Please use this identifier to cite or link to this item:
|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|
Show full item record
Files in This Item:
There are no files associated with this item.
checked on Feb 22, 2020
WEB OF SCIENCETM
checked on Jul 1, 2019
checked on Feb 18, 2020
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.