- AutorIn
- Daniel Huster
- Titel
- Solid-state NMR spectroscopy to study protein-lipid interactions
- Zitierfähige Url:
- https://nbn-resolving.org/urn:nbn:de:bsz:15-qucosa-190961
- Quellenangabe
- Biochimica et biophysica acta : Molecular and cell biology of lipids (2014), Aug, 1841(8):1146-1160
- Erstveröffentlichung
- 2014
- DOI
- https://doi.org/10.1016/jbbalip.2013.12.002
- Abstract (EN)
- The appropriate lipid environment is crucial for the proper function of membrane proteins. There is a tremendous variety of lipid molecules in the membrane and so far it is often unclear which component of the lipid matrix is essential for the function of a respective protein. Lipid molecules and proteins mutually influence each other; parameters such as acyl chain order, membrane thickness, membrane elasticity, permeability, lipid-domain and annulus formation are strongly modulated by proteins. More recent data also indicates that the influence of proteins goes beyond a single annulus of next-neighbor boundary lipids. Therefore, a mesoscopic approach to membrane lipid-protein interactions in terms of elastic membrane deformations has been developed. Solid-state NMR has greatly contributed to the understanding of lipid-protein interactions and the modern view of biological membranes. Methods that detect the influence of proteins on the membrane as well as direct lipid-protein interactions have been developed and are reviewed here. Examples for solid-state NMR studies on the interaction of Ras proteins, the antimicrobial peptide protegrin-1, the G protein-coupled receptor rhodopsin, and the K+ channel KcsA are discussed.
- Andere Ausgabe
- DOI: 10.1016/jbbalip.2013.12.002
- Link zur Originalpublikation in der Zeitschrift Biochimica et biophysica acta : Molecular and cell biology of lipids
Link: http://dx.doi.org/10.1016/jbbalip.2013.12.002 - Freie Schlagwörter (DE)
- Kernspinresonanzspektroskopie, NMR-Spektroskopie, Protein-Lipid Wechselwirkungen
- Freie Schlagwörter (EN)
- Nuclear magnetic resonance spectroscopy, NMR spectroscopy, protein-lipid interactions
- Klassifikation (DDC)
- 570
- Herausgeber (Institution)
- Universität Leipzig
- Verlag
- Universität Leipzig, Leipzig
- URN Qucosa
- urn:nbn:de:bsz:15-qucosa-190961
- Veröffentlichungsdatum Qucosa
- 07.12.2015
- Dokumenttyp
- Artikel
- Sprache des Dokumentes
- Englisch