To understand the conformational behavior of a protein, it is necessary to define not only the structure of its native state but also that of various denatured states. Recent studies have revealed the biological significance of denatured states in processes such as aggregation, chaperone binding, and transport across membrane. A variety of denatured states have also been identified, differing in their overall dimensions and the extent of residual secondary and tertiary structures. Pepsin is a particularly good model for the study of conformational behavior under several conditions because detailed information is available on its secondary structure, enzymatic properties, and zymogen activation. Solution small angle X-ray scattering (SAXS) is an effective technique for measuring structure and structural difference of protein under various environments. In this study, the structural characteristics of various conformational states of porcine pepsin were studied in terms of size and shape under several pH conditions by solution SAXS.
Journal: TechConnect Briefs
Volume: 1, Technical Proceedings of the 2007 NSTI Nanotechnology Conference and Trade Show, Volume 1
Published: May 20, 2007
Pages: 646 - 647
Industry sector: Medical & Biotech
Topics: Biomaterials, Informatics, Modeling & Simulation