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Scaling properties of the radius of gyration and surface area for EF-hand calcium binding proteins

Author

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  • Pitulice, L.
  • Isvoran, A.
  • Craescu, C.T.
  • Chiriac, A.

Abstract

In this paper, we analyze the scaling properties of both the radius of gyration and the surface area for EF-hand calcium binding proteins. These properties are different for two conformational subfamilies: proteins with extended and compact structures, respectively. The radius of gyration is a measure of the shape of protein, whereas its surface fractal dimension is a measure of its interatomic packing. Different scaling properties for the radius of gyration underline that these two subfamilies present different shapes whilst different scaling properties for the surface area reveal different strengths of their intermolecular forces. All these data suggest different mechanisms responsible for the global folding of proteins belonging to these two subfamilies.

Suggested Citation

  • Pitulice, L. & Isvoran, A. & Craescu, C.T. & Chiriac, A., 2009. "Scaling properties of the radius of gyration and surface area for EF-hand calcium binding proteins," Chaos, Solitons & Fractals, Elsevier, vol. 40(2), pages 684-690.
    • Handle: RePEc:eee:chsofr:v:40:y:2009:i:2:p:684-690
    DOI: 10.1016/j.chaos.2007.08.016
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    References listed on IDEAS

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    1. Isvoran, Adriana & Pitulice, Laura & Craescu, Constantin T. & Chiriac, Adrian, 2008. "Fractal aspects of calcium binding protein structures," Chaos, Solitons & Fractals, Elsevier, vol. 35(5), pages 960-966.
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