Interplay between folding and assembly of fibril-forming polypeptides

Autor:	Ni, Ran, Abeln, Sanne, Schor, Marieke, Stuart, Martien A. Cohen, Bolhuis, Peter G.
Rok vydání:	2013
Předmět:	Condensed Matter - Soft Condensed Matter Physics - Biological Physics Quantitative Biology - Biomolecules
Zdroj:	Phys. Rev. Lett. 111, 058101 (2013)
Druh dokumentu:	Working Paper
DOI:	10.1103/PhysRevLett.111.058101
Popis:	Polypeptides can self-assemble into hierarchically organized fibrils consisting of a stack of individually folded polypeptides driven together by hydrophobic interaction. Using a coarse grained model, we systematically studied this self-assembly as a function of temperature and hydrophobicity of the residues on the outside of the building block. We find the self-assembly can occur via two different pathways - a random aggregation-folding route, and a templated-folding process - thus indicating a strong coupling between folding and assembly. The simulation results can explain experimental evidence that assembly through stacking of folded building blocks is rarely observed, at the experimental concentrations. The model thus provides a generic picture of hierarchical fibril formation. Comment: Accepted in Physical Review Letters
Databáze:	arXiv
Externí odkaz:	http://arxiv.org/abs/1307.3076 Zobrazit plný text záznamu View this record from Arxiv