Myristoylation as a general method for immobilization and alignment of soluble proteins for solid-state NMR structural studies

Journal of Biomolecular NMR

Volumn 25, Issue 1, 2003, Pages 55-61

  Mesleh, M F ^a   Valentine, K G ^c   Opella, S J ^a   Louis, J M ^b   Gronenborn, A M ^b  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

^c UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

Lipid bilayer; Myristoylation; Orientational restraints; PISEMA; Protein GB1; Solid state NMR

Indexed keywords

AMPHOPHILE; IMMUNOGLOBULIN BINDING FACTOR; LIPID; NITROGEN 15; PHOSPHATIDYLCHOLINE; PHOSPHOLIPID; PROTEIN; PROTEIN G; PROTON;

AMINO TERMINAL SEQUENCE; AQUEOUS SOLUTION; CONTROLLED STUDY; LIPID BILAYER; MAGNETIC FIELD; MYRISTYLATION; NUCLEAR MAGNETIC RESONANCE; ORIENTATION; PHOSPHOLIPID BILAYER; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN IMMOBILIZATION; PROTEIN INTERACTION; PROTEIN LOCALIZATION; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; REVIEW; SOLID STATE; SOLUBILITY; STREPTOCOCCUS GROUP G;

BACTERIAL PROTEINS; DIMYRISTOYLPHOSPHATIDYLCHOLINE; LIPID BILAYERS; MEMBRANE PROTEINS; MODELS, BIOLOGICAL; MUTAGENESIS, SITE-DIRECTED; MYRISTATES; NITROGEN ISOTOPES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN STRUCTURE, SECONDARY; SOLUBILITY;

STREPTOCOCCUS; STREPTOCOCCUS SP. 'GROUP G';

EID: 0037263087     PISSN: 09252738     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1021964314987     Document Type: Review

References (18)

1. Bielecki, A., Kolbert, A.C., deGroot, H.J.M., Griffin, R.G. and Levitt, M.H. (1990) Adv. Magn. Reson., 14, 111-124.
2. Clore, G.M. and Garrett, D.S. (1999) J. Am. Chem. Soc., 121, 9008-9012.
3. Duronio, R.J., Jackson-Machelski, E., Heuckeroth, R.O., Olins, P.O., Devine, C.S., Yonemoto, W., Slice, L.W., Taylor, S.S. and Gordon, J.I. (1990) Proc. Natl. Acad. Sci. USA, 87, 1506-1510.
4. Gronenborn, A.M., Filpula, D.R., Essig, N.Z., Achari, A., Whitlow, M., Wingfield, P.T. and Clore, G.M. (1991) Science, 253, 657-661.
5. Herzfeld, J., Griffin, R.G. and Haberkorn, R.A. (1978) Biochemistry, 17, 2711-2718.
6. Lee, M. and Goldburg, W.I. (1965) Phys. Rev., A140, 1261-1271.
7. Levitt, M.H., Suter, D. and Ernst, R.R. (1986) J. Chem. Phys., 84, 4243-4255.
8. Marassi, F.M. (2001) Biophys. J., 80, 994-1003.
9. Marassi, F.M. and Opella, S.J. (2000) J. Magn. Reson. 144, 150-155.
10. Marassi, F.M., Ramamoorthy, A. and Opella, S.J. (1997) Proc. Natl. Acad. Sci. USA, 94, 8551-8556.
11. Oas, T.G., Hartzell, C.J., Dahlquist, W. and Drobny, G.P. (1987) J. Am. Chem. Soc., 109, 5962-5966.
12. Opella, S.J., Ma, C. and Marassi, F.M. (2001) Meth. EnzymoL, 339, 285-313.
13. Opella S.J., Stewart, P.L. and Valentine, K.G. (1987) Quart. Rev. Biophys., 19, 7-49.
14. Petrache, H.I., Tristam-Nagle, S. and Nagle, J.F. (1998) Chem. Phys. Lipids, 95, 83-94.
15. Pines, A., Gibby, M.G. and Waugh, J.S. (1973) J. Chem. Phys., 59, 569-590.
16. Prosser, R.S., Hunt, S.A. and Vold, R.R. (1995) J. Magn. Reson., B109, 109-111.
17. Wu, C., Ramamoorthy, A., Gierasch, L.M. and Opella, S.J. (1995) J. Am. Chem. Soc., 117, 6148-6149.
18. Wu, C.H., Ramamoorthy, A. and Opella, S.J. (1994) J. Magn. Reson., 109, 270-272.