Imaging Membrane Protein Helical Wheels

Journal of Magnetic Resonance

Volumn 144, Issue 1, 2000, Pages 162-167

  Wang, J ^b   Denny, J ^b   Tian, C ^b   Kim, S ^b   Mo, Y ^b   Kovacs, F ^b   Song, Z ^a   Nishimura, K ^a   Gan, Z ^a   Fu, R ^a   Quine, J R ^a,b   Cross, T A ^a,b  

^a FLORIDA STATE UNIVERSITY   (United States)

^b FLORIDA STATE UNIVERSITY   (United States)

Author keywords

15 N solid state NMR; Membrane proteins; Orientational constraints; Oriented samples; PISEMA

Indexed keywords

MEMBRANE PROTEIN; NITROGEN;

ARTICLE; CHEMISTRY; INFLUENZA VIRUS A; LIPID BILAYER; METHODOLOGY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN SECONDARY STRUCTURE;

INFLUENZA A VIRUS; LIPID BILAYERS; MAGNETIC RESONANCE SPECTROSCOPY; MEMBRANE PROTEINS; NITROGEN ISOTOPES; PROTEIN STRUCTURE, SECONDARY;

EID: 0034184852     PISSN: 10907807     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmre.2000.2037     Document Type: Editorial

References (29)

1. 15 N correlation solid-state NMR, J. Am. Chem. Soc. 120, 7113-7114 (1998).
2. F. M. Marassi, J. J. Gesell, A. P. Valente, Y. Kim, M. Oblatt-Montal, M. Montal, and S. J. Opella, Dilute spin-exchange assignment of solid-state NMR spectra of oriented proteins: acetylcholine M2 in bilayers, J. Biomol. NMR 14, 141-148 (1999).
3. R. R. Ketchem, W. Hu, and T. A. Cross, High resolution conformation of gramicidin A in a lipid bilayer by solid-state NMR, Science 261, 1457-1460 (1993).
4. R. R. Ketchem, B. Roux, and T. A. Cross, High-resolution polypeptide structure in a lamellar phase lipid environment from solid-state NMR derived orientational constraints, Structure 5, 1655-1669 (1997).
5. S. J. Opella, F. M. Marassi, J. J. Gesell, A. P. Valente, Y. Kim, M. Oblatt-Montal, and M. Montal, Structures of the M2 channel-lining segments from nicotinic acetylcholine and NMDA receptors by NMR spectroscopy, Nat. Struct. Biol. 6, 374-379 (1999).
6. C. H. Wu, A. Ramamoorthy, and S. J. Opella, High-resolution heteronuclear dipolar solid-state NMR spectroscopy, J. Magn. Reson. A 109, 270-274 (1994).
7. F. M. Marassi and S. J. Opella, NMR structural studies of membrane proteins, Curr. Opin. Struct. Biol. 8, 640-648 (1998).
8. K.-J. Shon, Y. Kim, L. A. Colnago, and S. J. Opella, NMR studies of the structure and dynamics of membrane-bound bacteriophage Pf1 coat protein, Science 252, 1303-1305 (1991).
9. T. A. Cross and S. J. Opella, Solid state NMR structural studies of peptides and proteins in membranes, Curr. Opin. Struct. Biol. 4, 574-581 (1994).
10. F. M. Marassi and S. J. Opella, A solid-state NMR index of helical membrane proteins structure and topology, J. Magn. Reson. 144, 150-155 (2000).
11. A. J. Hay, The action of adamantamines against Influenza A virus: Inhibition of the M2 ion channel protein, Semin. Virol. 3, 21-30 (1992).
12. R. A. Lamb and R. M. Krug, Orthomyxoviridae: The viruses and their replication, in "Field's virology" (B. N. Fields, D. M. Knipe, and P. M. Howley, Eds.), p. 1353. Lippincot-Raven, Philadelphia (1996).
13. T. Sakaguchi, Q. Tu, L. H. Pinto, and R. A. Lamb, The active oligomeric state of the minimalistic Influenza virus M2 ion channel is a tetramer, Proc. Natl. Acad. Sci. USA 94, 5000-5005 (1997).
14. D. Salom, J. D. Lear, and W. F. DeGrado, Aggregation of Influenza A M2 transmembrane segment in micelles, Biophys. J. 76, A123 (1999).
15. K. C. Duff and R. H. Ashley, The transmembrane domain in Influenza A M2 protein forms amantadine-sensitive proton channels in planar lipid bilayers, Virology 190, 485-489 (1992).
16. K. C. Duff, S. M. Kelly, N. C. Price, and J. P. Bradshaw, The secondary structure of Influenza A M2 transmembrane domain. A circular dichroism study, FEBS Lett. 311, 256-258 (1992).
17. F. A. Kovacs and T. A. Cross, Transmembrane four-helix bundle of Influenza A M2 protein channel: Structural implications from helix tilt and orientation, Biophys. J. 73, 2511-2517 (1997).
18. F. Tian, Z. Song, and T. A. Cross, Orientational constraints derived from hydrated powder samples by two-dimensional PISEMA, J. Magn. Reson. 135, 227-231 (1998).
19. + channel, J. Mol. Biol. 286, 951-962 (1999).
20. 15 N]glycine hydrochloride monohydrate, J. Magn. Reson. 60, 79-82 (1984).
21. 15 N]alanine from the dipole-coupled powder patterns, J. Am. Chem. Soc. 109, 5966-5969 (1987).
22. 13 C dipole-coupled chemical shift powder patterns, J. Am. Chem. Soc. 109, 5962-5966 (1987).
23. 15 N chemical shift tensor orientation in a polypeptide, J. Magn. Reson. 85, 439-447 (1989).
24. W. Mai, W. Hu, C. Wang, and T. A. Cross, Three dimensional structural constraints in the form of orientational constraints from chemical shift anisotropy: The polypeptide backbone of gramicidin A in a lipid bilayer, Prot. Sci. 2, 532-542 (1993).
25. 15 N chemical shift anisotropy in solution, J. Am. Chem. Soc. 120, 10947-10952 (1998).
26. Y. Kim, K. Valente, S. J. Opella, S. L. Schendel, and W. A. Cramer, Solid-state NMR studies of the membrane-bound closed state of the colicin E1 channel domain in lipid bilayers, Prot. Sci. 7, 342-348 (1998).
27. 15 N-labeled membrane protein in phospholipid bilayers, Proc. Natl. Acad. Sci. USA 94, 8551-8556 (1997).
28. D. L. Farrens, C. Altenbach, K. Yang, W. L. Hubble, and H. G. Khorana, Requirement of rigid-body motion of transmembrane helices for light activation of Rhodopsin, Science 274, 768-770 (1996).
29. + -channel activating gating, Science 285, 73-78 (1999).