earticle

영어

Previous experimental and simulated results reported that mutations of protein cavity could improve the thermal stability. Many comparative studies between thermophilic and mesophilic proteins have been conducted to understand which cavity properties were related to the protein thermostability. However, previous statistical studies compared simple one dimensional information of cavities, e.g., surface area, volume, number of cavity and did not identify important differences of cavity properties between thermophilic and mesophilic proteins responsible for protein thermostability. In this study, we attempted to investigate the role of cavity properties in protein thermostability using three dimensional information of cavity properties. Protein structures were classified into three areas, i.e., core, boundary, and surface and cavity properties were compared using this structure index. According to statistical results, cavity flexibility is closely related to protein thermostability. Thermophilic proteins had less cavities in boundary and surface areas and in particular, cavities of mesophilic proteins in all areas were more flexible than those of thermophilic proteins. Compared to the thermophilic proteins, the flexible cavities of mesophilic proteins in boundary and surface can be deleterious to the stability. Based on this study, rational or computational design of flexibility cavity in surface or boundary areas could be a good strategy to improve the thermostability of mesophilic proteins.