alpha-helix formation: discontinuous molecular dynamics on an intermediate-resolution protein model.
about
Structural Conversion of Aβ17-42 Peptides from Disordered Oligomers to U-Shape Protofilaments via Multiple Kinetic PathwaysPhase diagrams describing fibrillization by polyalanine peptides.Spontaneous fibril formation by polyalanines; discontinuous molecular dynamics simulationsProbing protein aggregation using discrete molecular dynamicsA closer look into the α-helix basin.Multidimensional persistence in biomolecular dataEnergy landscapes of the monomer and dimer of the Alzheimer's peptide Abeta(1-28).PRIMO/PRIMONA: a coarse-grained model for proteins and nucleic acids that preserves near-atomistic accuracy.Mechanism of the pH-Controlled Self-Assembly of Nanofibers from Peptide AmphiphilesCholesterol-induced protein sorting: an analysis of energetic feasibilityFolding Trp-cage to NMR resolution native structure using a coarse-grained protein modelSolvent and mutation effects on the nucleation of amyloid beta-protein foldingIn silico study of amyloid beta-protein folding and oligomerization.Dominance of misfolded intermediates in the dynamics of α-helix foldingImpact of sequence on the molecular assembly of short amyloid peptides.Effects of macromolecular crowding on amyloid beta (16-22) aggregation using coarse-grained simulations.Side-chain interactions determine amyloid formation by model polyglutamine peptides in molecular dynamics simulations.Structural basis for Aβ1–42 toxicity inhibition by Aβ C-terminal fragments: discrete molecular dynamics study.Transferable coarse-grained potential for de novo protein folding and designSpontaneous formation of twisted Aβ(16-22) fibrils in large-scale molecular-dynamics simulations.Fibrillization propensity for short designed hexapeptides predicted by computer simulationRole of electrostatic interactions in amyloid beta-protein (A beta) oligomer formation: a discrete molecular dynamics studyStructural transitions and oligomerization along polyalanine fibril formation pathways from computer simulationsComputer simulation study of amyloid fibril formation by palindromic sequences in prion peptidesFolding of pig gastric mucin non-glycosylated domains: a discrete molecular dynamics study.Revisiting the Ramachandran plot: hard-sphere repulsion, electrostatics, and H-bonding in the alpha-helix.Folding of gas-phase polyalanines in a static electric field: alignment, deformations, and polarization effectsExploring the suitability of coarse-grained techniques for the representation of protein dynamics.Polymorphism of fibrillar structures depending on the size of assembled Aβ17-42 peptides.Molecular dynamics simulations of spontaneous fibril formation by random-coil peptides.Computational approaches to understanding protein aggregation in neurodegeneration.Molecular mechanics.Molecular dynamics simulation of amyloid beta dimer formation.Monte Carlo studies of folding, dynamics, and stability in alpha-helices.Coarse-grained strategy for modeling protein stability in concentrated solutions.Generic coarse-grained model for protein folding and aggregation.Solvent effects on the conformational transition of a model polyalanine peptide.A coarse-grained alpha-carbon protein model with anisotropic hydrogen-bonding.N-terminal Prion Protein Peptides (PrP(120-144)) Form Parallel In-register β-Sheets via Multiple Nucleation-dependent PathwaysFast in silico protein folding by introduction of alternating hydrogen bond potentials.
P2860
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P2860
alpha-helix formation: discontinuous molecular dynamics on an intermediate-resolution protein model.
description
2001 nî lūn-bûn
@nan
2001 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
alpha-helix formation: discont ...... iate-resolution protein model.
@ast
alpha-helix formation: discont ...... iate-resolution protein model.
@en
alpha-helix formation: discont ...... iate-resolution protein model.
@nl
type
label
alpha-helix formation: discont ...... iate-resolution protein model.
@ast
alpha-helix formation: discont ...... iate-resolution protein model.
@en
alpha-helix formation: discont ...... iate-resolution protein model.
@nl
prefLabel
alpha-helix formation: discont ...... iate-resolution protein model.
@ast
alpha-helix formation: discont ...... iate-resolution protein model.
@en
alpha-helix formation: discont ...... iate-resolution protein model.
@nl
P2860
P356
P1433
P1476
alpha-helix formation: discont ...... iate-resolution protein model.
@en
P2093
Voegler Smith A
P2860
P304
P356
10.1002/PROT.1100
P407
P577
2001-08-01T00:00:00Z