Arrel membrane proteins: composition and architecture of known structures. Protein Sci. 11, 30112 (2002). ten. Grosse, W. et al. Structure-based engineering of a minimal porin reveals loopindependent channel closure. Biochemistry 53, 4826838 (2014). 11. Barbet-Massin, E. et al. Out-and-back 13C-13C scalar transfers in protein resonance assignment by proton-detected solid-state NMR beneath ultra-fast MAS. J. Biomol. NMR 56, 37986 (2013). 12. Barbet-Massin, E. et al. Rapid proton-detected NMR assignment for proteins with quick magic angle spinning. J. Am. Chem. Soc. 136, 124892497 (2014). 13. Hong, M. Jakes, K. Selective and in depth 13C labeling of a membrane protein for solid-state NMR investigations. J. Biomol. NMR 14, 714 (1999). 14. Hansen, P. E. Isotope effects in nuclear shielding. Prog. Nucl. Mag. Res. Spectrosc. 20, 20755 (1988). 15. Higman, V. A. et al. Assigning big proteins inside the solid state: a MAS NMR resonance assignment method applying selectively and extensively 13C-labeled proteins. J. Biomol. NMR 44, 24560 (2009). 16. Hiller, M. et al. [2,3-(13)C]-labeling of aromatic residues–getting a head begin in the magic-angle-spinning NMR assignment of membrane proteins. J. Am. Chem. Soc. 130, 40809 (2008). 17. Hong, M. Determination of various –A11466 5 cathepsin Inhibitors Reagents torsion angles in proteins by selective and substantial (13)C labeling and two-dimensional solid-state NMR. J. Magn. Reson. 139, 38901 (1999). 18. LeMaster, D. M. Kushlan, D. M. Dynamical mapping of E-coli thioredoxin through C-13 NMR relaxation evaluation. J. Am. Chem. Soc. 118, 9255264 (1996). 19. Maltsev, A. S., Ying, J. F. Bax, A. Deuterium isotope shifts for backbone H-1, N-15 and C-13 nuclei in intrinsically disordered protein alpha-synuclein. J. Biomol. NMR 54, 18191 (2012). 20. Venters, R. A., Farmer, B. T., Fierke, C. A. Spicer, L. D. Characterizing the usage of perdeuteration in NMR research of massive proteins C-13, N-15 and H-1 assignments of human carbonic anhydrase II. J. Mol. Biol. 264, 1101116 (1996). 21. Bennett, A. E. et al. Homonuclear radio frequency-driven recoupling in rotating solids. J. Chem. Phys. 108, 9463479 (1998). 22. Cornilescu, G., Delaglio, F. Bax, A. Protein backbone angle restraints from looking a database for chemical shift and sequence homology. J. Biomol. NMR 13, 28902 (1999). 23. Shen, Y., Delaglio, F., Cornilescu, G. Bax, A. TALOS plus: a hybrid strategy for predicting protein backbone torsion angles from NMR chemical shifts. J. Biomol. NMR 44, 21323 (2009). 24. Bagos, P. G., Liakopoulos, T. D., Spyropoulos, I. C. Hamodrakas, S. J. PREDTMBB: a web server for predicting the topology of beta-barrel outer membrane proteins. 15(S)-15-Methyl Prostaglandin F2�� Epigenetic Reader Domain Nucleic Acids Res. 32, W400 404 (2004). 25. Linge, J. P., Habeck, M., Rieping, W. Nilges, M. ARIA: automated NOE assignment and NMR structure calculation. Bioinformatics 19, 31516 (2003). 26. Rieping, W. et al. ARIA2: automated NOE assignment and data integration in NMR structure calculation. Bioinformatics 23, 38182 (2007). 27. Grosse, W. et al. Structural and functional characterization of a synthetically modified OmpG. Bioorg. Med. Chem. 18, 7716723 (2010). 28. Korkmaz-Ozkan, F., Koster, S., Kuhlbrandt, W., Mantele, W. Yildiz, O. Correlation in between the OmpG secondary structure and its pH-dependent alterations monitored by FTIR. J. Mol. Biol. 401, 567 (2010). 29. Damaghi, M. et al. pH-dependent interactions guide the folding and gate the transmembrane pore on the beta-barrel membrane protein OmpG. J. Mol. Biol. 397, 87882 (20.

By mPEGS 1