Variational Approach to Protein Design and Extraction of Interaction Potentials

Flavio Seno, Cristian Micheletti, Amos Maritan, and Jayanth R. Banavar
Phys. Rev. Lett. 81, 2172 – Published 7 September 1998
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Abstract

We present and discuss a novel approach to the direct and inverse protein folding problem. The proposed strategy is based on a variational approach that allows the simultaneous extraction of amino acid interactions and the low-temperature free energy of sequences of amino acids. The knowledge-based technique is simple and straightforward to implement even for realistic off-lattice proteins because it does not entail threadinglike procedures. Its validity is assessed in the context of a lattice model by means of a variety of stringent checks.

  • Received 6 April 1998

DOI:https://doi.org/10.1103/PhysRevLett.81.2172

©1998 American Physical Society

Authors & Affiliations

Flavio Seno1, Cristian Micheletti2,3, Amos Maritan2,3, and Jayanth R. Banavar4

  • 1Dipartimento di Fisica and INFM, Università di Padova, Via Marzolo 8, 35131 Padova, Italy
  • 2International School for Advanced Studies, (S.I.S.S.A. and INFM), Via Beirut 2-4, 34014 Trieste, Italy
  • 3and The Abdus Salam Centre for Theoretical Physics, Trieste, Italy
  • 4Department of Physics and Center for Materials Physics, The Pennsylvania State University, 104 Davey Laboratory, University Park, Pennsylvania 16802

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Issue

Vol. 81, Iss. 10 — 7 September 1998

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