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Daniel Otzen

The length distribution of frangible biofilaments

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Standard

The length distribution of frangible biofilaments. / Michaels, Thomas C T; Yde, Pernille; Willis, Julian C W; Jensen, Mogens H; Otzen, Daniel; Dobson, Christopher M; Buell, Alexander K; Knowles, Tuomas P J.

In: Journal of Chemical Physics, Vol. 143, No. 16, 164901, 28.10.2015, p. 1-15.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

Michaels, TCT, Yde, P, Willis, JCW, Jensen, MH, Otzen, D, Dobson, CM, Buell, AK & Knowles, TPJ 2015, 'The length distribution of frangible biofilaments', Journal of Chemical Physics, vol. 143, no. 16, 164901, pp. 1-15. https://doi.org/10.1063/1.4933230

APA

Michaels, T. C. T., Yde, P., Willis, J. C. W., Jensen, M. H., Otzen, D., Dobson, C. M., Buell, A. K., & Knowles, T. P. J. (2015). The length distribution of frangible biofilaments. Journal of Chemical Physics, 143(16), 1-15. [164901]. https://doi.org/10.1063/1.4933230

CBE

Michaels TCT, Yde P, Willis JCW, Jensen MH, Otzen D, Dobson CM, Buell AK, Knowles TPJ. 2015. The length distribution of frangible biofilaments. Journal of Chemical Physics. 143(16):1-15. https://doi.org/10.1063/1.4933230

MLA

Michaels, Thomas C T et al. "The length distribution of frangible biofilaments". Journal of Chemical Physics. 2015, 143(16). 1-15. https://doi.org/10.1063/1.4933230

Vancouver

Michaels TCT, Yde P, Willis JCW, Jensen MH, Otzen D, Dobson CM et al. The length distribution of frangible biofilaments. Journal of Chemical Physics. 2015 Oct 28;143(16):1-15. 164901. https://doi.org/10.1063/1.4933230

Author

Michaels, Thomas C T ; Yde, Pernille ; Willis, Julian C W ; Jensen, Mogens H ; Otzen, Daniel ; Dobson, Christopher M ; Buell, Alexander K ; Knowles, Tuomas P J. / The length distribution of frangible biofilaments. In: Journal of Chemical Physics. 2015 ; Vol. 143, No. 16. pp. 1-15.

Bibtex

@article{206b9a3fd4374a83a28c0c381e1b28b6,
title = "The length distribution of frangible biofilaments",
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.",
author = "Michaels, {Thomas C T} and Pernille Yde and Willis, {Julian C W} and Jensen, {Mogens H} and Daniel Otzen and Dobson, {Christopher M} and Buell, {Alexander K} and Knowles, {Tuomas P J}",
year = "2015",
month = oct,
day = "28",
doi = "10.1063/1.4933230",
language = "English",
volume = "143",
pages = "1--15",
journal = "Journal of Chemical Physics",
issn = "0021-9606",
publisher = "AMER INST PHYSICS",
number = "16",

}

RIS

TY - JOUR

T1 - The length distribution of frangible biofilaments

AU - Michaels, Thomas C T

AU - Yde, Pernille

AU - Willis, Julian C W

AU - Jensen, Mogens H

AU - Otzen, Daniel

AU - Dobson, Christopher M

AU - Buell, Alexander K

AU - Knowles, Tuomas P J

PY - 2015/10/28

Y1 - 2015/10/28

N2 - 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.

AB - 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.

U2 - 10.1063/1.4933230

DO - 10.1063/1.4933230

M3 - Journal article

C2 - 26520548

VL - 143

SP - 1

EP - 15

JO - Journal of Chemical Physics

JF - Journal of Chemical Physics

SN - 0021-9606

IS - 16

M1 - 164901

ER -