Format

Send to

Choose Destination
J Chem Phys. 2015 Oct 28;143(16):164901. doi: 10.1063/1.4933230.

The length distribution of frangible biofilaments.

Author information

1
Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, United Kingdom.
2
Niels Bohr Institute, University of Copenhagen, Blegdamsvej 17, 2100 Copenhagen, Denmark.
3
Interdisciplinary Nanoscience Center, Department of Molecular Biology and Genetics, Center for Insoluble Protein Structures, Aarhus University, Gustav Wieds Vej 14, 8000 Aarhus C, Denmark.

Abstract

A number of different proteins possess the ability to polymerize into filamentous structures. Certain classes of such assemblies can have key functional roles in the cell, such as providing the structural basis for the cytoskeleton in the case of actin and tubulin, while others are implicated in the development of many pathological conditions, including Alzheimer's and Parkinson's diseases. In general, the fragmentation of such structures changes the total number of filament ends, which act as growth sites, and hence is a key feature of the dynamics of filamentous growth phenomena. In this paper, we present an analytical study of the master equation of breakable filament assembly and derive closed-form expressions for the time evolution of the filament length distribution for both open and closed systems with infinite and finite monomer supply, respectively. We use this theoretical framework to analyse experimental data for length distributions of insulin amyloid fibrils and show that our theory allows insights into the microscopic mechanisms of biofilament assembly to be obtained beyond those available from the conventional analysis of filament mass only.

PMID:
26520548
DOI:
10.1063/1.4933230
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for American Institute of Physics
Loading ...
Support Center