Fractal structure and conformational entropy of protein chain

H Q Li; S H Chen; H M Zhao

doi:10.1016/0141-8130(90)90046-d

Fractal structure and conformational entropy of protein chain

Int J Biol Macromol. 1990 Dec;12(6):374-8. doi: 10.1016/0141-8130(90)90046-d.

Authors

H Q Li¹, S H Chen, H M Zhao

Affiliation

¹ Department of Chemistry, Sichuan University, Chengdu, People's Republic of China.

PMID: 2088495
DOI: 10.1016/0141-8130(90)90046-d

Abstract

The structures of 25 proteins arbitrarily chosen are investigated by fractal geometry, and their fractal dimensions (Df) and conformational entropies S(NO) are calculated by Havlin-Ben Avraham and Monte Carlo method, respectively. Comparison of the Df and S(NO) give the relation: Df = 1.532 - 3.00 x 10(-4) S(NO). The entropy data obtained by Monte Carlo method for the chain of random self-avoiding walks confirm the prediction of renormalization group: S(NO) = 1.544NO + 0.1667 In NO + 0.1570 where NO is the number of residues in a protein chain. Both the Df and S(NO) reflect the conformational properties of a protein molecular chain. The idea resulting from the present communication suggests that the thermodynamic behaviours of proteins may be related to multifractals.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Mathematics
Monte Carlo Method
Protein Conformation*
Proteins / chemistry*
Thermodynamics

Substances

Proteins