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Ro-fibrils. This was suggested to be crucial for HA mineral nucleation [59]. Self-assembly is thus another way that the IDP proteins can regulate the process of biomineralization.Author Manuscript Author Manuscript Author Manuscript Author Manuscript3. Potential Mechanisms of IDP Action: BiomineralizationThere must be precise reasons why so many IDP proteins are associated with mineralization. It
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F the IDP domain containing an asparagine and proline (Asn- and Pro)-rich region, with glycine (Gly)- and glutamine (Gln)-rich repeats mid-sequence is implicated in self- assembly. Based on analytical ultracentrifugation, the glycine-rich region oligomerizes to form large protein assemblies. The proline-rich region also shows a self-Author Manuscript Author Manuscript Author Manuscript Author Man
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Ficient RNA replication resulting in almost 200000 RNA copies [27] from each RNAFicient RNA replication resulting in almost 200000 RNA copies [27] from each RNA template . Although replication-deficient particles provide a high level of safety, there is still a marginal risk of the generation of replication-proficient particles through nonhomologous recombination. To minimize this risk, spli

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E to the change in entropy S, when an unstructured protein is bound and folded (transiently), is smaller than when a structured protein is bound ( G = H S). This concept may be debated, however, due to the relative order of the IDP vs. the dis-order of water upon IDP-partner binding in aqueous media. ii) An open structure gives an IDP the ability to bind to more than one partner and present di

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