Some Factors in the Interpretation of Protein Denaturation

Abstract

Publisher Summary This chapter explores that the changes that take place in the protein molecules during denaturation constitute one of the most interesting and complex classes of reactions that can be found either in nature or in the laboratory. These reactions are important because of the information they can provide about the more intimate details of protein structure and function. They are also significant because they challenge the chemist with a difficult area for the application of chemical principles. The chapter reviews that the denaturation is a process in which the spatial arrangement of the polypeptide chains within the molecule is changed from that typical of the native protein to a more disordered arrangement. The chapter also discusses the classification of protein structures: primary, secondary, and tertiary structures. The primary structure is that expressed by the structural chemical formula and depends entirely on the chemical valence bonds that the classical organic chemist would write down for the protein molecule. The secondary structure is the configuration of the polypeptide chain that results from the satisfaction of the hydrogen bonding potential between the peptide N-H and C=O groups. The tertiary structure is the pattern according to which the secondary structures are packed together within the native protein molecule. The term “denaturation” as used in this chapter is indented to include changes in both the secondary and tertiary structures.