Conformational diversity and the emergence of sequence signatures during protein evolution.

GUSTAVO PARISI; DIEGO ZEA; ALEXANDER MONZON; CRISTINA MARINO BUSLJE

CURRENT OPINION IN STRUCTURAL BIOLOGY

CURRENT BIOLOGY LTD

Año: 2015

0959-440X

Proteins? native structure is an ensemble of conformers in equilibrium, including all their respective functional states and intermediates. The induced-fit first and the pre-equilibrium theories later, described how structural changes are required to explain the allosteric and cooperative behaviours in proteins, which are key to protein function. The conformational ensemble concept has become a key tool in explaining an endless list of essential protein properties such as function, enzyme and antibody promiscuity, signal transduction, protein?protein recognition, origin of diseases, origin of new protein functions, evolutionary rate and order?disorder transitions, among others. Conformational diversity is encoded by the amino acid sequence and such a signature can be evidenced through evolutionary studies as evolutionary rate, conservation and coevolution