Please use this identifier to cite or link to this item:
https://olympias.lib.uoi.gr/jspui/handle/123456789/16453Full metadata record
| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Gitsas, A. | en |
| dc.contributor.author | Floudas, G. | en |
| dc.contributor.author | Mondeshki, M. | en |
| dc.contributor.author | Spiess, H. W. | en |
| dc.contributor.author | Aliferis, T. | en |
| dc.contributor.author | Iatrou, H. | en |
| dc.contributor.author | Hadjichristidis, N. | en |
| dc.date.accessioned | 2015-11-24T18:31:21Z | - |
| dc.date.available | 2015-11-24T18:31:21Z | - |
| dc.identifier.issn | 0024-9297 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/16453 | - |
| dc.rights | Default Licence | - |
| dc.subject | functionalized polyphenylene dendrimers | en |
| dc.subject | angle-spinning nmr | en |
| dc.subject | poly-l-alanine | en |
| dc.subject | solid-state | en |
| dc.subject | block-copolymers | en |
| dc.subject | cross-polarization | en |
| dc.subject | diblock copolymers | en |
| dc.subject | molecular-dynamics | en |
| dc.subject | alpha-helix | en |
| dc.subject | x-ray | en |
| dc.title | Control of Peptide Secondary Structure and Dynamics in Poly(gamma-benzyl-L-glutamate)-b-polyalanine Peptides | en |
| heal.type | journalArticle | - |
| heal.type.en | Journal article | en |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.identifier.primary | Doi 10.1021/Ma801770b | - |
| heal.identifier.secondary | <Go to ISI>://000260612700044 | - |
| heal.identifier.secondary | http://pubs.acs.org/doi/pdfplus/10.1021/ma801770b | - |
| heal.language | en | - |
| heal.access | campus | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών και Τεχνολογιών. Τμήμα Βιολογικών Εφαρμογών και Τεχνολογιών | el |
| heal.publicationDate | 2008 | - |
| heal.abstract | The stability, persistence and dynamics of the peptide secondary motifs are investigated in a series of poly(gamma-benZyl-L-glutainate)-b-polyalanine (PBLG-b-PAla) polypeptides through a combination of structural (X-rays, NMR) and dynamic (Dielectric Spectroscopy, NMR) probes. The unfavorable enthalpic interactions between the unlike blocks give rise to nanophase separation that results in the destabilization of PAla beta-sheets. Contrary to. this, the overall helicity of PBLG alpha-helices is enhanced. The dynamics of the "defected" amorphous segments and of the more ordered segments are studied by DS and C-13 NMR, respectively. These probes provide information on the time scale and the mechanism of molecular and supramolecular motion. | en |
| heal.journalName | Macromolecules | en |
| heal.journalType | peer reviewed | - |
| heal.fullTextAvailability | TRUE | - |
| Appears in Collections: | Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά) | |
Files in This Item:
| File | Description | Size | Format | |
|---|---|---|---|---|
| Gitsas-2008-Control of Peptide S.pdf | 429.98 kB | Adobe PDF | View/Open Request a copy |
This item is licensed under a Creative Commons License
