Solid-state NMR spectroscopy to study protein-lipid interactions

• Main Author: Huster, Daniel
• Other Authors: Universität Leipzig, Institut für Medizinische Physik und Biophysik
• Format: Article
• Language: English
• Published: Universitätsbibliothek Leipzig 2015
• Subjects: Kernspinresonanzspektroskopie; NMR-Spektroskopie; Protein-Lipid Wechselwirkungen; Nuclear magnetic resonance spectroscopy; NMR spectroscopy; protein-lipid interactions; ddc:570
• Online Access: http://nbn-resolving.de/urn:nbn:de:bsz:15-qucosa-190961; http://nbn-resolving.de/urn:nbn:de:bsz:15-qucosa-190961; http://www.qucosa.de/fileadmin/data/qucosa/documents/19096/Huster_BBA_2014_08_1841_8.pdf

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.