The role of side-chain interactions in the early steps of aggregation: Molecular dynamics simulations of an amyloid-forming peptide from the yeast prion Sup35.
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CHARMM: the biomolecular simulation programLocal order in the unfolded state: conformational biases and nearest neighbor interactionsExploring the accessible conformations of N-terminal acetylated α-synucleinInvestigation of the Josephin Domain protein-protein interaction by molecular dynamicsMapping the conformational dynamics and pathways of spontaneous steric zipper Peptide oligomerizationFormation of partially ordered oligomers of amyloidogenic hexapeptide (NFGAIL) in aqueous solution observed in molecular dynamics simulations.Phase diagrams describing fibrillization by polyalanine peptides.The role of Phe in the formation of well-ordered oligomers of amyloidogenic hexapeptide (NFGAIL) observed in molecular dynamics simulations with explicit solvent.Spontaneous fibril formation by polyalanines; discontinuous molecular dynamics simulationsA multiscale approach to characterize the early aggregation steps of the amyloid-forming peptide GNNQQNY from the yeast prion sup-35An Atomistic View of Amyloidogenic Self-assembly: Structure and Dynamics of Heterogeneous Conformational States in the Pre-nucleation Phase.Low molecular weight oligomers of amyloid peptides display beta-barrel conformations: a replica exchange molecular dynamics study in explicit solvent.Wetting of nonconserved residue-backbones: A feature indicative of aggregation associated regions of proteins.Are current atomistic force fields accurate enough to study proteins in crowded environments?Kinetic control of dimer structure formation in amyloid fibrillogenesisSimulation of pH-dependent edge strand rearrangement in human beta-2 microglobulin.Free cholesterol induces higher β-sheet content in Aβ peptide oligomers by aromatic interaction with Phe19.Prediction of amyloidogenic and disordered regions in protein chainsAmyloidogenesis abolished by proline substitutions but enhanced by lipid binding.Thermodynamic selection of steric zipper patterns in the amyloid cross-beta spinePrinciples governing oligomer formation in amyloidogenic peptides.Energy landscape of amyloidogenic peptide oligomerization by parallel-tempering molecular dynamics simulation: significant role of Asn ladder.Polymorphism in Alzheimer Abeta amyloid organization reflects conformational selection in a rugged energy landscape.The stability and dynamics of the human calcitonin amyloid peptide DFNKFSelf-assembly of the ionic peptide EAK16: the effect of charge distributions on self-assembly.Insight into the stability of cross-β amyloid fibril from VEALYL short peptide with molecular dynamics simulation.Free energy landscapes for amyloidogenic tetrapeptides dimerization.Binary and ternary aggregation within tethered protein constructs.Structural characterization of GNNQQNY amyloid fibrils by magic angle spinning NMRExploring the role of hydration and confinement in the aggregation of amyloidogenic peptides Aβ(16-22) and Sup35(7-13) in AOT reverse micellesMolecular dynamics analyses of cross-beta-spine steric zipper models: beta-sheet twisting and aggregation.Structural stability and dynamics of an amyloid-forming peptide GNNQQNY from the yeast prion sup-35.Interplay of sequence, topology and termini charge in determining the stability of the aggregates of GNNQQNY mutants: a molecular dynamics study.Structural complexity of a composite amyloid fibril.Monomer adds to preformed structured oligomers of Abeta-peptides by a two-stage dock-lock mechanism.Molecular dynamics simulation suggests possible interaction patterns at early steps of beta2-microglobulin aggregation.A variational model for oligomer-formation process of GNNQQNY peptide from yeast prion protein Sup35Molecular dynamics simulations on the oligomer-formation process of the GNNQQNY peptide from yeast prion protein Sup35.Quantitative characterization of intrinsic disorder in polyglutamine: insights from analysis based on polymer theories.A peptide study of the relationship between the collagen triple-helix and amyloid
P2860
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P2860
The role of side-chain interactions in the early steps of aggregation: Molecular dynamics simulations of an amyloid-forming peptide from the yeast prion Sup35.
description
2003 nî lūn-bûn
@nan
2003 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
The role of side-chain interac ...... de from the yeast prion Sup35.
@ast
The role of side-chain interac ...... de from the yeast prion Sup35.
@en
The role of side-chain interac ...... de from the yeast prion Sup35.
@nl
type
label
The role of side-chain interac ...... de from the yeast prion Sup35.
@ast
The role of side-chain interac ...... de from the yeast prion Sup35.
@en
The role of side-chain interac ...... de from the yeast prion Sup35.
@nl
prefLabel
The role of side-chain interac ...... de from the yeast prion Sup35.
@ast
The role of side-chain interac ...... de from the yeast prion Sup35.
@en
The role of side-chain interac ...... de from the yeast prion Sup35.
@nl
P2093
P2860
P356
P1476
The role of side-chain interac ...... de from the yeast prion Sup35.
@en
P2093
Amedeo Caflisch
Jörg Gsponer
Urs Haberthür
P2860
P304
P356
10.1073/PNAS.0835307100
P407
P577
2003-04-16T00:00:00Z