Please use this identifier to cite or link to this item: https://doi.org/10.1002/anie.200500261
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. 
Vivekanandan, S. 
Lakshminarayanan, R. 
Jois, S.D.S. 
Kini, R.M. 
Valiyaveettil, S. 
Keywords: Biomineralization
Eggshell
Peptides
Proteins
Structure-activity relationships
Issue Date: 2-Sep-2005
Source: 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
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