Comparison of force fields for Alzheimer's A β42: A case study for intrinsically disordered proteins.
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High-Resolution Structures of the Amyloid-β 1-42 Dimers from the Comparison of Four Atomistic Force Fields.Emergence of Alternative Structures in Amyloid Beta 1-42 Monomeric Landscape by N-terminal Hexapeptide Amyloid Inhibitors.Conformational Ensembles of the Wild-Type and S8C Aβ1-42 Dimers.Force field development and simulations of intrinsically disordered proteins.Peptide dimerization-dissociation rates from replica exchange molecular dynamics.Islet Amyloid Polypeptide Promotes Amyloid-beta Aggregation by Binding-induced Helix-unfolding of the Amyloidogenic Core.Insights into the Molecular Mechanisms of Alzheimer's and Parkinson's Diseases with Molecular Simulations: Understanding the Roles of Artificial and Pathological Missense Mutations in Intrinsically Disordered Proteins Related to Pathology.Small static electric field strength promotes aggregation-prone structures in amyloid-β(29-42).Cooperative structural transitions in amyloid-like aggregation.Looking at the Disordered Proteins through the Computational Microscope.Conformational analysis of replica exchange MD: Temperature-dependent Markov networks for FF amyloid peptides
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Comparison of force fields for Alzheimer's A β42: A case study for intrinsically disordered proteins.
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2016 nî lūn-bûn
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2016年の論文
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2016年学术文章
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2016年学术文章
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2016年学术文章
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2016年学术文章
@zh-my
2016年学术文章
@zh-sg
2016年學術文章
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name
Comparison of force fields for ...... insically disordered proteins.
@en
Comparison of force fields for ...... insically disordered proteins.
@nl
type
label
Comparison of force fields for ...... insically disordered proteins.
@en
Comparison of force fields for ...... insically disordered proteins.
@nl
prefLabel
Comparison of force fields for ...... insically disordered proteins.
@en
Comparison of force fields for ...... insically disordered proteins.
@nl
P2860
P356
P1433
P1476
Comparison of force fields for ...... rinsically disordered proteins
@en
P2093
Birgit Strodel
P2860
P304
P356
10.1002/PRO.3064
P577
2016-10-26T00:00:00Z