title: Teaching noncovalent interactions using protein molecular evolution.
abstract: Noncovalent interactions and physicochemical properties of amino acids are important topics in biochemistry courses. Here, we present a computational laboratory where the capacity of each of the 20 amino acids to maintain different noncovalent interactions are used to investigate the stabilizing forces in a set of proteins coming from organisms adapted to different environments. Using protein sequence and structure information it is possible to evaluate the noncovalent contributions to the stabilization of a given protein fold. As a case study, we use the protein lumazine synthase from three different organisms adapted to live in extreme temperatures: one psychrophilic (optimal growth temperature, 0-20 °C), one mesophilic (optimal growth temperature, 20-50 °C), and one thermophilic (optimal growth temperature, 80-110 °C). We found that this computational laboratory for biochemistry and molecular biology courses enhances student amino acid noncovalent interaction understanding and how these interactions are involved in protein stability.
authors: Centro de Estudios e Investigaciones, Universidad Nacional de Quilmes, 1876 Bernal, Argentina.
authors: María Silvina
authors: MS
authors: Fornasari
authors: Gustavo
authors: G
authors: Parisi
authors: Julián
authors: J
authors: Echave