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Tructures on binding. 2.4 Self-Assembly of IDPs IDPs frequently undergo self-assembly. The extended conformation of IDPs facilitates the intermolecular interactions between them and promotes formation of supramolecular architecture [109]. This is illustrated in some of the mineralized tissues discussed above. Silaffins, for example, are protein constituents of biosilica, playing an active role in
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Tructures on binding. 2.4 Self-Assembly of IDPs IDPs frequently undergo self-assembly. The extended conformation of IDPs facilitates the intermolecular interactions between them and promotes formation of supramolecular architecture [109]. This is illustrated in some of the mineralized tissues discussed above. Silaffins, for example, are protein constituents of biosilica, playing an active role in
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Tructures on binding. 2.4 Self-Assembly of IDPs IDPs frequently undergo self-assembly. The extended conformation of IDPs facilitates the intermolecular interactions between them and promotes formation of supramolecular architecture [109]. This is illustrated in some of the mineralized tissues discussed above. Silaffins, for example, are protein constituents of biosilica, playing an active role in
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Tructures on binding. 2.4 Self-Assembly of IDPs IDPs frequently undergo self-assembly. The extended conformation of IDPs facilitates the intermolecular interactions between them and promotes formation of supramolecular architecture [109]. This is illustrated in some of the mineralized tissues discussed above. Silaffins, for example, are protein constituents of biosilica, playing an active role in
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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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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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An N-terminus with small acidic motif (DSpSpEE) that is also found in SIBLING proteins [65]. When solubilized, statherin has a random coil conformation. When bound to HA, it takes on a more alpha-helical structure exposing a bacterial binding site [63], leading to bacterial entrapment. Another example is the role of the IDP, DMP1, in preventing kidney and cardiovascular calcification. The double k
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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 Manu