Simplified Exactly Solvable Model forβ-Amyloid Aggregation
about
Physical mechanism for biopolymers to aggregate and maintain in non-equilibrium states.Inversion of the balance between hydrophobic and hydrogen bonding interactions in protein folding and aggregationStatistical mechanical treatments of protein amyloid formation.Finite-size corrections and scaling for the dimer model on the checkerboard lattice.Cooperativity and modularity in protein folding.Pseudo-one-dimensional nucleation in dilute polymer solutionsFrustration-induced protein intrinsic disorder.Simplified lattice model for polypeptide fibrillar transitions.A statistical mechanical approach to protein aggregation.Fibril elongation mechanisms of HET-s prion-forming domain: Topological evidence for growth polarity
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Simplified Exactly Solvable Model forβ-Amyloid Aggregation
description
article publié dans la revue scientifique Physical Review Letters
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im August 2010 veröffentlichter wissenschaftlicher Artikel
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scientific article published in Physical Review Letters
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wetenschappelijk artikel
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наукова стаття, опублікована в серпні 2010
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name
Simplified Exactly Solvable Model forβ-Amyloid Aggregation
@en
Simplified Exactly Solvable Model forβ-Amyloid Aggregation
@nl
type
label
Simplified Exactly Solvable Model forβ-Amyloid Aggregation
@en
Simplified Exactly Solvable Model forβ-Amyloid Aggregation
@nl
prefLabel
Simplified Exactly Solvable Model forβ-Amyloid Aggregation
@en
Simplified Exactly Solvable Model forβ-Amyloid Aggregation
@nl
P2860
P1476
Simplified exactly solvable model for β-amyloid aggregation
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P2093
P2860
P304
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10.1103/PHYSREVLETT.105.108102
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2010-08-31T00:00:00Z