Triangulating a Tightly Bound Lipid on a Membrane Protein by Paramagnetic Solid-State NMR
Abstract
Nonannular lipids tightly associate with membrane proteins, influencing their structure and function. Here, we present a solid-state NMR (ssNMR)-based strategy to localize such lipids on protein surfaces with a high specificity. We previously identified a tightly bound glycophospholipid which copurifies with Anabaena Sensory Rhodopsin trimers and displays resolved NMR signals. By introducing paramagnetic labels at defined sites and measuring paramagnetic relaxation enhancements (PREs), we triangulate the lipid’s position near a periplasmic intermonomer cleft. Docking calculations guided by PRE restraints further define a nonannular lipid binding site. Our approach provides a broadly applicable framework for mapping tightly bound lipids in membrane proteins under native-like conditions.
Fields of Study & Subjects
Lipid Membrane Structure and Behavior
Advanced NMR Techniques and Applications
Photoreceptor and optogenetics research
Publication details
- Journal / source
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Volume
- 148
- Issue
- 6
- Pages
- 5909–5915
- Publication date
- 5 February 2026
- Language
- EN