Statistical analysis of protein molecules

Kushal Shah

doi:10.1038/npre.2011.6298.1

Abstract

AbstractIn this paper, entropy and auto-correlation values of main chain dihedral angles of 22,356 protein molecules are calculated and found to lie within a well-specified range for most proteins. Also, the entropy values obey a Gaussian distribution, which indicates that entropy plays a crucial role in evolution and conservation of protein tertiary structures. A comparison of the auto-correlation values of the dihedral angles of the entire protein molecule with those of the alpha helices and beta sheets indicates that random coils play an important role in determining the tertiary structure of protein molecules.

Highlights

Many important molecular processes in the cell are carried out by protein-protein interactions
To be able to predict a protein structure correctly, we need to be able to understand the dynamics of a protein molecule as it folds from an unfolded state to its native state [6]
Most of the current models used to study protein folding and predict protein structure are based on the concept of global free-energy minimum [7,8,9,10,11]

Summary

Introduction

Many important molecular processes in the cell are carried out by protein-protein interactions These interactions depend on the ability of a protein molecule to be able to bind to other protein molecules and are primarily driven by favorable changes in the free energy of the protein complex (increase in entropy and/or decrease in enthalpy) [1, 2]. These free energy changes are governed by the tertiary structures of the interacting proteins [3,4,5]. Most of the current models used to study protein folding and predict protein structure are based on the concept of global free-energy minimum [7,8,9,10,11]

Methods

Results

Conclusion