| Autor: |
Lalli D; Centre de RMN à Très Hauts Champs, Institut des Sciences Analytiques (UMR 5280 - CNRS, ENS Lyon, UCB Lyon 1), Université de Lyon , 69100 Villeurbanne, France., Idso MN; Department of Chemical Engineering, University of California , Santa Barbara, California 93106, United States., Andreas LB; Centre de RMN à Très Hauts Champs, Institut des Sciences Analytiques (UMR 5280 - CNRS, ENS Lyon, UCB Lyon 1), Université de Lyon , 69100 Villeurbanne, France., Hussain S; Department of Chemical Engineering, University of California , Santa Barbara, California 93106, United States., Baxter N; Department of Chemistry and Biochemistry, University of California , Santa Barbara, California 93106, United States., Han S; Department of Chemical Engineering, University of California , Santa Barbara, California 93106, United States.; Department of Chemistry and Biochemistry, University of California , Santa Barbara, California 93106, United States., Chmelka BF; Department of Chemical Engineering, University of California , Santa Barbara, California 93106, United States., Pintacuda G; Centre de RMN à Très Hauts Champs, Institut des Sciences Analytiques (UMR 5280 - CNRS, ENS Lyon, UCB Lyon 1), Université de Lyon , 69100 Villeurbanne, France. |
| Abstrakt: |
The structures and properties of membrane proteins in lipid bilayers are expected to closely resemble those in native cell-membrane environments, although they have been difficult to elucidate. By performing solid-state NMR measurements at very fast (100 kHz) magic-angle spinning rates and at high (23.5 T) magnetic field, severe sensitivity and resolution challenges are overcome, enabling the atomic-level characterization of membrane proteins in lipid environments. This is demonstrated by extensive 1 H-based resonance assignments of the fully protonated heptahelical membrane protein proteorhodopsin, and the efficient identification of numerous 1 H- 1 H dipolar interactions, which provide distance constraints, inter-residue proximities, relative orientations of secondary structural elements, and protein-cofactor interactions in the hydrophobic transmembrane regions. These results establish a general approach for high-resolution structural studies of membrane proteins in lipid environments via solid-state NMR. |
