IQUIFIB   02644
INSTITUTO DE QUIMICA Y FISICOQUIMICA BIOLOGICAS "PROF. ALEJANDRO C. PALADINI"
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
Structural dynamics of members of CyaY family
Autor/es:
ERNESTO A. ROMAN; PATRICIO O. CRAIG; JAVIER SANTOS
Lugar:
San Javier, Tucumán
Reunión:
Congreso; Reunión anual de la Sociedad Argentina de Biofísica; 2012
Institución organizadora:
Sociedad Argentina de Biofísica
Resumen:
The structural dynamics of proteins is crucial for their function. A balance between stability and flexibility exist for optimal functionality of proteins. The analysis of the local stability distribution, the description of alternative configurations near the native basin and their interconvertion rates, is essential for understanding the role of proteins in the biological processes they are involved. In this work, we characterized CyaY protein family motions as studied by molecular dynamic simulations. We studied three members of this family: I) Homo sapiens frataxin, II) Escherichia coli frataxin, and III) Psychromonas ingrahamii frataxin. We found that the most mobile regions are the ones corresponding to a) the first N-terminus loop (position ~110-120 in all sequences), b) the b5-b6 loop (position ~156-170), and c) the C-terminus (position ~195-210). The local flexibility observed in the simulations is compared to topological factors and the distribution of local energetic frustration calculated with an all atom potentials (FOLDX). We expect that our results contribute to understand the relation between sequence, flexibility, and stability. Further experiments and analysis would aid in the rational tuning of protein function.