Fibril elongation mechanisms of HET-s prion-forming domain: Topological evidence for growth polarity

Proteins: Structure, Function and Bioinformatics

Volumn 79, Issue 11, 2011, Pages 3067-3081

  Baiesi, Marco ^a   Seno, Flavio ^a   Trovato, Antonio ^a  

^a UNIVERSITY OF PADOVA   (Italy)

Author keywords

Coarse grained models; Dock and lock mechanism; Monte Carlo simulations; Protein aggregation; Topology based models

Indexed keywords

HET S PRION PROTEIN; PRION PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; CARBOXY TERMINAL SEQUENCE; FIBRIL ELONGATION; MOLECULAR DOCKING; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN LOCALIZATION; PROTEIN STRUCTURE; THERMAL ANALYSIS; THERMODYNAMIC ANALYSIS;

AMYLOID; FUNGAL PROTEINS; HYDROGEN BONDING; MODELS, MOLECULAR; MONTE CARLO METHOD; PODOSPORA; PRIONS; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; THERMODYNAMICS;

FUNGAL PRION; HET-S PRION; RUMEX;

EID: 80053943942     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.23133     Document Type: Article

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