Results and Applications
In addition to important potential industrial applications, Makhatadze also believes the research sheds some light on the evolution of proteins. The researchers compared the mutations that they made within the proteins in order to optimize the protein’s performance with the mutations naturally occurring in the proteins from the evolutionary distant organisms.
Instead of seeing more mutations along with increased performance as with most evolutionary adaptations, the researchers saw that less frequent mutations resulted in a more stable protein. “This suggests that the stability of proteins might not be evolutionarily important,” he said. “It appears that as soon as the protein is able to function in given conditions and is stable at a given temperature, anything above that is not really necessary.”
Publication and Funding
This research was published Feb. 5 in the online Early Edition of the Proceedings of the National Academy of Sciences (PNAS), and was fully funded by the National Science Foundation.
Makhatadze was assisted in his research by post-doctoral researcher Mayank Patel, graduate student Jiajing Liu, NMR Core Director Scott McCallum, and Assistant Professor of Biology Chunyu Wang, all of Rensselaer, as well as former graduate student Alexey Gribenko, who is currently a member of the faculty at the University of Texas Medical Branch. In addition, the structure of one the proteins used in the study, acylphosphatase (AcPh), was actually solved at Rensselaer using the sophisticated nuclear magnetic resonance core within the Center for Biotechnology and Interdisciplinary Studies.