Near-native Protein Structure Simulation

Abstract

The protein folding problem is a fundamental problem in computational molecular biology and biochemical physics. The high resolution 3D structure of a protein is the key to the understanding and manipulating of its biochemical and cellular functions. All information necessary to fold a protein to its native structure is contained in its amino-acid sequence. Proteins structure could be calculated from knowledge of its sequence and our understanding of the sequence-structure relationships. Various optimization methods have been applied to formulation of the folding problem. There are two main approaches. The one is based on properties of homologous proteins. Other is based on reduced models of proteins structure like hydrophobic-polar (HP) protein model. After that, the folding problem is defined like optimization problem. It is a hard optimization problem and most of the authors apply Monte Carlo or metaheuristic methods to solve it. In this paper other approach will be used. By HP model is explained the structures of proteins conformation observed by biologists and is studied the correspondence between the primary and tertiary structures of the proteins.

Keywords

• Protein folding
• Hydrophobic
• 3D HP model