Predicting Protein Surface Property with its Surface Hydrophobicity

Abstract

This article reviews and discusses the relationship between surface hydrophobicity and other surface properties of proteins and the possibility of using surface hydrophobicity as a key indicator to predict and evaluate the changes in the surface properties of a protein. Hydrophobicity is the main driving force of protein folding; it affects the structure and functions. Surface hydrophobicity and other surface properties of proteins are controlled by their spatial structures. Due to the hydrophobic interactions, most proteins fold into their globular structures, and they lack sufficient hydrophobic residues on the molecular surface; thus, they do not exhibit excellent surface properties. Surface hydrophobicity is closely related to the changes in the surface property of proteins because it directly reflects the actual distribution of the hydrophobic residues on the surface of a protein. The molecular structure of a protein can be changed or modified to remove the constraints of spatial structures and expose more hydrophobic residues on the molecular surface, which may improve the surface properties of proteins. Therefore, the changes in the surface hydrophobicity caused by changes in the molecular structure can be an ideal key indicator to predict and evaluate the changes in the surface properties of a protein.