Conformational diversity and the emergence of sequence signatures during evolution

作者: Gustavo Parisi , Diego Javier Zea , Alexander Miguel Monzon , Cristina Marino-Buslje

DOI: 10.1016/J.SBI.2015.02.005

关键词: Function (biology)CoevolutionEnzymeProtein structureBiologyPeptide sequenceAllosteric regulationSequence (medicine)GeneticsEvolutionary biologyConformational isomerism

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

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