Teaching non-covalent interactions using protein molecular evolution

17. FORNASARI, MS, PARISI, G AND ECHAVE, J.

BIOCHEMISTRY AND MOLECULAR BIOLOGY EDUCATION

JOHN WILEY & SONS INC

Año: 2008 vol. 36 p. 284 - 286

1470-8175

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 8C), one mesophilic (optimal growth temperature, 20–50 8C), and one thermophilic (optimal growth temperature, 80–110 8C). 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.