The Journal of Chemical Physics · 2012 · 21 citations · 19 references
Life SciencesBiochemistryBiophysicsProtein BiochemistryProtein FoldingStructural BiologyFibrous ProteinsFolding KineticsMacromolecular Assembly ModelingProtein DynamicsProtein Folding ThermodynamicsProtein StructureAmyloid Fibril FormationAmyloidogenic PeptidesCritical Nucleus FormationCritical Nucleus SizeLattice ModelsNascent Chain FoldingNascent Polypeptide FoldingProtein Nucleus Formation
A new method for determining the size of critical nucleus of fibril formation of polypeptide chains is proposed. Based on the hypothesis that the fibril grows by addition of a nascent peptide to the preformed template, the nucleus size N(c) is defined as the number of forming template peptides above which the time to add a new monomer becomes independent of the template size. Using lattice models one can show that our method and the standard method which is based on calculation of the free energy, provide the same result for N(c).
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Mechanism of Prion Propagation: Amyloid Growth Occurs by Monomer Addition
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Alzheimer's Disease Amyloid Propagation by a Template-Dependent Dock-Lock Mechanism
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