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Protein folding and the robustness of cells

Tan, G. J. Shawn, Revilla, Ferran D. and Zauner, Klaus-Peter (2007) Protein folding and the robustness of cells BioSystems, 87, pp. 289-298.

Record type: Article

Abstract

The intricate intracellular infrastructure of all known life forms is based on proteins. The folded shape of a protein determines both the protein’s function and the set of molecules it will bind to. This tight coupling between a protein’s function and its interconnections in the molecular interaction network has consequences for the molecular course of evolution. It is also counter to human engineering approaches. Here we report on a simulation study investigating the impact of random errors in an abstract metabolic network of 500 enzymes. Tight coupling between function and interconnectivity of nodes is compared to the case where these two properties are independent. Our results show that the model system under consideration is more robust if function and interconnection are intertwined. These ?ndings are discussed in the context of nanosystems engineering.

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More information

Published date: 2007
Keywords: Self-isolation, Organic devices, Complex networks, Nanoengineering, Evolvability, Modularity
Organisations: Agents, Interactions & Complexity

Identifiers

Local EPrints ID: 263583
URI: http://eprints.soton.ac.uk/id/eprint/263583
PURE UUID: d1cd53a6-7199-4a26-8c69-f3594e872f57

Catalogue record

Date deposited: 21 Feb 2007
Last modified: 18 Jul 2017 07:43

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Contributors

Author: G. J. Shawn Tan
Author: Ferran D. Revilla
Author: Klaus-Peter Zauner

University divisions

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