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Multifractality, Levinthal paradox, and energy hypersurface

M. A. Moret, P. G. Pascutti, K. C. Mundim, P. M. Bisch, and E. Nogueira, Jr.
Phys. Rev. E 63, 020901(R) – Published 10 January 2001
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Abstract

Multifractal properties in the potential energy hypersurface of polypeptides and proteins are investigated. Characteristic multifractal behavior for different molecular systems is obtained from the f(α) spectra. The analysis shows that the dimension of the phase space of the problem influences the accessibility to different parts of the potential energy hypersurface. Also, we show that it is necessary to take into account the H-bond formation between amino acids in the conformational-folding search. The present findings indicate that the f(α) function describes some structural properties of a protein. The behavior of the f(α) spectra gives an alternative explanation about the Levinthal paradox. Furthermore, the anomalous temperature dependence of the Raman spin-lattice relaxation rates can be related to the perturbations in the secondary structures.

  • Received 21 June 2000

DOI:https://doi.org/10.1103/PhysRevE.63.020901

©2001 American Physical Society

Authors & Affiliations

M. A. Moret1,2, P. G. Pascutti2, K. C. Mundim3, P. M. Bisch2, and E. Nogueira, Jr.3

  • 1Departamento de Física, Universidade Estadual de Feira de Santana, Campus Universitário, 44031-460 Feira de Santana, Bahia, Brazil
  • 2Instituto de Biofísica, Universidad Federal do Rio de Janeiro, 21949-900 Rio de Janeiro, RJ, Brazil
  • 3Instituto de Física, Universidad Federal da Bahia, Campus de Ondina, 40210-340 Salvador, Bahia, Brazil

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Vol. 63, Iss. 2 — February 2001

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