Role of conservative mutations in protein multi-property adaptation.

ABSTRACT: Protein physicochemical properties must undergo complex changes during evolution, as a response to modifications in the organism environment, the result of the proteins taking up new roles or because of the need to cope with the evolution of molecular interacting partners. Recent work has emphasized the role of stability and stability-function trade-offs in these protein adaptation processes. In the present study, on the other hand, we report that combinations of a few conservative, high-frequency-of-fixation mutations in the thioredoxin molecule lead to largely independent changes in both stability and the diversity of catalytic mechanisms, as revealed by single-molecule atomic force spectroscopy. Furthermore, the changes found are evolutionarily significant, as they combine typically hyp

SUBMITTER: Rodriguez-Larrea D 

PROVIDER: S-EPMC2895784 | biostudies-literature | 2010 Jul

REPOSITORIES: biostudies-literature