Please use this identifier to cite or link to this item:
https://olympias.lib.uoi.gr/jspui/handle/123456789/16357Full metadata record
| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Koynov, K. | en |
| dc.contributor.author | Mihov, G. | en |
| dc.contributor.author | Mondeshki, M. | en |
| dc.contributor.author | Moon, C. | en |
| dc.contributor.author | Spiess, H. W. | en |
| dc.contributor.author | Mullen, K. | en |
| dc.contributor.author | Butt, H. J. | en |
| dc.contributor.author | Floudas, G. | en |
| dc.date.accessioned | 2015-11-24T18:30:19Z | - |
| dc.date.available | 2015-11-24T18:30:19Z | - |
| dc.identifier.issn | 1525-7797 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/16357 | - |
| dc.rights | Default Licence | - |
| dc.subject | solid-state nmr | en |
| dc.subject | dynamics | en |
| dc.subject | diagnostics | en |
| dc.subject | stability | en |
| dc.subject | polymers | en |
| dc.title | Diffusion and conformation of peptide-functionalized polyphenylene dendrimers studied by fluorescence correlation and C-13 NMR spectroscopy | en |
| heal.type | journalArticle | - |
| heal.type.en | Journal article | en |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.identifier.primary | Doi 10.1021/Bm0702760 | - |
| heal.identifier.secondary | <Go to ISI>://000246413600047 | - |
| heal.identifier.secondary | http://pubs.acs.org/doi/abs/10.1021/bm0702760 | - |
| heal.language | en | - |
| heal.access | campus | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών και Τεχνολογιών. Τμήμα Βιολογικών Εφαρμογών και Τεχνολογιών | el |
| heal.publicationDate | 2007 | - |
| heal.abstract | We report on the combined use of fluorescence correlation spectroscopy (FCS) and H-1 and C-13 NMR spectroscopy to detect the size and type of peptide secondary structures in a series of poly-Z-L-lysine functionalized polyphenylene dendrimers bearing the fluorescent perylenediimide core in solution. In dilute solution, the size of the molecule as detected from FCS and H-1 NMR diffusion measurements matches nicely. We show that FCS is a sensitive probe of the core size as well as of the change in the peptide secondary structure. However, FCS is less sensitive to functionality. A change in the peptide secondary conformation from beta-sheets to alpha-helices detected by C-13 NMR spectroscopy gives rise to a steep increase in the hydrodynamic radii for number of residues n >= 16. Nevertheless, helices are objects of low persistence. | en |
| heal.journalName | Biomacromolecules | en |
| heal.journalType | peer reviewed | - |
| heal.fullTextAvailability | TRUE | - |
| Appears in Collections: | Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά) | |
Files in This Item:
There are no files associated with this item.
This item is licensed under a Creative Commons License
