Journal of Proteome Science & Computational Biology

Journal of Proteome Science & Computational Biology

ISSN 2050-2273
Original Research

Information catalysis and intrinsically disordered proteins in large complexes

Rodrick Wallace

Correspondence: Rodrick Wallace Wallace@nyspi.columbia.edu

Author Affiliations :

Division of Epidemiology, the New York State Psychiatric Institute, USA.


Abstract

Background: Recent studies indicate that intrinsically disordered proteins (IDP) do not preferentially bind to chaperones in vivo, suggesting that their role is to either prevent pathological conformations, or to aid in the assembly of large complexes. This, in turn, suggests that large IDP complexes must form under the control of a sophisticated regulatory system of chemical cognition – in effect, an information catalysis – that, while it may have evolutionarily exapted existing chaperones, is likely to have evolved other, specialized, mechanisms or modalities of process modulation.

Methods: We model this using recently developed 'statistical' approaches from information theory that exploit the fact that information is itself a form of free energy.

Results: Information catalysis is found to arise directly from the 'chain rule' of information theory, via a statistical mechanical argument in which metabolic free energy both powers the transmission of information and applies available entropy as a tool to correct malformed complexes by local heating. Conclusions The regulatory mechanisms or modalities may well be IDP's within the complexes themselves, an extension of the chaperone concept explaining the observed prevalence of disorder in large complexes.

keywords: catalysis, information theory, rate distortion, regulation

ISSN 2050-2273
Volume 1
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