β-sheet propensity controls the kinetic pathways and morphologies of seeded peptide aggregation.
about
Polymorphism in self-assembly of peptide-based β-hairpin contributes to network morphology and hydrogel mechanical rigidity.Gold-Induced Fibril Growth: The Mechanism of Surface-Facilitated Amyloid Aggregation.Protein Polymerization into Fibrils from the Viewpoint of Nucleation Theory.Fibrillation-prone conformations of the amyloid-β-42 peptide at the gold/water interface.Multiscale simulations for understanding the evolution and mechanism of hierarchical peptide self-assembly.Dynamics of the conformational transitions during the dimerization of an intrinsically disordered peptide: a case study on the human islet amyloid polypeptide fragment.Interplay between the hydrophobic effect and dipole interactions in peptide aggregation at interfaces.The interaction with gold suppresses fiber-like conformations of the amyloid β (16–22) peptide
P2860
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P2860
β-sheet propensity controls the kinetic pathways and morphologies of seeded peptide aggregation.
description
2012 nî lūn-bûn
@nan
2012 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
β-sheet propensity controls th ...... of seeded peptide aggregation.
@ast
β-sheet propensity controls th ...... of seeded peptide aggregation.
@en
type
label
β-sheet propensity controls th ...... of seeded peptide aggregation.
@ast
β-sheet propensity controls th ...... of seeded peptide aggregation.
@en
prefLabel
β-sheet propensity controls th ...... of seeded peptide aggregation.
@ast
β-sheet propensity controls th ...... of seeded peptide aggregation.
@en
P2860
P50
P356
P1476
β-sheet propensity controls th ...... of seeded peptide aggregation.
@en
P2860
P304
P356
10.1063/1.4755748
P407
P577
2012-10-01T00:00:00Z