Disordered Proteins.Temperature-dependent solvation modulates the dimensions of disordered proteins.A theoretical view of protein dynamics.Dissecting mechanism of coupled folding and binding of an intrinsically disordered protein by chemical synthesis of conformationally constrained analogues.Intramolecular interactions stabilizing compact conformations of the intrinsically disordered kinase-inhibitor domain of Sic1: a molecular dynamics investigation.Conformational Dynamics of the Partially Disordered Yeast Transcription Factor GCN4Force field development and simulations of intrinsically disordered proteins.Enhanced Sampling of Intrinsic Structural Heterogeneity of the BH3-Only Protein Binding Interface of Bcl-xL.Intrinsically disordered inhibitor of glutamine synthetase is a functional protein with random-coil-like pKa values.Accounting for the kinetics in order parameter analysis: lessons from theoretical models and a disordered peptide.Sequence- and Temperature-Dependent Properties of Unfolded and Disordered Proteins from Atomistic Simulations.
P2860
Q27301215-7757D533-0D79-4EEE-B8CB-16DFCE137FF0Q28067028-41368BCC-2692-49DA-B17D-5759D369C630Q28070759-20AD0D61-976D-493E-BDAF-03B33F2D8E78Q28534062-8BCE07EE-4FFE-4A36-B042-8A3688A35249Q28546597-9539954E-4298-4D78-B5AE-0DCF89FADFE0Q30358999-2FE60878-552D-42F9-9DEB-33954BBEF27DQ30375668-BD6C14EA-787D-4308-A045-D83C817DF975Q31121568-8518DAF0-E0DD-4F6C-A306-711ED52E8DB8Q33655583-5F136759-08BB-4E67-B076-F0440690C30EQ33791740-2D1E7B3A-A58C-4957-85E7-6BAB2AAB436CQ33989616-302257AD-C5EC-4076-A028-B35ACDF3BEA6Q34044947-CF6786DB-4849-4F79-9C2B-D5E806A39C87Q34044981-F9ED4B48-4C6D-4D94-B96E-84887ED8EA7DQ34310142-51777487-0A06-4C8A-8774-8D15399FFC96Q34406035-3D89F25D-BE0E-422A-83F6-C1ACBBBCD664Q34447530-BE79B5AA-CEA3-4F03-8472-F4690FD5E6C2Q34503099-5088B7D2-83C3-4FAD-B698-79967EF25009Q34563791-E22517F6-7C0A-4959-9F69-46099B34A67FQ35238378-5248F3B5-C8C2-40EB-BBE3-32E193876696Q35571730-673C3B46-08AF-4394-8623-CE8D4D1DF3DAQ36089426-8D7BAE80-A271-4C7E-8C1D-B1E2C1047DA1Q36205942-3D29CBB4-0412-4E68-B68D-7EE7B52EE47FQ36218681-4047C9C2-F9CA-4B79-AB78-46490F9A2C84Q36283040-1419CFD8-AB58-4459-8A29-7A3488FA9D8CQ36554344-85BFC438-451E-423B-AAEE-6B439AF8A6FDQ36727341-C01EF18B-548D-4AFF-AE3C-F602E70A8417Q36749693-59B4E554-7D6A-4DA2-9598-1355B334F534Q36823266-EBC9683F-9BB9-4B36-9DBF-B102D4B7B63CQ37218609-00AC3A3D-35BB-42CA-8E48-CCE58BC0897AQ37354855-261DA1D4-C4A9-4BFE-8E35-FAF9E412F846Q37702019-A047C043-FCE5-4283-83FB-FEE4DDFC7177Q38202826-FCBBDD91-9726-4660-B853-8A6E68AAEC2DQ38730298-A7320143-4E65-4437-852E-7D95CEE63D7DQ41728638-E30B2157-5032-4664-B1FE-1A68E40E8C8CQ41853245-F1D603C4-203A-4EF6-8F72-1D1750FFBF94Q47591502-9FEAEE56-3EAE-40F1-A460-861777A6B1B1Q47807596-5337BD52-C61E-4C69-9A77-9BC9D459EAD3Q51098464-103DEA2B-6B92-416A-898E-B62B4B9F64BEQ51297007-D1113760-4119-4B12-A474-1C61EAA9B945Q51673743-DC585430-EF05-4CD9-9EF2-437CF7ED4C67
P2860
A preformed binding interface in the unbound ensemble of an intrinsically disordered protein: evidence from molecular simulations.
description
2012 nî lūn-bûn
@nan
2012 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
A preformed binding interface ...... ce from molecular simulations.
@ast
A preformed binding interface ...... ce from molecular simulations.
@en
A preformed binding interface ...... ce from molecular simulations.
@nl
type
label
A preformed binding interface ...... ce from molecular simulations.
@ast
A preformed binding interface ...... ce from molecular simulations.
@en
A preformed binding interface ...... ce from molecular simulations.
@nl
prefLabel
A preformed binding interface ...... ce from molecular simulations.
@ast
A preformed binding interface ...... ce from molecular simulations.
@en
A preformed binding interface ...... ce from molecular simulations.
@nl
P2860
P1476
A preformed binding interface ...... ce from molecular simulations.
@en
P2093
Michael Knott
P2860
P304
P356
10.1371/JOURNAL.PCBI.1002605
P577
2012-07-19T00:00:00Z