New force field on modeling intrinsically disordered proteins.
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Binding Mechanisms of Intrinsically Disordered Proteins: Theory, Simulation, and ExperimentConformational Entropy of Intrinsically Disordered Proteins from Amino Acid TriadsAllosteric Autoinhibition Pathway in Transcription Factor ERG: Dynamics Network and Mutant Experimental Evaluations.Discrete molecular dynamics can predict helical prestructured motifs in disordered proteinsff14IDPs force field improving the conformation sampling of intrinsically disordered proteins.Test and Evaluation of ff99IDPs Force Field for Intrinsically Disordered Proteins.Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Dynamics Correlation Network for Allosteric Switching of PreQ1 RiboswitchSynergistic Allosteric Mechanism of Fructose-1,6-bisphosphate and Serine for Pyruvate Kinase M2 via Dynamics Fluctuation Network AnalysisCrystal Structure of StnA for the Biosynthesis of Antitumor Drug Streptonigrin Reveals a Unique Substrate Binding Mode.Advances in free-energy-based simulations of protein folding and ligand binding.Toward accurately modeling N-methylated cyclic peptides.Molecular Dynamics Simulation of Tau Peptides for the Investigation of Conformational Changes Induced by Specific Phosphorylation Patterns.Grid-based backbone correction to the ff12SB protein force field for implicit-solvent simulationsAllosteric mechanism of cyclopropylindolobenzazepine inhibitors for HCV NS5B RdRp via dynamic correlation network analysis.Revealing the binding mode between respiratory syncytial virus fusion protein and benzimidazole-based inhibitors.Conformation Dynamics of the Intrinsically Disordered Protein c-Myb with the ff99IDPs Force Field.Hydrodynamic effects on β-amyloid (16-22) peptide aggregation.The IDP-Specific Force Field ff14IDPSFF Improves the Conformer Sampling of Intrinsically Disordered Proteins.Force field development and simulations of intrinsically disordered proteins.Positive cooperative regulation of double binding sites for human acetylcholinesterase.Selectivity Mechanism of ATP-Competitive Inhibitors for PKB and PKA.
P2860
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P2860
New force field on modeling intrinsically disordered proteins.
description
2014 nî lūn-bûn
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2014年の論文
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2014年学术文章
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2014年学术文章
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name
New force field on modeling intrinsically disordered proteins.
@en
New force field on modeling intrinsically disordered proteins.
@nl
type
label
New force field on modeling intrinsically disordered proteins.
@en
New force field on modeling intrinsically disordered proteins.
@nl
prefLabel
New force field on modeling intrinsically disordered proteins.
@en
New force field on modeling intrinsically disordered proteins.
@nl
P2093
P2860
P356
P1476
New force field on modeling intrinsically disordered proteins
@en
P2093
Cheng Jiang
Hai-Feng Chen
P2860
P304
P356
10.1111/CBDD.12314
P577
2014-07-01T00:00:00Z