Chemically Denatured Structures of Porcine Pepsin using Small-Angle X-ray Scattering
| Autor: | Kyeong Sik Jin, Yecheol Rho, Jun Ha Kim, Byoungseok Min |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
Polymers and Plastics
denaturation small-angle X-ray scattering (SAXS) Ab initio urea 02 engineering and technology Article 03 medical and health sciences chemistry.chemical_compound fluids and secretions Pepsin Native state Molecule Denaturation (biochemistry) 030304 developmental biology chemistry.chemical_classification 0303 health sciences biology Small-angle X-ray scattering digestive oral and skin physiology General Chemistry 021001 nanoscience & nanotechnology Crystallography Enzyme Porcine pepsin chemistry Raman spectroscopy Urea biology.protein 0210 nano-technology |
| Zdroj: | Polymers Volume 11 Issue 12 |
| ISSN: | 2073-4360 |
| Popis: | Porcine pepsin is a gastric aspartic proteinase that reportedly plays a pivotal role in the digestive process of many vertebrates. We have investigated the three-dimensional (3D) structure and conformational transition of porcine pepsin in solution over a wide range of denaturant urea concentrations (0&ndash 10 M) using Raman spectroscopy and small-angle X-ray scattering. Furthermore, 3D GASBOR ab initio structural models, which provide an adequate conformational description of pepsin under varying denatured conditions, were successfully constructed. It was shown that pepsin molecules retain native conformation at 0&ndash 5 M urea, undergo partial denaturation at 6 M urea, and display a strongly unfolded conformation at 7&ndash 10 M urea. According to the resulting GASBOR solution models, we identified an intermediate pepsin conformation that was dominant during the early stage of denaturation. We believe that the structural evidence presented here provides useful insights into the relationship between enzymatic activity and conformation of porcine pepsin at different states of denaturation. |
| Databáze: | OpenAIRE |
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