Extremophilic proteins represent a natural template to understand how enzymatic activity can be performed in non conventional conditions, i.e. high temperature, high salt concentration, low temperature, high pressure. Evolution has driven this migration of protein sequences/folds toward optimal states for different environments. How 'artificial evolution' can do the same job? In other words, how protein design can succeed in mutating proteins for changing their working milieu, or even incorporate new chemical activity? I propose to the readers two interesting reviews on this subject. One is from J.G. Saven group [1], the other from D. Baker and K.N Houk [2]. It is amazing how leading groups in the field have advanced the research combining multiple approaches. Enjoy!
[1] I. Samish, C.M. MacDermaid, J.M. Perez-Aguilar, J.G. Saven, Ann.Rev.Phys.Chem. (2011) 62, 129-149. (here)
[2] G. Kiss, N. Celebi-Olcum, R. Moretti, D. Baker, and K.N. Houk, Angew. Chem. Int. Ed. (2013) 52, 5700-5725. (here)
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