On the emergence of orientational order in folded proteins with implications for allostery

  title={On the emergence of orientational order in folded proteins with implications for allostery},
  author={Debayan Chakraborty and Mauro Lorenzo Mugnai and D. Thirumalai},
The beautiful structures of single and multi-domain proteins are clearly ordered in some fashion but cannot be readily classified using group theory methods that are successfully used to describe periodic crystals. For this reason, protein structures are considered to be aperiodic, and may have evolved this way for functional purposes, especially in instances that require a combination of softness and rigidity within the same molecule. By analyzing the solved protein structures, we show that… 


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A fundamental requirement for a body supporting fluctuation-induced allostery is a strongly inhomogeneous elastic modulus, reflected in many real proteins, where a good approximation of the elastic structure maps strongly coherent domains onto rigid blocks connected by more flexible interface regions.
Protein topology and allostery.
  • Juan Xie, L. Lai
  • Biology, Medicine
    Current opinion in structural biology
  • 2020
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Structural rigidity is shown to be a fundamental underlying property that promotes cooperativity and non-locality seen in allostery and is associated with a general global change in rigidity associated with allosteric transitions where the R state is more rigid than the T state.
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It is established that changes to the conformational landscapes of proteins are an essential aspect of molecular evolution and that change in function can be achieved through enrichment of preexisting conformational sub-states.