Interplay between Folding and Assembly of Fibril-Forming Polypeptides.

R. Ni, S. Abeln, M. Schor, M.A.C. Stuart, P.G. Bolhuis

Research output: Contribution to JournalArticleAcademicpeer-review

Abstract

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. © 2013 American Physical Society.
Original languageEnglish
Pages (from-to)058101
JournalPhysical Review Letters
Volume111
Issue number5
DOIs
Publication statusPublished - 2013

Fingerprint

polypeptides
folding
assembly
self assembly
hydrophobicity
routes
simulation
interactions
temperature

Cite this

Ni, R. ; Abeln, S. ; Schor, M. ; Stuart, M.A.C. ; Bolhuis, P.G. / Interplay between Folding and Assembly of Fibril-Forming Polypeptides. In: Physical Review Letters. 2013 ; Vol. 111, No. 5. pp. 058101.
@article{eb18ad46a777416c816cba1b62abfa11,
title = "Interplay between Folding and Assembly of Fibril-Forming Polypeptides.",
abstract = "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. {\circledC} 2013 American Physical Society.",
author = "R. Ni and S. Abeln and M. Schor and M.A.C. Stuart and P.G. Bolhuis",
year = "2013",
doi = "10.1103/PhysRevLett.111.058101",
language = "English",
volume = "111",
pages = "058101",
journal = "Physical Review Letters",
issn = "0031-9007",
publisher = "American Physical Society",
number = "5",

}

Interplay between Folding and Assembly of Fibril-Forming Polypeptides. / Ni, R.; Abeln, S.; Schor, M.; Stuart, M.A.C.; Bolhuis, P.G.

In: Physical Review Letters, Vol. 111, No. 5, 2013, p. 058101.

Research output: Contribution to JournalArticleAcademicpeer-review

TY - JOUR

T1 - Interplay between Folding and Assembly of Fibril-Forming Polypeptides.

AU - Ni, R.

AU - Abeln, S.

AU - Schor, M.

AU - Stuart, M.A.C.

AU - Bolhuis, P.G.

PY - 2013

Y1 - 2013

N2 - 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. © 2013 American Physical Society.

AB - 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. © 2013 American Physical Society.

U2 - 10.1103/PhysRevLett.111.058101

DO - 10.1103/PhysRevLett.111.058101

M3 - Article

VL - 111

SP - 058101

JO - Physical Review Letters

JF - Physical Review Letters

SN - 0031-9007

IS - 5

ER -