A simple lattice model that captures protein folding, aggregation and amyloid formation.
about
Knotted proteins: A tangled tale of Structural BiologyLattice model for amyloid peptides: OPEP force field parametrization and applications to the nucleus size of Alzheimer's peptides.The hydrophobic temperature dependence of amino acids directly calculated from protein structuresAmyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Effects of knot type in the folding of topologically complex lattice proteins.Thermodynamics of amyloid formation and the role of intersheet interactions.Sequence dependent aggregation of peptides and fibril formation.The attachment of α-synuclein to a fiber: A coarse-grain approach.Steric confinement and enhanced local flexibility assist knotting in simple models of protein folding.Contribution of Water to Pressure and Cold Denaturation of Proteins.Interplay between the hydrophobic effect and dipole interactions in peptide aggregation at interfaces.Consistent Treatment of Hydrophobicity in Protein Lattice Models Accounts for Cold DenaturationCompetition between surface adsorption and folding of fibril-forming polypeptidesHow determinant is N-terminal to C-terminal coupling for protein folding?
P2860
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P2860
A simple lattice model that captures protein folding, aggregation and amyloid formation.
description
2014 nî lūn-bûn
@nan
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
2014年论文
@zh
2014年论文
@zh-cn
name
A simple lattice model that captures protein folding, aggregation and amyloid formation.
@en
type
label
A simple lattice model that captures protein folding, aggregation and amyloid formation.
@en
prefLabel
A simple lattice model that captures protein folding, aggregation and amyloid formation.
@en
P2860
P50
P1433
P1476
A simple lattice model that captures protein folding, aggregation and amyloid formation.
@en
P2860
P304
P356
10.1371/JOURNAL.PONE.0085185
P407
P577
2014-01-15T00:00:00Z