Conformational diversity and the emergence of sequence signatures during evolution.
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.
Departamento de Ciencia y Tecnología, Universidad Nacional de Quilmes, Roque Saenz Pena 182, 1876 Bernal, Argentina.
Gustavo
G
Parisi
Departamento de Ciencia y Tecnología, Universidad Nacional de Quilmes, Roque Saenz Pena 182, 1876 Bernal, Argentina.
Diego Javier
DJ
Zea
Departamento de Ciencia y Tecnología, Universidad Nacional de Quilmes, Roque Saenz Pena 182, 1876 Bernal, Argentina.
Alexander Miguel
AM
Monzon
Bioinformactics Unit, Fundación Instituto Leloir, Av. Patricias Argentinas 435, C1405BWE Buenos Aires, Argentina. Electronic address: cmb@leloir.org.ar.
Cristina
C
Marino-Buslje
D000595:Amino Acid Sequence; D000818:Animals; D019143:Evolution, Molecular; D006801:Humans; D008958:Models, Molecular; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000235:genetics
D011506:Proteins