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|Title:||Mimicking the function of eggshell matrix proteins: The role of multiplets of charged amino acid residues and self-assembly of peptides in biomineralization||Authors:||Ajikumar, P.K.
|Issue Date:||2-Sep-2005||Citation:||Ajikumar, P.K., Vivekanandan, S., Lakshminarayanan, R., Jois, S.D.S., Kini, R.M., Valiyaveettil, S. (2005-09-02). Mimicking the function of eggshell matrix proteins: The role of multiplets of charged amino acid residues and self-assembly of peptides in biomineralization. Angewandte Chemie - International Edition 44 (34) : 5476-5479. ScholarBank@NUS Repository. https://doi.org/10.1002/anie.200500261||Abstract:||(Figure Presented) An eggshell finish: Designed peptides can be used as a tool to unravel the structure-activity relationships of eggshell matrix proteins. The ordered arrangement of doublets of charged residues on the peptide and its self-assembling characteristics play a key role in the biomimetic nucleation of polycrystalline calcite crystal aggregates (see picture), which models that initiated by the goose eggshell matrix protein, ansocalcin. © 2005 Wiley-VCH Verlag GmbH & Co. KGaA.||Source Title:||Angewandte Chemie - International Edition||URI:||http://scholarbank.nus.edu.sg/handle/10635/53033||ISSN:||14337851||DOI:||10.1002/anie.200500261|
|Appears in Collections:||Staff Publications|
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