4.8 Article

Covalently circularized nanodiscs for studying membrane proteins and viral entry

Journal

NATURE METHODS
Volume 14, Issue 1, Pages 49-52

Publisher

NATURE PUBLISHING GROUP
DOI: 10.1038/NMETH.4079

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Funding

  1. NIH [32GM113406, AI20566, GM047467, GM075879, AI037581]
  2. Human Frontiers Science program
  3. HHMI
  4. TUM Institute for Advanced Study
  5. European Commission
  6. CIPSM excellence cluster
  7. DFG [SFB1035]
  8. NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [R01AI037581, R21AI020566, R01AI020566, R37AI020566] Funding Source: NIH RePORTER
  9. NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [F32GM113406, P01GM047467, R01GM075879] Funding Source: NIH RePORTER

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We engineered covalently circularized nanodiscs (cNDs) which, compared with standard nanodiscs, exhibit enhanced stability, defined diameter sizes and tunable shapes. Reconstitution into cNDs enhanced the quality of nuclear magnetic resonance spectra for both VDAC-1, a beta-barrel membrane protein, and the G-protein-coupled receptor NTR1, an alpha-helical membrane protein. In addition, we used cNDs to visualize how simple, nonenveloped viruses translocate their genomes across membranes to initiate infection.

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