Structural and dynamical transitions in Ankyrin repeat proteins

PARRA, RG; ESPADA R; VERSTRAETE, N; FERREIRO DU

Belo Horizonte

Conferencia; 3rd ISCB Latin American Conference / X Meeting; 2014

ISCB

Repeat proteins are made up of tandem arrays of similar 20~40 amino acid stretches that usually fold up in elongated architectures mainly stabilized by local interactions. Due to their simple and linear structure that lacks of sequence-distant contacts, these proteins represent a useful model to studyprotein folding, dynamics and function. Ankyrin Repeat Proteins (ARPs) are widely distributed in nature. Their ?biological function? is usually attributed as mediating specific protein-protein interactions with versatility for recognition paralleled to that of antibodies. These proteins usually show sophisticated behaviours that are incontrast with their apparently simple structure. We have calculated and analyzed several parameters in order to dissect theenergetic contributions that underlie the conformational transitions thatcontribute to ARPs function. We have collected, processed and depurated all available ARPs sequences, structures and other publicly available data to build a relational database from which we aim to extract information to better understand how these proteins work. We focused in localizing, analyzing and quantifying frustration in ARPs structures.