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-149 fragment of osteopontin maintained its flexible linear chain structure in solution, stabilizing ACP particles [115]. Additionally, stabilization of calcium-carbonate nanoparticles and creation of nano-porosities within them is due to the IDP mollusk protein, AP7 [37], discussed above, implying this could be a common IDP ineral regulation mechanism. As reviewed elsewhere [116] the initialMatr
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-149 fragment of osteopontin maintained its flexible linear chain structure in solution, stabilizing ACP particles [115]. Additionally, stabilization of calcium-carbonate nanoparticles and creation of nano-porosities within them is due to the IDP mollusk protein, AP7 [37], discussed above, implying this could be a common IDP ineral regulation mechanism. As reviewed elsewhere [116] the initialMatr
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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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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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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 dif
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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 dif
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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