Please use this identifier to cite or link to this item:
https://olympias.lib.uoi.gr/jspui/handle/123456789/23010Full metadata record
| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Sanfelice, D. | en |
| dc.contributor.author | Tancredi, T. | en |
| dc.contributor.author | Politou, A. | en |
| dc.contributor.author | Pastore, A. | en |
| dc.contributor.author | Temussi, P. A. | en |
| dc.date.accessioned | 2015-11-24T19:30:00Z | - |
| dc.date.available | 2015-11-24T19:30:00Z | - |
| dc.identifier.issn | 1520-5126 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/23010 | - |
| dc.rights | Default Licence | - |
| dc.subject | Acrylic Resins/pharmacology | en |
| dc.subject | *Cold Temperature | en |
| dc.subject | Magnetic Resonance Spectroscopy | en |
| dc.subject | Muscle Proteins/*chemistry/*metabolism | en |
| dc.subject | Polyethylene Glycols/pharmacology | en |
| dc.subject | Protein Binding/drug effects | en |
| dc.subject | Protein Denaturation | en |
| dc.subject | Protein Kinases/*chemistry/*metabolism | en |
| dc.subject | Protein Stability | en |
| dc.subject | Thermodynamics | en |
| dc.title | Cold denaturation and aggregation: a comparative NMR study of titin I28 in bulk and in a confined environment | en |
| heal.type | journalArticle | - |
| heal.type.en | Journal article | en |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.identifier.primary | 10.1021/ja904462n | - |
| heal.identifier.secondary | http://www.ncbi.nlm.nih.gov/pubmed/19653628 | - |
| heal.identifier.secondary | http://pubs.acs.org/doi/pdfplus/10.1021/ja904462n | - |
| heal.language | en | - |
| heal.access | campus | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικής | el |
| heal.publicationDate | 2009 | - |
| heal.abstract | An NMR study of the thermal stability of titin I28 in the temperature range from -16 to 65 degrees C showed that this protein can undergo cold denaturation at physiological conditions. This is the second case of a protein undergoing unbiased cold denaturation. Comparison of the stability curves in buffer and in crowded conditions shows that it is possible to measure thermodynamics parameters for unfolding even when proteins aggregate at high temperature. The use of confinement in polyacrylamide gels, with the addition of polyethylene glycol, allows easy access to subzero temperatures that might enable studies of cold denaturation of many proteins. | en |
| heal.journalName | J Am Chem Soc | en |
| heal.journalType | peer-reviewed | - |
| heal.fullTextAvailability | TRUE | - |
| Appears in Collections: | Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά) - ΙΑΤ | |
Files in This Item:
| File | Description | Size | Format | |
|---|---|---|---|---|
| Sanfelice-2009-Cold denaturation an.pdf | 157.64 kB | Adobe PDF | View/Open Request a copy |
This item is licensed under a Creative Commons License
