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