The intrinsic dynamics, encoded in proteins’ sequences and structures, are utilized by stimuli to trigger allosteric and functional actions.
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The modes of allosteric actions of modular units of biological assemblies evolve as the complexity of organisms increases.
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Emerging computational tools provide new insights into understanding protein dynamics and allosteric effects.
Allosteric behavior is central to the function of many proteins, enabling molecular machinery, metabolism, signaling and regulation. Recent years have shown that the intrinsic dynamics of allosteric proteins defined by their 3-dimensional architecture or by the topology of inter-residue contacts favors cooperative motions that bear close similarity to structural changes they undergo during their allosteric actions. These conformational motions are usually driven by energetically favorable or soft modes at the low frequency end of the mode spectrum, and they are evolutionarily conserved among orthologs. These observations brought into light evolutionary adaptation mechanisms that help maintain, optimize or regulate allosteric behavior as the evolution from bacterial to higher organisms introduces sequential heterogeneities and structural complexities.