Structure and dynamics of the Abeta(21-30) peptide from the interplay of NMR experiments and molecular simulations.
about
Constructing ensembles for intrinsically disordered proteinsAtomic-level characterization of the ensemble of the Aβ(1-42) monomer in water using unbiased molecular dynamics simulations and spectral algorithmsAmyloid beta-protein monomer folding: free-energy surfaces reveal alloform-specific differencesDisrupting self-assembly and toxicity of amyloidogenic protein oligomers by "molecular tweezers" - from the test tube to animal modelsSynergistic applications of MD and NMR for the study of biological systemsDimer formation enhances structural differences between amyloid β-protein (1-40) and (1-42): an explicit-solvent molecular dynamics studyInfluence of preformed Asp23-Lys28 salt bridge on the conformational fluctuations of monomers and dimers of Abeta peptides with implications for rates of fibril formationLigand clouds around protein clouds: a scenario of ligand binding with intrinsically disordered proteinsComparisons with amyloid-β reveal an aspartate residue that stabilizes fibrils of the aortic amyloid peptide medin.Evaluating the performance of the ff99SB force field based on NMR scalar coupling data.The C-terminal threonine of Aβ43 nucleates toxic aggregation via structural and dynamical changes in monomers and protofibrils.Comparison of structure determination methods for intrinsically disordered amyloid-β peptides.Contrasting disease and nondisease protein aggregation by molecular simulationHomogeneous and heterogeneous tertiary structure ensembles of amyloid-β peptides.Polymorphism in Alzheimer Abeta amyloid organization reflects conformational selection in a rugged energy landscape.Sucrose in aqueous solution revisited, Part 2: adaptively biased molecular dynamics simulations and computational analysis of NMR relaxationDisordered amyloidogenic peptides may insert into the membrane and assemble into common cyclic structural motifs.A maximum entropy approach to the study of residue-specific backbone angle distributions in α-synuclein, an intrinsically disordered protein.Comparative studies of disordered proteins with similar sequences: application to Aβ40 and Aβ42The peculiar role of the A2V mutation in amyloid-β (Aβ) 1-42 molecular assemblyInvestigating how peptide length and a pathogenic mutation modify the structural ensemble of amyloid beta monomer.Interpeptide interactions induce helix to strand structural transition in Abeta peptidesDynamics of metastable β-hairpin structures in the folding nucleus of amyloid β-protein.Varied Probability of Staying Collapsed/Extended at the Conformational Equilibrium of Monomeric Aβ40 and Aβ42Assessing and refining molecular dynamics simulations of proteins with nuclear magnetic resonance data.The conformational ensembles of α-synuclein and tau: combining single-molecule FRET and simulations.Transient β-hairpin formation in α-synuclein monomer revealed by coarse-grained molecular dynamics simulation.C-terminal turn stability determines assembly differences between Aβ40 and Aβ42Monomeric Aβ(1-40) and Aβ(1-42) Peptides in Solution Adopt Very Similar Ramachandran Map Distributions That Closely Resemble Random Coil.Differences in β-strand populations of monomeric Aβ40 and Aβ42.Microsecond Simulations of the Diphtheria Toxin Translocation Domain in Association with Anionic Lipid BilayersNMR relaxation in proteins with fast internal motions and slow conformational exchange: model-free framework and Markov state simulationsAmino acid substitutions [K16A] and [K28A] distinctly affect amyloid β-protein oligomerization.Systematic improvement of a classical molecular model of waterAβ monomers transiently sample oligomer and fibril-like configurations: ensemble characterization using a combined MD/NMR approachFinding Our Way in the Dark Proteome.Small molecule inhibitors of amyloid β peptide aggregation as a potential therapeutic strategy for Alzheimer's disease.Protein misfolding in the late-onset neurodegenerative diseases: common themes and the unique case of amyotrophic lateral sclerosis.Effect of zinc binding on β-amyloid structure and dynamics: implications for Aβ aggregation.Structure of ring-shaped Aβ₄₂ oligomers determined by conformational selection.
P2860
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P2860
Structure and dynamics of the Abeta(21-30) peptide from the interplay of NMR experiments and molecular simulations.
description
2008 nî lūn-bûn
@nan
2008 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Structure and dynamics of the ...... nts and molecular simulations.
@ast
Structure and dynamics of the ...... nts and molecular simulations.
@en
type
label
Structure and dynamics of the ...... nts and molecular simulations.
@ast
Structure and dynamics of the ...... nts and molecular simulations.
@en
prefLabel
Structure and dynamics of the ...... nts and molecular simulations.
@ast
Structure and dynamics of the ...... nts and molecular simulations.
@en
P2093
P2860
P356
P1476
Structure and dynamics of the ...... nts and molecular simulations.
@en
P2093
Aaron H Phillips
David E Wemmer
Jory Z Ruscio
Michaeleen Doucleff
Teresa Head-Gordon
P2860
P304
P356
10.1021/JA710366C
P407
P577
2008-04-16T00:00:00Z