How Many Conformations Can a Protein Remember?

Thomas M. A. Fink and Robin C. Ball
Phys. Rev. Lett. 87, 198103 – Published 23 October 2001
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Abstract

We show that a protein can be trained to recognize multiple conformations, analogous to an associative memory, and provide capacity calculations based on energy fluctuations and information theory. Unlike the linear capacity of a Hopfield network, the number of conformations which can be remembered by a protein sequence depends on the size of the amino acid alphabet as lnA, independent of protein length. This admits the possibility of certain proteins, such as prions, evolving to fold to independent stable conformations, as well as novel possibilities for protein and heteropolymer design.

  • Received 1 May 2000

DOI:https://doi.org/10.1103/PhysRevLett.87.198103

©2001 American Physical Society

Authors & Affiliations

Thomas M. A. Fink* and Robin C. Ball

  • Theory of Condensed Matter, Cavendish Laboratory, Cambridge CB3 0HE, United Kingdom

  • *Present address: Laboratoire de Physique Statistique, Ecole Normale Supérieure, 75231 Paris Cedex 05, France.Electronic address: fink@lps.ens.fr; http://www.tcm.phy.cam.ac.uk/~tmf20/
  • Present address: Department of Physics, University of Warwick, Coventry CV4 7AL, United Kingdom.Electronic address: r.c.ball@warwick.ac.uk

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Issue

Vol. 87, Iss. 19 — 5 November 2001

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