Role of conservative mutations in protein multi-property adaptation.

摘要: Protein physicochemical properties must undergo complex changes during evolution, as a response to modifications in the organism environment, result of proteins taking up new roles or because need cope with evolution molecular interacting partners. Recent work has emphasized role stability and stability–function trade-offs these protein adaptation processes. In present study, on other hand, we report that combinations few conservative, high-frequency-of-fixation mutations thioredoxin molecule lead largely independent both diversity catalytic mechanisms, revealed by single-molecule atomic force spectroscopy. Furthermore, found are evolutionarily significant, they combine typically hyperthermophilic enhancements modulations function span ranges defined quite different patterns thioredoxins from bacterial eukaryotic origin. These results suggest evolutionary may use, some cases at least, potential conservative originate multiplicity allowed mutational paths leading variety modulation patterns. addition support feasibility using information achieve multi-feature optimization, an important biotechnological goal.