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TitleProtein β-interfaces as a generic source of native peptide tectons
Publication TypeJournal Article
Year of Publication2013
AuthorsValéry, C., Pandey R., and Gerrard J.A.
JournalChemical Communications
Pagination2825 - 2827
Date Published2013
ISSN13597345 (ISSN)
Keywordsamino acid sequence, Animals, article, beta lactoglobulin, beta sheet, Carboxy-Lyases, cattle, diaminopimelic acid, dilution, Electron microscopy, Escherichia coli Proteins, Infrared spectroscopy, Lactoglobulins, Models, Molecular, Nanostructures, nonhuman, peptide, Peptide Fragments, peroxiredoxin 3, Peroxiredoxin III, pH, protein, Protein Conformation, Protein Multimerization, protein secondary structure, water
AbstractMotifs of 7-8 amino acids were designed from the β-continuous interfaces of non-related homo-oligomeric proteins. These peptides intrinsically self-assembled into nanoarchitectures in water, while retaining some properties of their parent interfaces, especially reversibility of assembly. These results reveal a novel source of native peptide tectons. © The Royal Society of Chemistry 2013.

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