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Fractal protein structure revisited: Topological, kinetic and thermodynamic relationships

Author

Listed:
  • Tejera, E.
  • Machado, A.
  • Rebelo, I.
  • Nieto-Villar, J.

Abstract

The present work explored the definitions and calculations of fractal dimensions in protein structures and the corresponding relationships with the protein class, secondary structure contents, fold type as well as kinetic and thermodynamic parameters like the folding and unfolding rate, the folding–unfolding free energy and others. The results showed a positive correlation of some fractal exponents with the kinetic and thermodynamic variables even considering the effect of the protein length. On the other hand the influences of secondary structures types, especially the turn conformation are significant as well as the fractal exponent profiles according to class and fold types.

Suggested Citation

  • Tejera, E. & Machado, A. & Rebelo, I. & Nieto-Villar, J., 2009. "Fractal protein structure revisited: Topological, kinetic and thermodynamic relationships," Physica A: Statistical Mechanics and its Applications, Elsevier, vol. 388(21), pages 4600-4608.
    • Handle: RePEc:eee:phsmap:v:388:y:2009:i:21:p:4600-4608
    DOI: 10.1016/j.physa.2009.07.015
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    Cited by:

    1. Saw, Vee-Liem & Chew, Lock Yue, 2015. "Helicalised fractals," Chaos, Solitons & Fractals, Elsevier, vol. 75(C), pages 191-203.
    2. Peng, Xin & Qi, Wei & Su, Rongxin & He, Zhimin, 2012. "Describing some characters of serine proteinase using fractal analysis," Chaos, Solitons & Fractals, Elsevier, vol. 45(7), pages 1017-1023.

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