dc.contributor.author | Tamamis, Phanourios | en |
dc.contributor.author | Kasotakis, E. | en |
dc.contributor.author | Archontis, Georgios Z. | en |
dc.contributor.author | Mitraki, A. | en |
dc.creator | Tamamis, Phanourios | en |
dc.creator | Kasotakis, E. | en |
dc.creator | Archontis, Georgios Z. | en |
dc.creator | Mitraki, A. | en |
dc.date.accessioned | 2019-12-02T15:33:32Z | |
dc.date.available | 2019-12-02T15:33:32Z | |
dc.date.issued | 2014 | |
dc.identifier.issn | 1064-3745 | |
dc.identifier.uri | http://gnosis.library.ucy.ac.cy/handle/7/59108 | |
dc.description.abstract | Self-assembling peptides that can form supramolecular structures such as fibrils, ribbons, and nanotubes are of particular interest to modern bionanotechnology and materials science. Their ability to form biocompatible nanostructures under mild conditions through non-covalent interactions offers a big biofabrication advantage. Structural motifs extracted from natural proteins are an important source of inspiration for the rational design of such peptides. Examples include designer self-assembling peptides that correspond to natural coiled-coil motifs, amyloid-forming proteins, and natural fibrous proteins. In this chapter, we focus on the exploitation of structural information from beta-structured natural fibers. We review a case study of short peptides that correspond to sequences from the adenovirus fiber shaft. We describe both theoretical methods for the study of their self-assembly potential and basic experimental protocols for the assessment of fibril-forming assembly. © Springer Science+Business Media New York 2014. | en |
dc.source | Methods in Molecular Biology | en |
dc.source.uri | https://www.scopus.com/inward/record.uri?eid=2-s2.0-84921842579&doi=10.1007%2f978-1-4939-1486-9_3&partnerID=40&md5=8613441bd53b42b46ee685f571839595 | |
dc.subject | algorithm | en |
dc.subject | priority journal | en |
dc.subject | amino acid sequence | en |
dc.subject | unclassified drug | en |
dc.subject | Article | en |
dc.subject | physiology | en |
dc.subject | chemistry | en |
dc.subject | Peptides | en |
dc.subject | protein tertiary structure | en |
dc.subject | Molecular dynamics | en |
dc.subject | Nanostructures | en |
dc.subject | low temperature | en |
dc.subject | X ray diffraction | en |
dc.subject | nanomaterial | en |
dc.subject | nanofiber | en |
dc.subject | beta sheet | en |
dc.subject | protein secondary structure | en |
dc.subject | amino terminal sequence | en |
dc.subject | peptide | en |
dc.subject | Protein Structure, Tertiary | en |
dc.subject | Protein Structure, Secondary | en |
dc.subject | conformational transition | en |
dc.subject | transmission electron microscopy | en |
dc.subject | high temperature | en |
dc.subject | Self-assembly | en |
dc.subject | nanotube | en |
dc.subject | peptide synthesis | en |
dc.subject | Implicit solvent | en |
dc.subject | Adenovirus | en |
dc.subject | Replica-exchange | en |
dc.subject | Adenoviridae | en |
dc.subject | adenovirus fiber | en |
dc.subject | amyloid | en |
dc.subject | Amyloid fibrils | en |
dc.subject | Beta-structure | en |
dc.subject | dodecapeptide | en |
dc.subject | fibril forming peptide | en |
dc.subject | nanofibril | en |
dc.subject | nanoribbon | en |
dc.subject | octapeptide | en |
dc.subject | Peptide Biosynthesis | en |
dc.subject | transition temperature | en |
dc.subject | uranyl acetate | en |
dc.title | Combination of theoretical and experimental approaches for the design and study of fibril-forming peptides | en |
dc.type | info:eu-repo/semantics/article | |
dc.identifier.doi | 10.1007/978-1-4939-1486-9_3 | |
dc.description.volume | 1216 | |
dc.description.startingpage | 53 | |
dc.description.endingpage | 70 | |
dc.author.faculty | Σχολή Θετικών και Εφαρμοσμένων Επιστημών / Faculty of Pure and Applied Sciences | |
dc.author.department | Τμήμα Φυσικής / Department of Physics | |
dc.type.uhtype | Article | en |
dc.description.notes | <p>Cited By :4</p> | en |
dc.source.abbreviation | Methods Mol. Biol. | en |
dc.contributor.orcid | Archontis, Georgios Z. [0000-0002-7750-8641] | |
dc.contributor.orcid | Tamamis, Phanourios [0000-0002-3342-2651] | |
dc.gnosis.orcid | 0000-0002-7750-8641 | |
dc.gnosis.orcid | 0000-0002-3342-2651 | |