메뉴 건너뛰기




Volumn 55, Issue 9, 2003, Pages 515-523

Solid-state NMR Structure Determination

Author keywords

Membrane peptides; Protein structure; Solid state NMR

Indexed keywords

MEMBRANE PROTEIN; PEPTIDE;

EID: 0344443818     PISSN: 15216543     EISSN: None     Source Type: Journal    
DOI: 10.1080/15216540310001622740     Document Type: Review
Times cited : (53)

References (41)
  • 3
    • 4243854361 scopus 로고
    • Low frequency motion in membranes: The effect of cholesterol and proteins
    • Cornell, B. A., Davenport, J. B., and Separovic, F. (1982) Low frequency motion in membranes: the effect of cholesterol and proteins. Biochim. Biophys. Acta. 690, 15-19.
    • (1982) Biochim. Biophys. Acta , vol.690 , pp. 15-19
    • Cornell, B.A.1    Davenport, J.B.2    Separovic, F.3
  • 4
    • 0037379727 scopus 로고    scopus 로고
    • Effects of the eukaryotic pore-forming cytolysin equinatoxin II on lipid membranes and the role of sphingomyelin
    • Bonev, B., Lam, Y.-H., Anderluh, G., Watts, A., Norton, R. S., and Separovic, F. (2003) Effects of the eukaryotic pore-forming cytolysin equinatoxin II on lipid membranes and the role of sphingomyelin. Biophys. J. 84, 2382-2392.
    • (2003) Biophys. J. , vol.84 , pp. 2382-2392
    • Bonev, B.1    Lam, Y.-H.2    Anderluh, G.3    Watts, A.4    Norton, R.S.5    Separovic, F.6
  • 5
    • 0023815974 scopus 로고
    • Conformation and orientation of gramicidin A in oriented phospholipid bilyaers measured by solid state carbon-13 NMR
    • Cornell, B. A., Separovic, F., Smith, R., and Baldassi, A. J. (1988) Conformation and orientation of gramicidin A in oriented phospholipid bilyaers measured by solid state carbon-13 NMR. Biophys. J. 53, 67-76.
    • (1988) Biophys. J. , vol.53 , pp. 67-76
    • Cornell, B.A.1    Separovic, F.2    Smith, R.3    Baldassi, A.J.4
  • 8
    • 0036968507 scopus 로고    scopus 로고
    • Structure determination of membrane proteins by NMR spectroscopy
    • Opella, S. J., Nevzorov, A., Mesleh, M. F., and Marassi, F. (2002) Structure determination of membrane proteins by NMR spectroscopy. Biochem. Cell Biol. 80, 597-604.
    • (2002) Biochem. Cell Biol. , vol.80 , pp. 597-604
    • Opella, S.J.1    Nevzorov, A.2    Mesleh, M.F.3    Marassi, F.4
  • 9
    • 0028210494 scopus 로고
    • The structure of an integral membrane peptide: A deuterium NMR study of gramicidin
    • Prosser, R. S., Daleman, S. I., and Davis, J. H. (1994) The structure of an integral membrane peptide: a deuterium NMR study of gramicidin. Biophys. J. 66, 1415-1428.
    • (1994) Biophys. J. , vol.66 , pp. 1415-1428
    • Prosser, R.S.1    Daleman, S.I.2    Davis, J.H.3
  • 10
    • 0033170449 scopus 로고    scopus 로고
    • 13C labelling and two-dimensional solid-state NMR
    • 13C labelling and two-dimensional solid-state NMR. J. Magn. Reson. 139, 389-401.
    • (1999) J. Magn. Reson. , vol.139 , pp. 389-401
    • Hong, M.1
  • 13
    • 0032717887 scopus 로고    scopus 로고
    • The structure, dynamics and orientation of antimicrobial peptides in membranes by multidimensional solid-state NMR spectroscopy
    • Bechinger, B. (1999) The structure, dynamics and orientation of antimicrobial peptides in membranes by multidimensional solid-state NMR spectroscopy. Biochim. Biophys. Acta. 1462, 157-183.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 157-183
    • Bechinger, B.1
  • 14
    • 0021099797 scopus 로고
    • P-31 nuclear magnetic resonance studies of the association of basic proteins with multilayers of diacyl phosphatidylserine
    • Smith, R., Cornell, B. A., Keniry, M. A., and Separovic, F. (1983) P-31 nuclear magnetic resonance studies of the association of basic proteins with multilayers of diacyl phosphatidylserine. Biochim. Biophys. Acta. 732, 492-498.
    • (1983) Biochim. Biophys. Acta , vol.732 , pp. 492-498
    • Smith, R.1    Cornell, B.A.2    Keniry, M.A.3    Separovic, F.4
  • 16
    • 0029997915 scopus 로고    scopus 로고
    • The effect of unsaturation and ethanol on order parameter profiles of mixed chain phosphatidylcholines in dioleoylphosphatidylethanolamine bilayers
    • Separovic. F., and Gawrisch, K. (1996) The effect of unsaturation and ethanol on order parameter profiles of mixed chain phosphatidylcholines in dioleoylphosphatidylethanolamine bilayers. Biophys. J. 71, 274-282.
    • (1996) Biophys. J. , vol.71 , pp. 274-282
    • Separovic, F.1    Gawrisch, K.2
  • 17
    • 0013039776 scopus 로고    scopus 로고
    • NMR of peptides and proteins in oriented membranes
    • Marassi, F. M. (2002) NMR of peptides and proteins in oriented membranes. Conc. Magn. Reson. 14, 212-224.
    • (2002) Conc. Magn. Reson. , vol.14 , pp. 212-224
    • Marassi, F.M.1
  • 18
    • 0032579341 scopus 로고    scopus 로고
    • Photoreceptor rhodopsin: Structural and conformational study of its chromophore 11-cis retinal in oriented membranes by deuterium solid state NMR
    • Grobner, G., Choi, G., Burnett, I. J., Glaubitz, C., Verdegem, P. J. E., Lugetenburg, J., and Watts, A. (1998) Photoreceptor rhodopsin: structural and conformational study of its chromophore 11-cis retinal in oriented membranes by deuterium solid state NMR. FEBS Lett. 422, 201-204.
    • (1998) FEBS Lett. , vol.422 , pp. 201-204
    • Grobner, G.1    Choi, G.2    Burnett, I.J.3    Glaubitz, C.4    Verdegem, P.J.E.5    Lugetenburg, J.6    Watts, A.7
  • 19
    • 0032763732 scopus 로고    scopus 로고
    • Orientation of cecropin A helices in phospholipid bilayers determined by solid-state NMR spectroscopy
    • Marassi, F. M., Opella, S. J., Juvvadi, P., and Merrifield, R. B. (1999) Orientation of cecropin A helices in phospholipid bilayers determined by solid-state NMR spectroscopy. Biophys. J. 77, 3152-3155.
    • (1999) Biophys. J. , vol.77 , pp. 3152-3155
    • Marassi, F.M.1    Opella, S.J.2    Juvvadi, P.3    Merrifield, R.B.4
  • 20
    • 0038652081 scopus 로고    scopus 로고
    • Structure of the coat protein in fd filamentous bacteriophage particles determined by solid-state NMR spectroscopy
    • Zeri, A. C., Mesleh, M. F., Nevzaroz, A. A., and Opella, S. J. (2003) Structure of the coat protein in fd filamentous bacteriophage particles determined by solid-state NMR spectroscopy. Proc. Natl Acad. Sci. USA 100, 6458-6463.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6458-6463
    • Zeri, A.C.1    Mesleh, M.F.2    Nevzaroz, A.A.3    Opella, S.J.4
  • 21
    • 0032532475 scopus 로고    scopus 로고
    • Bicelles: A model membrane system for all season?
    • Sanders, C. R., and Prosser, R. S. (1998) Bicelles: a model membrane system for all season? Structure 6, 1227-1234.
    • (1998) Structure , vol.6 , pp. 1227-1234
    • Sanders, C.R.1    Prosser, R.S.2
  • 22
    • 84989629173 scopus 로고
    • Conformation-dependent carbon-13 chemical shifts: A new means of conformational characterization as obtained by high-resolution solid-state carbon-13 NMR
    • Saito, H. (1986) Conformation-dependent carbon-13 chemical shifts: a new means of conformational characterization as obtained by high-resolution solid-state carbon-13 NMR. Mag. Res. Chem. 24, 835-852.
    • (1986) Mag. Res. Chem. , vol.24 , pp. 835-852
    • Saito, H.1
  • 23
    • 0001390547 scopus 로고
    • Magic-angle-spinning carbon-13 NMR with atomic resolution of a photosynthetic reaction centre enriched in [4′-3C]tyrosine
    • De Groot, H. J. M., Raap, J., Winkel, C., Hoff, A. J., and Lugtenburg, A. (1990) Magic-angle-spinning carbon-13 NMR with atomic resolution of a photosynthetic reaction centre enriched in [4′-3C]tyrosine. Chem. Phys. Lett. 169, 307-310.
    • (1990) Chem. Phys. Lett. , vol.169 , pp. 307-310
    • De Groot, H.J.M.1    Raap, J.2    Winkel, C.3    Hoff, A.J.4    Lugtenburg, A.5
  • 24
    • 0028230816 scopus 로고
    • NMR observation of substrate in the binding site of an active sugar-H + symport protein in native membranes
    • Spooner, P. J. R., Rutherford, N. G., Watts, A., and Henderson, P. J. F. (1994) NMR observation of substrate in the binding site of an active sugar-H + symport protein in native membranes. Proc. Natl Acad. Sci. USA 91, 3877-3881.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3877-3881
    • Spooner, P.J.R.1    Rutherford, N.G.2    Watts, A.3    Henderson, P.J.F.4
  • 25
    • 0036816798 scopus 로고    scopus 로고
    • Solid-State NMR studies of the structure and mechanisms of proteins
    • Thompson, L. K. (2002) Solid-State NMR studies of the structure and mechanisms of proteins. Curr. Opinions Struct. Biol. 12, 661-669.
    • (2002) Curr. Opinions Struct. Biol. , vol.12 , pp. 661-669
    • Thompson, L.K.1
  • 26
    • 0031993272 scopus 로고    scopus 로고
    • Magic angle-oriented sample spinning (MAOSS): A new approach toward biomembrane studies
    • Glaubitz, C., and Watts, A. (1998) Magic angle-oriented sample spinning (MAOSS): A new approach toward biomembrane studies. J. Mag. Reson. 130, 305-316.
    • (1998) J. Mag. Reson. , vol.130 , pp. 305-316
    • Glaubitz, C.1    Watts, A.2
  • 27
    • 0037330672 scopus 로고    scopus 로고
    • Switched-angle spinning applied to bicelles containing phospholipid-associated peptides
    • Zandomeneghi, G., Williamson, P. T. F., Hunkeler, A., and Meier, B. A. (2003) Switched-angle spinning applied to bicelles containing phospholipid-associated peptides. J. Biomol. NMR 25, 125-132.
    • (2003) J. Biomol. NMR , vol.25 , pp. 125-132
    • Zandomeneghi, G.1    Williamson, P.T.F.2    Hunkeler, A.3    Meier, B.A.4
  • 28
    • 0034763782 scopus 로고    scopus 로고
    • Solid-state NMR structure determination of melittin in a lipid environment
    • Lato, Y.-H., Wassall, S. R., Morton, C. J., Smith, R., and Separovic, F. (2001) Solid-state NMR structure determination of melittin in a lipid environment. Biophys. J. 81, 2752-2761.
    • (2001) Biophys. J. , vol.81 , pp. 2752-2761
    • Lato, Y.-H.1    Wassall, S.R.2    Morton, C.J.3    Smith, R.4    Separovic, F.5
  • 29
    • 0036734994 scopus 로고    scopus 로고
    • Solid-state NMR conformational studies of a melittin-inhibitor complex
    • Lam, Y.-H., Morton, C. J., and Separovic, F. (2002) Solid-state NMR conformational studies of a melittin-inhibitor complex. Eur. Biophys. J. 31, 383-388.
    • (2002) Eur. Biophys. J. , vol.31 , pp. 383-388
    • Lam, Y.-H.1    Morton, C.J.2    Separovic, F.3
  • 30
    • 0025316922 scopus 로고
    • Rotational resonance determination of the structure of an enzyme-inhibitor complex: Phosphorylation of an (aminoalkyl)phosphinate inhibitor of D-alanyl D-alanine ligase by ATP
    • McDermott, A. E., Creuzet, F., and Griffin, R. G. (1990) Rotational resonance determination of the structure of an enzyme-inhibitor complex: Phosphorylation of an (aminoalkyl)phosphinate inhibitor of D-alanyl D-alanine ligase by ATP. Biochemistry 29, 5767-5775.
    • (1990) Biochemistry , vol.29 , pp. 5767-5775
    • McDermott, A.E.1    Creuzet, F.2    Griffin, R.G.3
  • 31
    • 0037129946 scopus 로고    scopus 로고
    • Relative orientation between the β-ionone ring and the polyene chain for the chromophore of rhodopsin in native membranes
    • Spooner, P. J. R., Sharples, J. M., Verhoeve, M. A., Lugtenburg, J., Glaubitz, C., and Watts, A. (2002) Relative orientation between the β-ionone ring and the polyene chain for the chromophore of rhodopsin in native membranes. Biochemistry 41, 7549-7555.
    • (2002) Biochemistry , vol.41 , pp. 7549-7555
    • Spooner, P.J.R.1    Sharples, J.M.2    Verhoeve, M.A.3    Lugtenburg, J.4    Glaubitz, C.5    Watts, A.6
  • 33
    • 0038412551 scopus 로고    scopus 로고
    • Backbone and side chain assignment strategies for multiply labeled membrane peptides and proteins in the solid state
    • Petkova, A. T., Baldus, M., Belenky, M., Hong, M., Griffin, R. G., and Herzfeld, J. (2003) Backbone and side chain assignment strategies for multiply labeled membrane peptides and proteins in the solid state. J. Mag. Reson. 160, 1-12.
    • (2003) J. Mag. Reson. , vol.160 , pp. 1-12
    • Petkova, A.T.1    Baldus, M.2    Belenky, M.3    Hong, M.4    Griffin, R.G.5    Herzfeld, J.6
  • 34
    • 0037465708 scopus 로고    scopus 로고
    • Insights into the amyloid folding problem from solid-state NMR
    • Tycko, R. (2003) Insights into the amyloid folding problem from solid-state NMR. Biochemistry 42, 3151-3159.
    • (2003) Biochemistry , vol.42 , pp. 3151-3159
    • Tycko, R.1
  • 35
    • 0037038365 scopus 로고    scopus 로고
    • Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy
    • Castellani, F., van Rossum, B., Diehl, A., Schubert, M., Rehbein, K., and Oschkinat, H. (2002) Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy. Nature 420, 98-102.
    • (2002) Nature , vol.420 , pp. 98-102
    • Castellani, F.1    Van Rossum, B.2    Diehl, A.3    Schubert, M.4    Rehbein, K.5    Oschkinat, H.6
  • 36
    • 0037125949 scopus 로고    scopus 로고
    • Expression and initial structural insights from solid-state NMR of the M2 proton channel from influenza A virus
    • Tian, C., Tobler, K., Lamb, R. A., Pinto, L. H., and Cross, T. A. (2002) Expression and initial structural insights from solid-state NMR of the M2 proton channel from influenza A virus. Biochemistry 41, 11294-11300.
    • (2002) Biochemistry , vol.41 , pp. 11294-11300
    • Tian, C.1    Tobler, K.2    Lamb, R.A.3    Pinto, L.H.4    Cross, T.A.5
  • 37
    • 33745590809 scopus 로고    scopus 로고
    • Lipid-peptide interaction investigated by NMR
    • (Simon, S. A., and McIntosh, T. J., ed.), Elsevier Science, San Diego, USA
    • Gawrisch, K., and Koenig, B. W. (2001). Lipid-peptide interaction investigated by NMR. In Current Topics in Membranes: Peptide-Lipid Interactions (Simon, S. A., and McIntosh, T. J., ed.). pp. 163-190, Elsevier Science, San Diego, USA.
    • (2001) Current Topics in Membranes: Peptide-Lipid Interactions , pp. 163-190
    • Gawrisch, K.1    Koenig, B.W.2
  • 39
    • 0036931451 scopus 로고    scopus 로고
    • 19F-NMR analysis of 19F-labeled trytophan in gramicidin A in oriented membranes
    • 19F-NMR analysis of 19F-labeled trytophan in gramicidin A in oriented membranes. Biophys. J. 83, 3336-3350.
    • (2002) Biophys. J. , vol.83 , pp. 3336-3350
    • Grage, S.L.1    Wang, J.2    Cross, T.A.3    Ulrich, A.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.