Structural and Chemical Characteristics of Extreme Temperature Adapted Proteins Investigated Using Molecular Dynamics

BUSTAMANTE, JUAN PABLO; BOECHI, LEONARDO; MARTÍ, MARCELO ADRIÁN; ESTRIN, DARÍO

Congreso; 2do Congreso Argentino de Bioinformática y Biología Computacional; 2011

In nature there are organisms that are adapted to live at extreme temperatures. Despite of that, in some cases it has found that these organisms that living at standard conditions share proteins evolutionary related (with high similarity between amino acid sequence). To understand the structural and dynamics differences that allow these proteins to be functionally active at such extreme temperatures, we have studied three hemeproteins from the same subfamily of proteins (truncated hemoglobins, trHb), that belong to organisms living at drastically different conditions: very high (Thermobifida fusca), very low (P haloplanktis), and moderate (Mycobacterium tuberculosis) temperatures, respectively. Molecular dynamics simulations of differents trHB at some temperatures (300K and 360K) were performed. Several structural parameters were analyzed: the radius of gyration (Rg), RMSD, residue flexibility, distances between active site residues and cavities, as well as the O2 affinity for each protein.