Please use this identifier to cite or link to this item:
https://olympias.lib.uoi.gr/jspui/handle/123456789/16077
Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Papadopoulos, P. | en |
dc.contributor.author | Floudas, G. | en |
dc.contributor.author | Schnell, I. | en |
dc.contributor.author | Klok, H. A. | en |
dc.contributor.author | Aliferis, T. | en |
dc.contributor.author | Iatrou, H. | en |
dc.contributor.author | Hadjichristidis, N. | en |
dc.date.accessioned | 2015-11-24T18:27:42Z | - |
dc.date.available | 2015-11-24T18:27:42Z | - |
dc.identifier.issn | 0021-9606 | - |
dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/16077 | - |
dc.rights | Default Licence | - |
dc.subject | dielectric-spectroscopy | en |
dc.subject | neutron-scattering | en |
dc.subject | ribonuclease-a | en |
dc.subject | relaxation | en |
dc.subject | dynamics | en |
dc.subject | liquids | en |
dc.subject | protein | en |
dc.subject | myoglobin | en |
dc.subject | formers | en |
dc.title | Glass transition in peptides: Temperature and pressure effects | en |
heal.type | journalArticle | - |
heal.type.en | Journal article | en |
heal.type.el | Άρθρο Περιοδικού | el |
heal.identifier.primary | Doi 10.1063/1.1931657 | - |
heal.identifier.secondary | <Go to ISI>://000229858500073 | - |
heal.identifier.secondary | http://link.aip.org/getpdf/servlet/GetPDFServlet?filetype=pdf&id=JCPSA6000122000022224906000001 | - |
heal.language | en | - |
heal.access | campus | - |
heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών και Τεχνολογιών. Τμήμα Βιολογικών Εφαρμογών και Τεχνολογιών | el |
heal.publicationDate | 2005 | - |
heal.abstract | We report on the origin of the liquid-to-glass transition in a series of oligopeptides of gamma-benzyl-L-glutamate up to the polymer (PBLG), and in Poly-Z-L-lysine (PZLL) and Polyglycine (PGly) using dielectric spectroscopy as a function of temperature and pressure. We show that temperature is the dominant control variable of the dynamics associated with the peptidic "glass transition." This is an intrinsic feature of the peptide dynamics, irrespective of the type of amino acid and of the peptide secondary structure. The influence of the type of secondary structure (alpha helix vs beta sheet) on the liquid-to-glass dynamics is discussed. | en |
heal.journalName | Journal of Chemical Physics | en |
heal.journalType | peer reviewed | - |
heal.fullTextAvailability | TRUE | - |
Appears in Collections: | Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά) |
Files in This Item:
File | Description | Size | Format | |
---|---|---|---|---|
Papadopoulos-2005-_Glass transition_ i.pdf | 250.23 kB | Adobe PDF | View/Open Request a copy |
This item is licensed under a Creative Commons License