Article
A Novel Strategy for Thermostability Improvement of Trypsin Based on N-Glycosylation within the Ω-Loop Region.
Journal of microbiology and biotechnology - 28 Jul 2016
Guo Chao, Liu Ye, Yu Haoran, Du Kun, Gan Yiru, Huang He
Abstract excerpt
The Ω-loop is a nonregular and flexible structure that plays an important role in molecular recognition, protein folding, and thermostability. In the present study, molecular dynamics simulation was carried out to assess the molecular stability and flexibility profile of the porcine trypsin structures. Two Ω-Loops (fragment 57-67 and fragment 78-91) were confirmed to represent the flexible region. Subsequently,...
Topics
- Animals
- Catalytic Domain
- Enzyme Stability
- Glycosylation
- Hydrolysis
- Models, Molecular
- Mutation
- Protein Conformation
- Protein Engineering
- Recombinant Proteins
- Spectrum Analysis