Conformational diversity and the emergence of sequence signatures during evolution

Current Opinion in Structural Biology
Gustavo ParisiCristina Marino-Buslje

Abstract

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.

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Citations

Mar 30, 2016·Database : the Journal of Biological Databases and Curation·Alexander Miguel MonzonGustavo Parisi
Apr 3, 2016·Protein Science : a Publication of the Protein Society·Diego Javier ZeaGustavo Parisi
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Mar 24, 2017·Molecular Biology and Evolution·Avital Sharir-Ivry, Yu Xia
Oct 3, 2018·Physical Chemistry Chemical Physics : PCCP·Rodrigo Dorantes-GilardiClaire Lesieur
Jul 6, 2019·European Biophysics Journal : EBJ·Tadeo E SaldañoSebastian Fernandez-Alberti
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Mar 29, 2020·Journal of Chemical Information and Modeling·Tadeo E SaldañoSebastian Fernandez-Alberti
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Aug 12, 2021·Physical Chemistry Chemical Physics : PCCP·Sergei F Chekmarev
Oct 29, 2021·Frontiers in Molecular Biosciences·Lorenza PaciniClaire Lesieur

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