Abstract
Thermostability is an important protein property essential for the protein industrial application. Different approaches of rational design are used for protein thermostability improvement. In this research, the effect of proline substitutions on the protein thermostability was tested. Several types of available data on protein characteristics were used for substitution position choosing in order to find those that are critical for thermostability improvement while maintaining the specific activity. The approach used was based on combined analysis of protein structure, structure-function relationship, multiple sequence alignment, and folding free energy. Proline substitutions that were carried out had a critical effect on thermostability of endoglucanase II from Penicillium verruculosum. The most stabilizing substitution S308P provided a 4- and 2.4-fold increase in time of half-life at 70 °C and 80 °C with maintaining the specific activity. Molecular dynamics simulations revealed the observed effects on the protein structure and indicated principal changes in flexibility and hydrogen bonds networks.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
