A Solid-State NMR Index of Helical Membrane Protein Structure and Topology

Journal of Magnetic Resonance

Volumn 144, Issue 1, 2000, Pages 150-155

  Marassi, Francesca M ^a   Opella, Stanley J ^b  

^a WISTAR INSTITUTE   (United States)

^b UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

Helical wheels; PISA wheels; PISEMA; Solid state NMR; Structure determination

Indexed keywords

ANTIMICROBIAL CATIONIC PEPTIDE; MAGAININ 2 PEPTIDE, XENOPUS; MEMBRANE PROTEIN; NITROGEN; PEPTIDE; XENOPUS PROTEIN;

ANIMAL; ARTICLE; CHEMISTRY; LIPID BILAYER; METHODOLOGY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PHYSICAL CHEMISTRY; PROTEIN SECONDARY STRUCTURE;

ANIMALS; ANTIMICROBIAL CATIONIC PEPTIDES; CHEMISTRY, PHYSICAL; LIPID BILAYERS; MAGNETIC RESONANCE SPECTROSCOPY; MEMBRANE PROTEINS; NITROGEN ISOTOPES; PEPTIDES; PROTEIN STRUCTURE, SECONDARY; XENOPUS PROTEINS;

EID: 0034186215     PISSN: 10907807     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmre.2000.2035     Document Type: Editorial

References (29)

1. S. J. Opella, NMR and membrane proteins, Nat. Struct. Biol. NMR I Suppl. 4, 845-848 (1997).
2. R. Griffin, Dipolar recoupling in MAS spectra of biological solids, Nat. Struct. Biol. NMR II Suppl. 5, 508-512 (1998).
3. S. O. Smith, K. Ascheim, and M. Groesbeck, Magic angle spinning NMR spectroscopy of membrane proteins, Q. Rev. Biophys. 29, 395-449 (1996).
4. L. M. McDowell and J. Schaefer, High resolution NMR of biological solids, Curr. Opin. Struct. Biol. 6, 624-629 (1996).
5. C. Glaubitz and A. Watts, Magic angle-oriented sample spinning (MAOSS): A new approach toward biomembrane studies, J. Magn. Reson. 130, 305-316 (1998).
6. 19 F homonuclear dipolar couplings, obtained by multipulse solid-state NMR on static and oriented systems, J. Magn. Reson. 138, 98-106 (1999).
7. 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).
8. F. M. Marassi and S. J. Opella, NMR structural studies of membrane proteins, Curr. Opin. Struct. Biol. 8, 640-648 (1998).
9. 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).
10. S. J. Opella, F. M. Marassi, J. J. Gesell, A. P. Valente, Y. Kim, M. Oblatt-Montal, and M. Montal, Three-dimensional structure of the membrane-embedded M2 channel-lining segment from nicotinic acetylcholine receptors and NMDA receptors by NMR spectroscopy, Nat. Struct. Biol. 6, 374-379 (1999).
11. 15 N-labeled membrane protein in phospholipid bilayers, Proc. Natl. Acad. Sci. USA 94, 8551-8556 (1997).
12. F. M. Marassi, J. J. Gesell, A. P. Valente, 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).
13. W. M. Tan, Z. Gu, A. C. Zeri, and S. J. Opella, Solid-state NMR triple resonance backbone assignments in a protein, J. Biomol. NMR 13, 337-342 (1999).
14. C. H. Wu, A. Ramamoorthy, and S. J. Opella, High resolution heteronuclear dipolar solid-state NMR spectroscopy, J. Magn. Reson. A 109, 270-272 (1994).
15. M. Schiffer and A. B. Edmunson, Use of helical wheels to represent the structures of proteins and to identify segments with helical potential, Biophys. J. 7, 121-135 (1967).
16. D. S. Wishart, B. D. Sykes, and F. M. Richards, The chemical shift index: A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy, Biochemistry 31, 1647-1651 (1992).
17. β chemical shifts on protein structure determination by NMR, J. Magn. Reson. B 106, 92-96 (1995).
18. J. Wang, J. Denny, C. Tian, S. Kim, Y. Mo, F. Kovacs, Z. Song, K. Nishimura, Z. Gan, R. Fu, J. R. Quine, and T. A. Cross, Imaging membrane protein helical wheels, J. Magn. Reson. 144, 162-167 (2000).
19. 15 N chemical shift interaction tensors in a peptide bond by three-dimensional solid-state NMR spectroscopy, J. Am. Chem. Soc. 117, 6148-6149 (1995).
20. J. U. Bowie, Helix packing in membrane proteins, J. Mol. Biol. 272, 780-789 (1997).
21. F. M. Marassi, C. Ma, H. Gratkowski, S. K. Straus, K. Strebel, M. Oblatt-Montal, M. Montai, and S. J. Opella, Correlation of the structural and functional domains in the membrane protein Vpu from HIV-1, Proc. Natl. Acad. Sci. USA 96, 14336-14341 (1999).
22. Y. Kim, K. Valentine, 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, Protein Sci. 7, 342-348 (1998).
23. W. Mai, W. Hu, C. Wang, and T. A. Cross, Orientational constraints as 3-dimensional structural constraints from chemical-shift anisotropy - The polypeptide backbone of gramicidin-A in a lipid bilayer, Protein Sci. 2, 532-542 (1993).
24. 15 N chemical shift anisotropy from NMR relaxation data. Ubiquitin as a test example, J. Amer. Chem. Soc. 120, 7109-7110 (1998).
25. A. Ramamoorthy, C. H. Wu, and S. J. Opella, Three-dimensional solid-state NMR experiment that correlates the chemical shift and dipolar coupling frequencies of two heteronuclei, J. Magn. Reson. B 107, 88-90 (1995).
26. 15 N-labeled helical membrane proteins in oriented lipid bilayers, J. Magn. Reson. 144, 156-161 (2000).
27. 1 H amide chemical shift tensor in structure determination of proteins by solid-state NMR spectroscopy, Appl. Magn. Reson. 17, 433-447 (1999).
28. 1 H NMR experiments show that the 23-residue magainin antibiotic peptide is an alpha helix in dodecylphosphocholine micelles, sodium dodecylsulfate micelles, and trifluoroethanol/water solution, J. Biomol. NMR 9, 127-135 (1997).
29. A. Ramamoorthy, F. M. Marassi, M. Zasloff, and S. J. Opella, Three-dimensional solid-state NMR spectroscopy of a peptide oriented in membrane bilayers, J. Biomol. NMR 6, 329-334 (1995).