Describing some characters of serine proteinase using fractal analysis

Xin Peng, Wei Qi, Rongxin Su and Zhimin He

Chaos, Solitons & Fractals, 2012, vol. 45, issue 7, 1017-1023

Abstract: In this paper we calculated the fractal dimensions of four proteins, chymotrypsin, elastase, trypsin and subtilisin, which are made up of about 220–275 amino acids and belong to the family of serine proteinase by using three definitions of fractal dimension i.e. the chain fractal dimension (DL), the mass fractal dimension (Dm) and the correlation fractal dimension (Dc). We also analyzed the relationship between fractal dimension and space structure or secondary structure contents of proteins. The results showed that the values of fractal dimensions are almost same for the global mammalian enzymes (chymotrypsin, elastase and trypsin), but different for the global subtilisin. This demonstrated that the more similar structures, the more equal fractal dimensions, and if the fractal dimensions of proteins are different from each other, the three dimensional structures should not be similar. On the other hand, the detailed structures and fractal dimensions of the active sites of four enzymes are extraordinarily similar. Therefore, the fractal method can be applied to the elucidation of the proteins evolution.

Date: 2012
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Persistent link: https://EconPapers.repec.org/RePEc:eee:chsofr:v:45:y:2012:i:7:p:1017-1023

DOI: 10.1016/j.chaos.2012.04.002

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