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

被引：11
|
作者：
Pitulice, L. [1 ]
Isvoran, A. [1 ]
Craescu, C. T. [2 ]
Chiriac, A. [1 ]
机构：
[1] W Univ Timisoara, Dept Chem, Timisoara 300115, Romania
[2] Ctr Univ Paris Sud, INSERM, U759, Inst Curie Rech, F-91405 Orsay, France
来源：
CHAOS SOLITONS & FRACTALS | 2009年 / 40卷 / 02期
关键词：
FRACTAL DIMENSION; SIMILARITY;
D O I：
10.1016/j.chaos.2007.08.016
中图分类号：
O1 [数学];
学科分类号：
0701 ; 070101 ;
摘要：
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. (C) 2007 Elsevier Ltd. All rights reserved.
引用
收藏
页码：684 / 690
页数：7
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