Abstract
The fact that membrane proteins are notoriously difficult to analyse using standard protocols for atomic-resolution structure determination methods have motivated adaptation of these techniques to membrane protein studies as well as development of new technologies. With this motivation, liquid-state nuclear magnetic resonance (NMR) has recently been used with success for studies of peptides and membrane proteins in detergent micelles, and solid-state NMR has undergone a tremendous evolution towards characterization of membrane proteins in native membrane and oriented phospholipid bilayers. In this mini-review, we describe some of the technological challenges behind these efforts and provide examples on their use in membrane biology.
| Originalsprog | Engelsk |
|---|---|
| Tidsskrift | Molecular Membrane Biology |
| Vol/bind | 21 |
| Udgave nummer | 3 |
| Sider (fra-til) | 129-141 |
| ISSN | 0968-7688 |
| DOI | |
| Status | Udgivet - 2004 |
| Udgivet eksternt | Ja |
Bibliografisk note
This article has been found as a ’Free Version’ from the Publisher on June 23 2020. When access to the article closes, please notify [email protected]Emneord
- Alamethicin
- Bacteriorhodopsin
- Ca -ATPase 2+
- Membrane proteins
- NMR spectroscopy
- Structure determination