| Online-Ressource |
Verfasst von: | Zaiß, Moritz [VerfasserIn]  |
| Radbruch, Alexander [VerfasserIn]  |
| Bachert, Peter [VerfasserIn]  |
Titel: | MR imaging of protein folding in vitro employing Nuclear-Overhauser-mediated saturation transfer |
Verf.angabe: | Moritz Zaiss, Patrick Kunz, Steffen Goerke, Alexander Radbruch, Peter Bachert |
E-Jahr: | 2013 |
Jahr: | 25 September 2013 |
Umfang: | 8 S. |
Teil: | volume:26 |
| year:2013 |
| number:12 |
| pages:1815-1822 |
| extent:8 |
Fussnoten: | Gesehen am 26.07.2021 |
Titel Quelle: | Enthalten in: NMR in biomedicine |
Ort Quelle: | New York, NY : Wiley, 1988 |
Jahr Quelle: | 2013 |
Band/Heft Quelle: | 26(2013), 12, Seite 1815-1822 |
ISSN Quelle: | 1099-1492 |
Abstract: | MR Z-spectroscopy allows enhanced imaging contrast on the basis of saturation transfer between the proton pools of cellular compounds and water, occurring via chemical exchange (chemical exchange saturation transfer, CEST) or dipole-dipole coupling (nuclear Overhauser effect, NOE). In previous studies, signals observed in the aliphatic proton region of Z-spectra have been assigned to NOEs between protons in water molecules and protons at the surface of proteins. We investigated a possible relationship between the signal strength of NOE peaks in Z-spectra obtained at B0 = 7 T and protein structure. Here, we report a correlation of NOE-mediated saturation transfer with the structural state of bovine serum albumin (BSA), which was monitored by fluorescence spectroscopy. Encouraged by CEST signal changes observed in tumor tissue, our observation also points to a possible contrast mechanism for MRI sensitive to the structural integrity of proteins in cells. Therefore, protein folding should be considered as an additional property affecting saturation transfer between water and proteins, in combination with the microenvironment and physiological quantities, such as metabolite concentration, temperature and pH. Copyright © 2013 John Wiley & Sons, Ltd. |
DOI: | doi:10.1002/nbm.3021 |
URL: | Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.
Volltext ; Verlag: https://doi.org/10.1002/nbm.3021 |
| Volltext: https://analyticalsciencejournals.onlinelibrary.wiley.com/doi/abs/10.1002/nbm.3021 |
| DOI: https://doi.org/10.1002/nbm.3021 |
Datenträger: | Online-Ressource |
Sprache: | eng |
Sach-SW: | bovine serum albumin (BSA) |
| brain tumors |
| cancer |
| chemical exchange saturation transfer (CEST) |
| MRI |
| nuclear Overhauser effect (NOE) |
| protein folding |
K10plus-PPN: | 1764378881 |
Verknüpfungen: | → Zeitschrift |
MR imaging of protein folding in vitro employing Nuclear-Overhauser-mediated saturation transfer / Zaiß, Moritz [VerfasserIn]; 25 September 2013 (Online-Ressource)