Localizando la frustración energética en proteínas

FERREIRO, DU

Puerto Madryn

Congreso; XLVI Reunión Anual Sociedad Argentina de Investigación en Bioquímica y Biología Molecular; 2010

Sociedad Argentina de Investigación en Bioquímica y Biología Molecular

Energy landscape theory does not deny the possibility that conflicting interactions may exist locally in a protein domain. Such ?local frustration", being tolerable, would naturally arise from neutral evolutionary drift or in some cases could indicate a functional adaptation, as alternate configurations become accesible and control protein motions. We recently developed a quantitative method for localizing frustration in native proteins (PNAS 104:19819). Here we present our latest applications of these "frustratometer" algorithms for the analysis of proteins' conformational fluctuations. We analyzed a non-redundant set of allosteric proteins and found that the regions that are known to undergo structural transitions are likely to be highly frustrated in either or both conformations. We relate the local frustration distribution to the function of these proteins and explore its relations to the transitions between the conformational substrates. We discuss how methods for localizing frustration can give insights into the functional aspects of the evolution of proteins' energy landscapes.