Title
Backbone fractal dimension and fractal hybrid orbital of protein structure
Abstract
Fractal geometry analysis provides a useful and desirable tool to characterize the configuration and structure of proteins. In this paper we examined the fractal properties of 750 folded proteins from four different structural classes, namely (1) the α-class (dominated by α-helices), (2) the β-class (dominated by β-pleated sheets), (3) the (α/ β)-class (α-helices and β-sheets alternately mixed) and (4) the (α+ β)-class (α-helices and β-sheets largely segregated) by using two fractal dimension methods, i.e. "the local fractal dimension" and "the backbone fractal dimension" (a new and useful quantitative parameter). The results showed that the protein molecules exhibit a fractal behavior in the range of 1 ≤ N≤ 15 (N is the number of the interval between two adjacent amino acid residues), and the value of backbone fractal dimension is distinctly greater than that of local fractal dimension for the same protein. The average value of two fractal dimensions decreased in order of α> α/ β> α+ β> β. Moreover, the mathematical formula for the hybrid orbital model of protein based on the concept of backbone fractal dimension is in good coincidence with that of the similarity dimension. So it is a very accurate and simple method to analyze the hybrid orbital model of protein by using the backbone fractal dimension. © 2013 Elsevier B.V.
Year
DOI
Venue
2013
10.1016/j.cnsns.2013.05.005
Communications in Nonlinear Science and Numerical Simulation
Keywords
DocType
Volume
Protein,Local fractal dimension,Backbone fractal dimension,Hybrid orbital model
Journal
18
Issue
ISSN
Citations 
12
1007-5704
0
PageRank 
References 
Authors
0.34
1
5
Name
Order
Citations
PageRank
Xin Peng100.34
Wei Qi200.34
Mengfan Wang300.34
Rongxin Su420.86
Zhimin He553635.90