Multifractality, Levinthal paradox, and energy hypersurface
Moret MA, Pascutti PG, Mundim KC, Bisch PM, Nogueira E
PHYSICAL REVIEW E
63 (2): art. no. 020901 Part 1 FEB 2001

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(alpha) 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(alpha) function describes some structural properties of a protein. The behavior of the f(alpha) 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.

KeyWords Plus:
MOLECULAR-DYNAMICS SIMULATION, FOLDING SIMULATIONS, INSECT DEFENSIN, OPTIMIZATION, PEPTIDES, CONFORMATIONS, RELAXATION, MODELS

Addresses:
Moret MA, Univ Estadual Feira de Santana, Dept Fis, Campus Univ, BR-44031460 Feira De Santana, BA, Brazil
Univ Estadual Feira de Santana, Dept Fis, BR-44031460 Feira De Santana, BA, Brazil
Univ Fed Rio de Janeiro, Inst Biofis, BR-21949900 Rio De Janeiro, Brazil
Univ Fed Bahia, Inst Fis, BR-40210340 Salvador, BA, Brazil

Publisher:        AMERICAN PHYSICAL SOC, COLLEGE PK
IDS Number:   403BH
ISSN:              1063-651X