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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
1
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
1
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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Ptide absorbed to CAP was consistent with an -helix, whereas when bound to HA the structure corresponded more to a random coil [107]. We studied DPP peptides by FTIR spectroscopy and found the phosphorylated peptides in solution in the presence of HA formed -helical structures and lost their random coil characteristics [108]. Perhaps, through evolution, the most efficient strategy found by nature
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Ptide absorbed to CAP was consistent with an -helix, whereas when bound to HA the structure corresponded more to a random coil [107]. We studied DPP peptides by FTIR spectroscopy and found the phosphorylated peptides in solution in the presence of HA formed -helical structures and lost their random coil characteristics [108]. Perhaps, through evolution, the most efficient strategy found by nature
1
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