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https://olympias.lib.uoi.gr/jspui/handle/123456789/17129Full metadata record
| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Floudas, G. | en |
| dc.contributor.author | Spiess, H. W. | en |
| dc.date.accessioned | 2015-11-24T18:35:44Z | - |
| dc.date.available | 2015-11-24T18:35:44Z | - |
| dc.identifier.issn | 1022-1336 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/17129 | - |
| dc.rights | Default Licence | - |
| dc.subject | dielectric spectroscopy | en |
| dc.subject | dynamics | en |
| dc.subject | glass transition | en |
| dc.subject | nmr | en |
| dc.subject | polypeptides | en |
| dc.subject | self-assembly | en |
| dc.subject | solid-state nmr | en |
| dc.subject | functionalized polyphenylene dendrimers | en |
| dc.subject | acid n-carboxyanhydrides | en |
| dc.subject | electric dipole moment | en |
| dc.subject | molecular-dynamics | en |
| dc.subject | glass-transition | en |
| dc.subject | block-copolymers | en |
| dc.subject | alpha-helix | en |
| dc.subject | dielectric properties | en |
| dc.subject | poly(gamma-benzyl l-glutamate) | en |
| dc.title | Self-Assembly and Dynamics of Polypeptides | en |
| heal.type | journalArticle | - |
| heal.type.en | Journal article | en |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.identifier.primary | DOI 10.1002/marc.200800700 | - |
| heal.identifier.secondary | <Go to ISI>://000263872600005 | - |
| heal.identifier.secondary | http://onlinelibrary.wiley.com/store/10.1002/marc.200800700/asset/278_ftp.pdf?v=1&t=h0xk9s3i&s=78062c3f0f664193b5aa55b5f2dd54524f686e5f | - |
| heal.language | en | - |
| heal.access | campus | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών και Τεχνολογιών. Τμήμα Βιολογικών Εφαρμογών και Τεχνολογιών | el |
| heal.publicationDate | 2009 | - |
| heal.abstract | This work highlights the results of recent efforts to understand the hierarchical self-assembly and dynamics of polypeptides with the aid of different NMR techniques, X-ray scattering, and dielectric spectroscopy. The concerted application of these techniques sheds light on the origin of the glass transition, the persistence of the a-helical peptide secondary motif, and the effects of topology and packing on the type and persistence of secondary structures. With respect to the freezing of the dynamics at the liquid-to-glass temperature it was found that the origin of this effect is a network of defected hydrogen bonds. The presence of defected hydrogen-bonded regions reduces the persistence length of a-helices. Block copolypeptides provide means to manipulate both the type and persistence of peptide secondary structures. | en |
| heal.journalName | Macromol Rapid Commun | en |
| heal.journalType | peer reviewed | - |
| heal.fullTextAvailability | TRUE | - |
| Appears in Collections: | Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά) | |
Files in This Item:
| File | Description | Size | Format | |
|---|---|---|---|---|
| Floudas-2009-Self-Assembly and Dy.pdf | 1.55 MB | Adobe PDF | View/Open Request a copy |
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