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Volumn 1768, Issue 12, 2007, Pages 3235-3259

The cytochromes P450 and b5 and their reductases-Promising targets for structural studies by advanced solid-state NMR spectroscopy

Author keywords

Cytochrome b5; Cytochrome P450; Membrane protein; Solid state NMR

Indexed keywords

CYTOCHROME B5; CYTOCHROME P450; CYTOCHROME REDUCTASE; MEMBRANE PROTEIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE FERRIHEMOPROTEIN REDUCTASE;

EID: 36849051197     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2007.08.007     Document Type: Review
Times cited : (105)

References (246)
  • 2
    • 0031954925 scopus 로고    scopus 로고
    • Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms
    • Wallin E., and von Heijne G. Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms. Protein Sci. 7 (1998) 1029-1038
    • (1998) Protein Sci. , vol.7 , pp. 1029-1038
    • Wallin, E.1    von Heijne, G.2
  • 4
    • 3042621274 scopus 로고    scopus 로고
    • The progress of membrane protein structure determination
    • White S.H. The progress of membrane protein structure determination. Protein Sci. 13 (2004) 1948-1949
    • (2004) Protein Sci. , vol.13 , pp. 1948-1949
    • White, S.H.1
  • 6
    • 0024587230 scopus 로고
    • Protein structure determination in solution by nuclear magnetic resonance spectroscopy
    • Wüthrich K. Protein structure determination in solution by nuclear magnetic resonance spectroscopy. Science 243 (1989) 45-50
    • (1989) Science , vol.243 , pp. 45-50
    • Wüthrich, K.1
  • 7
    • 85056029714 scopus 로고    scopus 로고
    • Ramamoorthy, A. NMR spectroscopy of biological solids. CRC Press, Taylor & Francis Group, New York (2006).
  • 8
    • 33645849830 scopus 로고    scopus 로고
    • How far can the sensitivity of NMR be increased?
    • Fujiwara T., and Ramamoorthy A. How far can the sensitivity of NMR be increased?. Annu. Rep. NMR Spectrosc. 58 (2006) 155-175
    • (2006) Annu. Rep. NMR Spectrosc. , vol.58 , pp. 155-175
    • Fujiwara, T.1    Ramamoorthy, A.2
  • 9
    • 0022998708 scopus 로고
    • Characterization of rat and human liver mitochondrial cytochrome P450 forms involved in nifedipine oxidation, a prototype for genetic polymorphism in oxidative drug metabolism
    • Guengerich F.P., Martin M.V., Beaune P.H., Kremers P., Wolff T., and Waxman D.J. Characterization of rat and human liver mitochondrial cytochrome P450 forms involved in nifedipine oxidation, a prototype for genetic polymorphism in oxidative drug metabolism. J. Biol. Chem. 261 (1986) 5051-5060
    • (1986) J. Biol. Chem. , vol.261 , pp. 5051-5060
    • Guengerich, F.P.1    Martin, M.V.2    Beaune, P.H.3    Kremers, P.4    Wolff, T.5    Waxman, D.J.6
  • 11
    • 36848999174 scopus 로고    scopus 로고
    • 5 catalyzes product formation by cytochrome P450 2B4 faster than cytochrome P450 reductase and competes with reductase for a binding site on cytochrome P450 2B4, J. Biol. Chem. (in press).
  • 14
    • 0028970539 scopus 로고
    • 5, its functions, structure, and membrane topology
    • 5, its functions, structure, and membrane topology. Biochimie 77 (1995) 604-620
    • (1995) Biochimie , vol.77 , pp. 604-620
    • Vergères, G.1    Waskell, L.2
  • 15
    • 0842312531 scopus 로고    scopus 로고
    • Comparison of cytochrome P450 (CYP) genes from the mouse and human genomes, including nomenclature recommendations for genes, pseudogenes and alternative-splice variants
    • Nelson D.R., Zeldin D.C., Hoffman S.M.G., Maltais L.J., Wain H.M., and Nebert D.W. Comparison of cytochrome P450 (CYP) genes from the mouse and human genomes, including nomenclature recommendations for genes, pseudogenes and alternative-splice variants. Pharmacogenetics 14 (2004) 1-14
    • (2004) Pharmacogenetics , vol.14 , pp. 1-14
    • Nelson, D.R.1    Zeldin, D.C.2    Hoffman, S.M.G.3    Maltais, L.J.4    Wain, H.M.5    Nebert, D.W.6
  • 16
    • 0036304873 scopus 로고    scopus 로고
    • Human CYP7A1 deficiency: progress and enigmas
    • Beigneux A., Hofmann A.F., and Young S.G. Human CYP7A1 deficiency: progress and enigmas. J. Clin. Invest. 110 (2002) 29-31
    • (2002) J. Clin. Invest. , vol.110 , pp. 29-31
    • Beigneux, A.1    Hofmann, A.F.2    Young, S.G.3
  • 18
    • 84892246340 scopus 로고    scopus 로고
    • Human cytochrome P450 enzymes
    • Ortiz de Montellano P.R. (Ed), Kluwer Press, New York
    • Guengerich F.P. Human cytochrome P450 enzymes. In: Ortiz de Montellano P.R. (Ed). Cytochrome P450: Structure, Mechanism, and Biochemistry (2005), Kluwer Press, New York 377-531
    • (2005) Cytochrome P450: Structure, Mechanism, and Biochemistry , pp. 377-531
    • Guengerich, F.P.1
  • 19
    • 33846483860 scopus 로고    scopus 로고
    • Complex reactions catalyzed by cytochrome P450 enzymes
    • Isin E.M., and Guengerich F.P. Complex reactions catalyzed by cytochrome P450 enzymes. Biochim. Biophys. Acta 1770 (2007) 314-329
    • (2007) Biochim. Biophys. Acta , vol.1770 , pp. 314-329
    • Isin, E.M.1    Guengerich, F.P.2
  • 20
    • 27544466682 scopus 로고    scopus 로고
    • Use of directed evolution of mammalian cytochromes P450 for investigating the molecular basis of enzyme function and generating novel biocatalysts
    • Kumar S., and Halpert J.R. Use of directed evolution of mammalian cytochromes P450 for investigating the molecular basis of enzyme function and generating novel biocatalysts. Biochem. Biophys. Res. Commun. 338 (2005) 456-464
    • (2005) Biochem. Biophys. Res. Commun. , vol.338 , pp. 456-464
    • Kumar, S.1    Halpert, J.R.2
  • 21
    • 0032924934 scopus 로고    scopus 로고
    • Cytochrome P-450 3A4: regulation and role in drug metabolism
    • Guengerich F.P. Cytochrome P-450 3A4: regulation and role in drug metabolism. Annu. Rev. Pharmacol. Toxicol. 39 (1999) 1-17
    • (1999) Annu. Rev. Pharmacol. Toxicol. , vol.39 , pp. 1-17
    • Guengerich, F.P.1
  • 22
    • 34250346536 scopus 로고    scopus 로고
    • Multiple sequential steps involved in the binding of inhibitors to cytochrome P450 3A4
    • Isin E.M., and Guengerich F.P. Multiple sequential steps involved in the binding of inhibitors to cytochrome P450 3A4. J. Biol. Chem. 282 (2007) 6863-6874
    • (2007) J. Biol. Chem. , vol.282 , pp. 6863-6874
    • Isin, E.M.1    Guengerich, F.P.2
  • 23
    • 0033569516 scopus 로고    scopus 로고
    • Pharmacogenomics: translating functional genomics into rational therapeutics
    • Evans W.E., and Relling M.V. Pharmacogenomics: translating functional genomics into rational therapeutics. Science 286 (1999) 487-491
    • (1999) Science , vol.286 , pp. 487-491
    • Evans, W.E.1    Relling, M.V.2
  • 24
    • 0036548404 scopus 로고    scopus 로고
    • Cytochromes P450 and experimental models of drug metabolism
    • Zuber R., Anzenbacherova E., and Anzenbacher P. Cytochromes P450 and experimental models of drug metabolism. J. Cell. Mol. Med. 6 (2002) 189-198
    • (2002) J. Cell. Mol. Med. , vol.6 , pp. 189-198
    • Zuber, R.1    Anzenbacherova, E.2    Anzenbacher, P.3
  • 27
    • 0141988883 scopus 로고    scopus 로고
    • Determination of the rate of reduction of oxyferrous cytochrome P450 2B4 by 5-deazariboflavin adenine dinucleotide T491V cytochrome P450 reductase
    • Zhang H., Gruenke L., Arscott D., Shen A., Kasper C., Harris D.L., Glavanovich M., Johnson R., and Waskell L. Determination of the rate of reduction of oxyferrous cytochrome P450 2B4 by 5-deazariboflavin adenine dinucleotide T491V cytochrome P450 reductase. Biochemistry 42 (2003) 11594-11603
    • (2003) Biochemistry , vol.42 , pp. 11594-11603
    • Zhang, H.1    Gruenke, L.2    Arscott, D.3    Shen, A.4    Kasper, C.5    Harris, D.L.6    Glavanovich, M.7    Johnson, R.8    Waskell, L.9
  • 29
    • 33845252049 scopus 로고    scopus 로고
    • Specific effects of potassium ion binding on wild-type and L358P cytochrome P450cam
    • OuYang B., Sondej Pochapsky S., Pagani G.M., and Pochapsky T.C. Specific effects of potassium ion binding on wild-type and L358P cytochrome P450cam. Biochemistry 45 (2006) 14379-14388
    • (2006) Biochemistry , vol.45 , pp. 14379-14388
    • OuYang, B.1    Sondej Pochapsky, S.2    Pagani, G.M.3    Pochapsky, T.C.4
  • 30
  • 31
    • 0029643786 scopus 로고
    • Structure and function of cytochromes P450: a comparative analysis of three crystal structures
    • Hasemann C.A., Kurumbail R.G., Boddupalli S.S., Peterson J.A., and Deisenhofer J. Structure and function of cytochromes P450: a comparative analysis of three crystal structures. Structure 2 (1995) 41-62
    • (1995) Structure , vol.2 , pp. 41-62
    • Hasemann, C.A.1    Kurumbail, R.G.2    Boddupalli, S.S.3    Peterson, J.A.4    Deisenhofer, J.5
  • 32
    • 0033970047 scopus 로고    scopus 로고
    • Mammalian microsomal cytochrome P450 monooxygenase: structural adaptations for membrane binding and functional diversity
    • Williams P.A., Cosme J., Sridhar V., Johnson E.F., and McRee D.E. Mammalian microsomal cytochrome P450 monooxygenase: structural adaptations for membrane binding and functional diversity. Mol. Cell 5 (2000) 121-131
    • (2000) Mol. Cell , vol.5 , pp. 121-131
    • Williams, P.A.1    Cosme, J.2    Sridhar, V.3    Johnson, E.F.4    McRee, D.E.5
  • 33
    • 0034723195 scopus 로고    scopus 로고
    • Engineering microsomal cytochrome P450 2C5 to be a soluble, monomeric enzyme
    • Cosme J., and Johnson E.F. Engineering microsomal cytochrome P450 2C5 to be a soluble, monomeric enzyme. J. Biol. Chem. 275 (2000) 2545-2553
    • (2000) J. Biol. Chem. , vol.275 , pp. 2545-2553
    • Cosme, J.1    Johnson, E.F.2
  • 34
    • 27544516024 scopus 로고    scopus 로고
    • Structural diversity of human xenobiotic-metabolizing cytochrome P450 monooxygenases
    • Johnson E.F., and Stout C.D. Structural diversity of human xenobiotic-metabolizing cytochrome P450 monooxygenases. Biochem. Biophys. Res. Commun. 338 (2005) 331-336
    • (2005) Biochem. Biophys. Res. Commun. , vol.338 , pp. 331-336
    • Johnson, E.F.1    Stout, C.D.2
  • 36
    • 0034738973 scopus 로고    scopus 로고
    • Microsomal cytochrome P450 2C5: comparison to microbial P450s and unique features
    • Williams P.A., Cosme J., Sridhar V., Johnson E.F., and McRee D.E. Microsomal cytochrome P450 2C5: comparison to microbial P450s and unique features. J. Inorg. Biochem. 81 (2000) 183-190
    • (2000) J. Inorg. Biochem. , vol.81 , pp. 183-190
    • Williams, P.A.1    Cosme, J.2    Sridhar, V.3    Johnson, E.F.4    McRee, D.E.5
  • 37
    • 3042553224 scopus 로고    scopus 로고
    • Structure of mammalian cytochrome P450 2B4 complexed with 4-(4-chlorophenyl)imidazole at 1.9-Å resolution
    • Scott E.E., White M.A., He Y.A., Johnson E.F., and Stout C.D. Structure of mammalian cytochrome P450 2B4 complexed with 4-(4-chlorophenyl)imidazole at 1.9-Å resolution. J. Biol. Chem. 279 (2004) 27294-27301
    • (2004) J. Biol. Chem. , vol.279 , pp. 27294-27301
    • Scott, E.E.1    White, M.A.2    He, Y.A.3    Johnson, E.F.4    Stout, C.D.5
  • 40
    • 33646854265 scopus 로고    scopus 로고
    • Structure of microsomal cytochrome P450 2B4 complexed with the antifungal drug bifonazole
    • Zhao Y., White M.A., Muralidhara B.K., Sun L., Halpert J.R., and Stout C.D. Structure of microsomal cytochrome P450 2B4 complexed with the antifungal drug bifonazole. J. Biol. Chem. 281 (2006) 5973-5981
    • (2006) J. Biol. Chem. , vol.281 , pp. 5973-5981
    • Zhao, Y.1    White, M.A.2    Muralidhara, B.K.3    Sun, L.4    Halpert, J.R.5    Stout, C.D.6
  • 41
    • 33744490360 scopus 로고    scopus 로고
    • Positioning of proteins in membranes: a computational approach
    • Lomize A.L., Pogozheva I.D., Lomize M.A., and Mosberg H.I. Positioning of proteins in membranes: a computational approach. Protein Sci. 15 (2006) 1318-1333
    • (2006) Protein Sci. , vol.15 , pp. 1318-1333
    • Lomize, A.L.1    Pogozheva, I.D.2    Lomize, M.A.3    Mosberg, H.I.4
  • 42
    • 33645673185 scopus 로고    scopus 로고
    • Identification of membrane-contacting loops of the catalytic domain of cytochrome P450 2C2 by tryptophan fluorescence scanning
    • Ozalp C., Szczesna-Skorupa E., and Kemper B. Identification of membrane-contacting loops of the catalytic domain of cytochrome P450 2C2 by tryptophan fluorescence scanning. Biochemistry 45 (2006) 4629-4637
    • (2006) Biochemistry , vol.45 , pp. 4629-4637
    • Ozalp, C.1    Szczesna-Skorupa, E.2    Kemper, B.3
  • 44
    • 33847386720 scopus 로고    scopus 로고
    • Simulation study of methemoglobin reduction in erythrocytes
    • Kinoshita A., Nakayama Y., Kitayama T., and Tomita M. Simulation study of methemoglobin reduction in erythrocytes. FEBS J. 274 (2007) 1449-1458
    • (2007) FEBS J. , vol.274 , pp. 1449-1458
    • Kinoshita, A.1    Nakayama, Y.2    Kitayama, T.3    Tomita, M.4
  • 49
    • 0018801347 scopus 로고
    • 5 reduction by NADPH-cytochrome P-450 reductase
    • 5 reduction by NADPH-cytochrome P-450 reductase. J. Biol. Chem. 254 (1979) 8976-8981
    • (1979) J. Biol. Chem. , vol.254 , pp. 8976-8981
    • Enoch, H.G.1    Strittmatter, P.2
  • 75
    • 0034800477 scopus 로고    scopus 로고
    • Allosteric phenomena in cytochrome P450-catalyzed monooxygenations
    • Hlavica P., and Lewis D.F.V. Allosteric phenomena in cytochrome P450-catalyzed monooxygenations. Eur. J. Biochem. 268 (2001) 4817-4832
    • (2001) Eur. J. Biochem. , vol.268 , pp. 4817-4832
    • Hlavica, P.1    Lewis, D.F.V.2
  • 77
    • 73649173283 scopus 로고
    • Microsomal triphosphopyridine nucleotide-cytochrome c reductase of liver
    • Williams Jr. C.H., and Kamin H. Microsomal triphosphopyridine nucleotide-cytochrome c reductase of liver. J. Biol. Chem. 237 (1962) 587-595
    • (1962) J. Biol. Chem. , vol.237 , pp. 587-595
    • Williams Jr., C.H.1    Kamin, H.2
  • 78
    • 73849173955 scopus 로고
    • Hepatic triphosphopyridine nucleotide-cytochrome c reductase: isolation, characterization, and kinetic studies
    • Phillips A.H., and Langdon R.G. Hepatic triphosphopyridine nucleotide-cytochrome c reductase: isolation, characterization, and kinetic studies. J. Biol. Chem. 237 (1962) 2652-2660
    • (1962) J. Biol. Chem. , vol.237 , pp. 2652-2660
    • Phillips, A.H.1    Langdon, R.G.2
  • 79
    • 23744510839 scopus 로고    scopus 로고
    • 5 by NADPH-cytochrome P450 reductase
    • 5 by NADPH-cytochrome P450 reductase. Arch. Biochem. Biophys. 440 (2005) 204-211
    • (2005) Arch. Biochem. Biophys. , vol.440 , pp. 204-211
    • Guengerich, F.P.1
  • 80
    • 0015217018 scopus 로고
    • Biochemical distinctions between the nuclear and microsomal membranes from rat hepatocytes
    • Kasper C.B. Biochemical distinctions between the nuclear and microsomal membranes from rat hepatocytes. J. Biol. Chem. 246 (1971) 577-581
    • (1971) J. Biol. Chem. , vol.246 , pp. 577-581
    • Kasper, C.B.1
  • 83
    • 0015919107 scopus 로고
    • 5 reductase containing both the catalytic site and an additional hydrophobic membrane-binding segment
    • 5 reductase containing both the catalytic site and an additional hydrophobic membrane-binding segment. J. Biol. Chem. 248 (1973) 793-799
    • (1973) J. Biol. Chem. , vol.248 , pp. 793-799
    • Spatz, L.1    Strittmatter, P.2
  • 85
    • 0033794450 scopus 로고    scopus 로고
    • New developments in isotope labeling strategies for protein solution NMR spectroscopy
    • Goto N.K., and Kay L.E. New developments in isotope labeling strategies for protein solution NMR spectroscopy. Curr. Opin. Struct. Biol. 10 (2000) 585-592
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 585-592
    • Goto, N.K.1    Kay, L.E.2
  • 86
    • 0024836418 scopus 로고
    • Expression and nitrogen-15 labeling of proteins for proton and nitrogen-15 nuclear magnetic resonance
    • Muchmore D.C., McIntosh L.P., Russell C.B., Anderson D.E., and Dahlquist F.W. Expression and nitrogen-15 labeling of proteins for proton and nitrogen-15 nuclear magnetic resonance. Methods Enzymol. 177 (1989) 44-73
    • (1989) Methods Enzymol. , vol.177 , pp. 44-73
    • Muchmore, D.C.1    McIntosh, L.P.2    Russell, C.B.3    Anderson, D.E.4    Dahlquist, F.W.5
  • 88
    • 0024284781 scopus 로고
    • NMR sequential assignment of Escherichia coli thioredoxin utilizing random fractional deuteration
    • LeMaster D.M., and Richards F.M. NMR sequential assignment of Escherichia coli thioredoxin utilizing random fractional deuteration. Biochemistry 27 (1988) 142-150
    • (1988) Biochemistry , vol.27 , pp. 142-150
    • LeMaster, D.M.1    Richards, F.M.2
  • 89
    • 0033121307 scopus 로고    scopus 로고
    • 13C labeling of a membrane protein for solid-state NMR investigations
    • 13C labeling of a membrane protein for solid-state NMR investigations. J. Biomol. NMR 14 (1999) 71-74
    • (1999) J. Biomol. NMR , vol.14 , pp. 71-74
    • Hong, M.1    Jakes, K.2
  • 90
    • 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. Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy. Nature 420 (2002) 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
  • 92
    • 0035714660 scopus 로고    scopus 로고
    • Overexpression and purification of the membrane-bound cytochrome P450 2B4
    • Saribas A.S., Gruenke L., and Waskell L. Overexpression and purification of the membrane-bound cytochrome P450 2B4. Prot. Expr. Purif. 21 (2001) 303-309
    • (2001) Prot. Expr. Purif. , vol.21 , pp. 303-309
    • Saribas, A.S.1    Gruenke, L.2    Waskell, L.3
  • 98
    • 0034216460 scopus 로고    scopus 로고
    • Fluorine as an NMR probe for structural studies of chemical and biological systems
    • Gakh Y.G., Gakh A.A., and Gronenborn A.M. Fluorine as an NMR probe for structural studies of chemical and biological systems. Magn. Reson. Chem. 38 (2000) 551-558
    • (2000) Magn. Reson. Chem. , vol.38 , pp. 551-558
    • Gakh, Y.G.1    Gakh, A.A.2    Gronenborn, A.M.3
  • 100
    • 4344704702 scopus 로고    scopus 로고
    • Structure determination of membrane proteins by NMR spectroscopy
    • Opella S.J., and Marassi F.M. Structure determination of membrane proteins by NMR spectroscopy. Chem. Rev. 104 (2004) 3587-3606
    • (2004) Chem. Rev. , vol.104 , pp. 3587-3606
    • Opella, S.J.1    Marassi, F.M.2
  • 101
    • 0025101067 scopus 로고
    • Optimizing and characterizing alignment of oriented lipid bilayers containing gramicidin D
    • Moll III F., and Cross T.A. Optimizing and characterizing alignment of oriented lipid bilayers containing gramicidin D. Biophys. J. 57 (1990) 351-362
    • (1990) Biophys. J. , vol.57 , pp. 351-362
    • Moll III, F.1    Cross, T.A.2
  • 102
    • 0000689027 scopus 로고
    • Saturated solutions for the control of humidity in biological research
    • Winston P.W., and Bates D.H. Saturated solutions for the control of humidity in biological research. Ecology 41 (1960) 232-237
    • (1960) Ecology , vol.41 , pp. 232-237
    • Winston, P.W.1    Bates, D.H.2
  • 103
    • 0027438626 scopus 로고
    • fd Coat protein structure in membrane environments
    • McDonnel P.A., Shon K., Kim Y., and Opella S.J. fd Coat protein structure in membrane environments. J. Mol. Biol. 233 (1993) 447-463
    • (1993) J. Mol. Biol. , vol.233 , pp. 447-463
    • McDonnel, P.A.1    Shon, K.2    Kim, Y.3    Opella, S.J.4
  • 104
    • 0027360175 scopus 로고
    • High-resolution conformation of gramicidin A in lipid bilayer by solid-state NMR
    • Ketchem R.R., Hu W., and Cross T.A. High-resolution conformation of gramicidin A in lipid bilayer by solid-state NMR. Science 261 (1993) 1457-1460
    • (1993) Science , vol.261 , pp. 1457-1460
    • Ketchem, R.R.1    Hu, W.2    Cross, T.A.3
  • 105
    • 0026447195 scopus 로고
    • Structure determination of the cyclohexene ring of retinal in bacteriorhodopsin by solid-state deuterium NMR
    • Ulrich A.S., Heyn M.P., and Watts A. Structure determination of the cyclohexene ring of retinal in bacteriorhodopsin by solid-state deuterium NMR. Biochemistry 31 (1992) 10390-10399
    • (1992) Biochemistry , vol.31 , pp. 10390-10399
    • Ulrich, A.S.1    Heyn, M.P.2    Watts, A.3
  • 106
    • 0035997051 scopus 로고    scopus 로고
    • Membrane composition determines pardaxin's mechanism of lipid bilayer disruption
    • Hallock K.J., Lee D.-K., Omnaas J., Mosberg H.I., and Ramamoorthy A. Membrane composition determines pardaxin's mechanism of lipid bilayer disruption. Biophys. J. 83 (2002) 1004-1013
    • (2002) Biophys. J. , vol.83 , pp. 1004-1013
    • Hallock, K.J.1    Lee, D.-K.2    Omnaas, J.3    Mosberg, H.I.4    Ramamoorthy, A.5
  • 107
    • 0037961563 scopus 로고    scopus 로고
    • MSI-78, an analogue of the magainin antimicrobial peptides, disrupts lipid bilayer structure via positive curvature strain
    • Hallock K.J., Lee D.-K., and Ramamoorthy A. MSI-78, an analogue of the magainin antimicrobial peptides, disrupts lipid bilayer structure via positive curvature strain. Biophys. J. 84 (2003) 3052-3060
    • (2003) Biophys. J. , vol.84 , pp. 3052-3060
    • Hallock, K.J.1    Lee, D.-K.2    Ramamoorthy, A.3
  • 108
    • 0038052326 scopus 로고    scopus 로고
    • Mechanism of lipid bilayer disruption by the human antimicrobial peptide, LL-37
    • Henzler Wildman K.A., Lee D.-K., and Ramamoorthy A. Mechanism of lipid bilayer disruption by the human antimicrobial peptide, LL-37. Biochemistry 42 (2003) 6558
    • (2003) Biochemistry , vol.42 , pp. 6558
    • Henzler Wildman, K.A.1    Lee, D.-K.2    Ramamoorthy, A.3
  • 109
    • 3142543171 scopus 로고    scopus 로고
    • Perturbation of the hydrophobic core of lipid bilayers by the human antimicrobial peptide LL-37
    • Henzler Wildman K.A., Martinez G.V., Brown M.F., and Ramamoorthy A. Perturbation of the hydrophobic core of lipid bilayers by the human antimicrobial peptide LL-37. Biochemistry 43 (2004) 8459-8469
    • (2004) Biochemistry , vol.43 , pp. 8459-8469
    • Henzler Wildman, K.A.1    Martinez, G.V.2    Brown, M.F.3    Ramamoorthy, A.4
  • 110
    • 33846562986 scopus 로고    scopus 로고
    • Topology and tilt of cell-signaling peptides containing nuclear localization sequences in membrane bilayers determined by solid-state NMR and molecular dynamics simulation studies
    • Ramamoorthy A., Kandasamy S.K., Lee D.-K., Kidambi S., and Larson R.G. Topology and tilt of cell-signaling peptides containing nuclear localization sequences in membrane bilayers determined by solid-state NMR and molecular dynamics simulation studies. Biochemistry 46 (2007) 965-975
    • (2007) Biochemistry , vol.46 , pp. 965-975
    • Ramamoorthy, A.1    Kandasamy, S.K.2    Lee, D.-K.3    Kidambi, S.4    Larson, R.G.5
  • 111
    • 7644228920 scopus 로고    scopus 로고
    • Investigation of the interaction of myelin basic protein with phospholipid bilayers using solid-state NMR spectroscopy
    • Pointer-Keenan C.D., Lee D.-K., Hallock K.J., Tan A., Zand R., and Ramamoorthy A. Investigation of the interaction of myelin basic protein with phospholipid bilayers using solid-state NMR spectroscopy. Chem. Phys. Lipids 132 (2004) 47-54
    • (2004) Chem. Phys. Lipids , vol.132 , pp. 47-54
    • Pointer-Keenan, C.D.1    Lee, D.-K.2    Hallock, K.J.3    Tan, A.4    Zand, R.5    Ramamoorthy, A.6
  • 112
    • 1542375007 scopus 로고    scopus 로고
    • Solid state NMR spectroscopy of aligned lipid bilayers at low temperatures
    • Lee D.-K., Henzler Wildman K.A., and Ramamoorthy A. Solid state NMR spectroscopy of aligned lipid bilayers at low temperatures. J. Am. Chem. Soc. 126 (2004) 2318-2319
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 2318-2319
    • Lee, D.-K.1    Henzler Wildman, K.A.2    Ramamoorthy, A.3
  • 113
    • 0036228299 scopus 로고    scopus 로고
    • An innovative procedure using a sublimable solid to align lipid bilayers for solid-state NMR studies
    • Hallock K.J., Henzler Wildman K.A., Lee D.-K., and Ramamoorthy A. An innovative procedure using a sublimable solid to align lipid bilayers for solid-state NMR studies. Biophys. J. 82 (2002) 2499-2503
    • (2002) Biophys. J. , vol.82 , pp. 2499-2503
    • Hallock, K.J.1    Henzler Wildman, K.A.2    Lee, D.-K.3    Ramamoorthy, A.4
  • 114
    • 0028730634 scopus 로고
    • Magnetically-oriented phospholipid micelles as a tool for the study of membrane-associated molecules
    • Sanders C.R., Hare B.J., Howard K.P., and Prestegard J.H. Magnetically-oriented phospholipid micelles as a tool for the study of membrane-associated molecules. Prog. Nucl. Magn. Reson. Spectrosc. 26 (1994) 421-444
    • (1994) Prog. Nucl. Magn. Reson. Spectrosc. , vol.26 , pp. 421-444
    • Sanders, C.R.1    Hare, B.J.2    Howard, K.P.3    Prestegard, J.H.4
  • 115
    • 0028947465 scopus 로고
    • Reconstitution of membrane proteins into lipid-rich bilayered mixed micelles for NMR studies
    • Sanders C.R., and Landis G.C. Reconstitution of membrane proteins into lipid-rich bilayered mixed micelles for NMR studies. Biochemistry 34 (1995) 4030-4040
    • (1995) Biochemistry , vol.34 , pp. 4030-4040
    • Sanders, C.R.1    Landis, G.C.2
  • 116
    • 33746045690 scopus 로고    scopus 로고
    • Current applications of bicelles in NMR studies of membrane-associated amphiphiles and proteins
    • Prosser R.S., Evanics F., Kitevski J.L., and Al-Abdul-Wahid M.S. Current applications of bicelles in NMR studies of membrane-associated amphiphiles and proteins. Biochemistry 45 (2006) 8453-8465
    • (2006) Biochemistry , vol.45 , pp. 8453-8465
    • Prosser, R.S.1    Evanics, F.2    Kitevski, J.L.3    Al-Abdul-Wahid, M.S.4
  • 118
    • 0031969085 scopus 로고    scopus 로고
    • Magnetically aligned phospholipids with positive ordering: a new model membrane system
    • Prosser R.S., Hwang J.S., and Vold R.R. Magnetically aligned phospholipids with positive ordering: a new model membrane system. Biophys. J. 74 (1998) 2405-2418
    • (1998) Biophys. J. , vol.74 , pp. 2405-2418
    • Prosser, R.S.1    Hwang, J.S.2    Vold, R.R.3
  • 119
    • 0031722552 scopus 로고    scopus 로고
    • Novel chelate-induced magnetic alignment of biological membranes
    • Prosser R.S., Volkov V.B., and Shiyanovskaya I.V. Novel chelate-induced magnetic alignment of biological membranes. Biophys. J. 75 (1998) 2163-2189
    • (1998) Biophys. J. , vol.75 , pp. 2163-2189
    • Prosser, R.S.1    Volkov, V.B.2    Shiyanovskaya, I.V.3
  • 120
    • 0032919273 scopus 로고    scopus 로고
    • Improved low pH bicelle system for orienting macromolecules over a wide temperature range
    • Cavagnero S., Dyson H.J., and Wright P.E. Improved low pH bicelle system for orienting macromolecules over a wide temperature range. J. Biomol. NMR 13 (1999) 387-391
    • (1999) J. Biomol. NMR , vol.13 , pp. 387-391
    • Cavagnero, S.1    Dyson, H.J.2    Wright, P.E.3
  • 121
    • 0033627891 scopus 로고    scopus 로고
    • Pegylation of magnetically oriented lipid bilayers
    • King V., Parker M., and Howard K.P. Pegylation of magnetically oriented lipid bilayers. J. Magn. Reson. 142 (2000) 177-182
    • (2000) J. Magn. Reson. , vol.142 , pp. 177-182
    • King, V.1    Parker, M.2    Howard, K.P.3
  • 122
    • 17444365826 scopus 로고    scopus 로고
    • Bicelles as model membranes for solid- and solution-state NMR studies of membrane peptides and proteins
    • Marcotte I., and Auger M. Bicelles as model membranes for solid- and solution-state NMR studies of membrane peptides and proteins. Magn. Reson. Part A 24A (2005) 17-37
    • (2005) Magn. Reson. Part A , vol.24 A , pp. 17-37
    • Marcotte, I.1    Auger, M.2
  • 123
    • 21244486782 scopus 로고    scopus 로고
    • Reinvestigation by phosphorus NMR of lipid distribution in bicelles
    • Triba M.N., Warschawski D.E., and Devaux P.F. Reinvestigation by phosphorus NMR of lipid distribution in bicelles. Biophys. J. 88 (2005) 1887-1901
    • (2005) Biophys. J. , vol.88 , pp. 1887-1901
    • Triba, M.N.1    Warschawski, D.E.2    Devaux, P.F.3
  • 124
    • 0035353437 scopus 로고    scopus 로고
    • Temperature dependence of DMPC/DHPC mixing in a bicellar solution and its structural implications
    • Sternin E., Nizza D., and Gawrisch K. Temperature dependence of DMPC/DHPC mixing in a bicellar solution and its structural implications. Langmuir 17 (2001) 2610-2616
    • (2001) Langmuir , vol.17 , pp. 2610-2616
    • Sternin, E.1    Nizza, D.2    Gawrisch, K.3
  • 125
    • 33746812736 scopus 로고    scopus 로고
    • Effects of lipid chain length and unsaturation on bicelles stability. A phosphorus NMR study
    • Triba M.N., Devaux P.F., and Warschawski D.E. Effects of lipid chain length and unsaturation on bicelles stability. A phosphorus NMR study. Biophys. J. 91 (2006) 1357-1367
    • (2006) Biophys. J. , vol.91 , pp. 1357-1367
    • Triba, M.N.1    Devaux, P.F.2    Warschawski, D.E.3
  • 126
    • 0036434495 scopus 로고    scopus 로고
    • Methods for studying transmembrane peptides in bicelles: consequences of hydrophobic mismatch and peptide sequence
    • Whiles J.A., Glover K.J., Vold R.R., and Komives E.A. Methods for studying transmembrane peptides in bicelles: consequences of hydrophobic mismatch and peptide sequence. J. Magn. Reson. 158 (2002) 149-156
    • (2002) J. Magn. Reson. , vol.158 , pp. 149-156
    • Whiles, J.A.1    Glover, K.J.2    Vold, R.R.3    Komives, E.A.4
  • 127
    • 0036841870 scopus 로고    scopus 로고
    • Cation modulation of bicelle size and magnetic alignment as revealed by solid-state NMR and electron microscopy
    • Arnold A., Labrot T., Oda R., and Dufourc E.J. Cation modulation of bicelle size and magnetic alignment as revealed by solid-state NMR and electron microscopy. Biophys. J. 83 (2006) 2667-2680
    • (2006) Biophys. J. , vol.83 , pp. 2667-2680
    • Arnold, A.1    Labrot, T.2    Oda, R.3    Dufourc, E.J.4
  • 128
    • 34250303513 scopus 로고    scopus 로고
    • Biphenyl bicelle disks align perpendicular to magnetic fields on large temperature scales. A study combining synthesis, solid state NMR, TEM and SAXS
    • Loudet C., Manet S., Gineste S., Oda R., Achard M.-F., and Dufourc E.J. Biphenyl bicelle disks align perpendicular to magnetic fields on large temperature scales. A study combining synthesis, solid state NMR, TEM and SAXS. Biophys. J. 92 (2007) 3949-3959
    • (2007) Biophys. J. , vol.92 , pp. 3949-3959
    • Loudet, C.1    Manet, S.2    Gineste, S.3    Oda, R.4    Achard, M.-F.5    Dufourc, E.J.6
  • 129
    • 34250217114 scopus 로고    scopus 로고
    • Characterization of lipid bilayer formation in aligned nanoporous aluminium oxide nanotube arrays
    • Karp E.S., Newstadt J.P., Chu S., and Lorigan G.A. Characterization of lipid bilayer formation in aligned nanoporous aluminium oxide nanotube arrays. J. Magn. Reson. 187 (2007) 112-119
    • (2007) J. Magn. Reson. , vol.187 , pp. 112-119
    • Karp, E.S.1    Newstadt, J.P.2    Chu, S.3    Lorigan, G.A.4
  • 130
    • 33845929561 scopus 로고    scopus 로고
    • Functional reconstitution of rhodopsin into tubular lipid bilayers supported by nanoporous material
    • Soubias O., Polozov I.V., Teague W.E., Yeliseev A.A., and Gawrisch K. Functional reconstitution of rhodopsin into tubular lipid bilayers supported by nanoporous material. Biochemistry 45 (2006) 15583-15590
    • (2006) Biochemistry , vol.45 , pp. 15583-15590
    • Soubias, O.1    Polozov, I.V.2    Teague, W.E.3    Yeliseev, A.A.4    Gawrisch, K.5
  • 131
    • 34548494605 scopus 로고    scopus 로고
    • Membrane fragmentation by an amyloidogenic fragment of human islet amyloid polypeptide detected by solid-state NMR spectroscopy of membrane nanotubes
    • Brender J.R., Dürr U.H.N., Heyl D., Budarapu M.B., and Ramamoorthy A. Membrane fragmentation by an amyloidogenic fragment of human islet amyloid polypeptide detected by solid-state NMR spectroscopy of membrane nanotubes. Biochim. Biophys. Acta 1768 (2007) 2026-2029
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 2026-2029
    • Brender, J.R.1    Dürr, U.H.N.2    Heyl, D.3    Budarapu, M.B.4    Ramamoorthy, A.5
  • 132
    • 34247847729 scopus 로고    scopus 로고
    • 15N solid-state NMR investigation of the dynamics and orientation of a transmembrane helical bundle
    • 15N solid-state NMR investigation of the dynamics and orientation of a transmembrane helical bundle. J. Am. Chem. Soc. 129 (2007) 5719-5729
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 5719-5729
    • Cady, S.D.1    Goodman, C.2    Tatko, C.D.3    DeGrado, W.F.4    Hong, M.5
  • 133
    • 33750935291 scopus 로고    scopus 로고
    • Orientation determination of membrane-disruptive proteins using powder samples and rotational diffusion: a simple solid-state NMR approach
    • Hong M., and Doherty T. Orientation determination of membrane-disruptive proteins using powder samples and rotational diffusion: a simple solid-state NMR approach. Chem. Phys. Lett. 432 (2006) 296-300
    • (2006) Chem. Phys. Lett. , vol.432 , pp. 296-300
    • Hong, M.1    Doherty, T.2
  • 135
    • 84906393014 scopus 로고    scopus 로고
    • Uniaxial motional averaging of the chemical shift anisotropy of membrane proteins in bilayer environments
    • Ramamoorthy A. (Ed), CRC Press, New York
    • Nevzorov A.A., De Angelis A.A., Park S.H., and Opella S.J. Uniaxial motional averaging of the chemical shift anisotropy of membrane proteins in bilayer environments. In: Ramamoorthy A. (Ed). NMR Spectroscopy of Biological Solids (2006), CRC Press, New York 177-190
    • (2006) NMR Spectroscopy of Biological Solids , pp. 177-190
    • Nevzorov, A.A.1    De Angelis, A.A.2    Park, S.H.3    Opella, S.J.4
  • 137
    • 0034832980 scopus 로고    scopus 로고
    • 13C NMR chemical shift anisotropy tensors of polypeptides
    • 13C NMR chemical shift anisotropy tensors of polypeptides. J. Am. Chem. Soc. 123 (2001) 6118-6126
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 6118-6126
    • Wei, Y.1    Lee, D.-K.2    Ramamoorthy, A.3
  • 138
    • 0035819626 scopus 로고    scopus 로고
    • Orientation of amide-nitrogen-15 chemical shift tensors in peptides: a quantum chemical study
    • Brender J.R., Taylor D.M., and Ramamoorthy A. Orientation of amide-nitrogen-15 chemical shift tensors in peptides: a quantum chemical study. J. Am. Chem. Soc. 123 (2001) 914-922
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 914-922
    • Brender, J.R.1    Taylor, D.M.2    Ramamoorthy, A.3
  • 140
    • 0032113597 scopus 로고    scopus 로고
    • A simple one-dimensional solid-state NMR method to characterize the nuclear spin interaction tensors associated with the peptide bond
    • Lee D.-K., and Ramamoorthy A. A simple one-dimensional solid-state NMR method to characterize the nuclear spin interaction tensors associated with the peptide bond. J. Magn. Reson. 133 (1998) 204-206
    • (1998) J. Magn. Reson. , vol.133 , pp. 204-206
    • Lee, D.-K.1    Ramamoorthy, A.2
  • 141
    • 0001404008 scopus 로고    scopus 로고
    • Application of one-dimensional dipolar shift solid-state NMR spectroscopy to study the backbone conformation of membrane-associated peptides in phospholipid bilayers
    • Lee D.-K., Santos J.S., and Ramamoorthy A. Application of one-dimensional dipolar shift solid-state NMR spectroscopy to study the backbone conformation of membrane-associated peptides in phospholipid bilayers. J. Phys. Chem. B 103 (1999) 8383-8390
    • (1999) J. Phys. Chem. B , vol.103 , pp. 8383-8390
    • Lee, D.-K.1    Santos, J.S.2    Ramamoorthy, A.3
  • 142
    • 0000780723 scopus 로고    scopus 로고
    • 15N dipolar coupling tensors associated with the phenylalanine residue in the solid state
    • 15N dipolar coupling tensors associated with the phenylalanine residue in the solid state. Chem. Phys. Lett. 309 (1999)
    • (1999) Chem. Phys. Lett. , vol.309
    • Lee, D.-K.1    Santos, J.S.2    Ramamoorthy, A.3
  • 143
    • 33846595904 scopus 로고    scopus 로고
    • High-resolution heteronuclear dipolar solid-state NMR spectroscopy
    • Wu C.H., Ramamoorthy A., and Opella S.J. High-resolution heteronuclear dipolar solid-state NMR spectroscopy. J. Magn. Reson. Ser. A 109 (2003) 207-272
    • (2003) J. Magn. Reson. Ser. A , vol.109 , pp. 207-272
    • Wu, C.H.1    Ramamoorthy, A.2    Opella, S.J.3
  • 144
    • 36849028996 scopus 로고    scopus 로고
    • A familiy of PISEMA experiments for structural studies of biological solids
    • Webb G.A. (Ed), Springer
    • Ramamoorthy A., and Yamamoto K. A familiy of PISEMA experiments for structural studies of biological solids. In: Webb G.A. (Ed). Modern Magnetic Resonance (2006), Springer 699-705
    • (2006) Modern Magnetic Resonance , pp. 699-705
    • Ramamoorthy, A.1    Yamamoto, K.2
  • 147
    • 0034186215 scopus 로고    scopus 로고
    • A solid-state NMR index of helical membrane protein structure and topology
    • Marassi F.M., and Opella S.J. A solid-state NMR index of helical membrane protein structure and topology. J. Magn. Reson. 144 (2000) 150-155
    • (2000) J. Magn. Reson. , vol.144 , pp. 150-155
    • Marassi, F.M.1    Opella, S.J.2
  • 148
    • 0037372352 scopus 로고    scopus 로고
    • Simultaneous assignment and structure determination of a membrane protein from NMR orientational restraints
    • Marassi F.M., and Opella S.J. Simultaneous assignment and structure determination of a membrane protein from NMR orientational restraints. Protein Sci. 12 (2003) 403-411
    • (2003) Protein Sci. , vol.12 , pp. 403-411
    • Marassi, F.M.1    Opella, S.J.2
  • 149
    • 33750959054 scopus 로고    scopus 로고
    • Assigning solid-state NMR spectra of aligned proteins using isotropic chemical shifts
    • De Angelis A.A., Howell S.C., and Opella S.J. Assigning solid-state NMR spectra of aligned proteins using isotropic chemical shifts. J. Magn. Reson. 183 (2006) 329-332
    • (2006) J. Magn. Reson. , vol.183 , pp. 329-332
    • De Angelis, A.A.1    Howell, S.C.2    Opella, S.J.3
  • 150
    • 0034146354 scopus 로고    scopus 로고
    • Spin dynamics of polarization inversion spin exchange at the magic angle in multiple spin systems
    • Gan Z. Spin dynamics of polarization inversion spin exchange at the magic angle in multiple spin systems. J. Magn. Reson. 143 (2000) 136-143
    • (2000) J. Magn. Reson. , vol.143 , pp. 136-143
    • Gan, Z.1
  • 151
    • 0042468159 scopus 로고    scopus 로고
    • A "magic sandwich" pulse sequence with reduced offset dependende for high-resolution separated local field spectroscopy
    • Nevzorov A.A., and Opella S.J. A "magic sandwich" pulse sequence with reduced offset dependende for high-resolution separated local field spectroscopy. J. Magn. Reson. 164 (2003) 182-186
    • (2003) J. Magn. Reson. , vol.164 , pp. 182-186
    • Nevzorov, A.A.1    Opella, S.J.2
  • 152
    • 33947586763 scopus 로고    scopus 로고
    • Selective averaging for high-resolution solid-state NMR spectroscopy of aligned samples
    • Nevzorov A.A., and Opella S.J. Selective averaging for high-resolution solid-state NMR spectroscopy of aligned samples. J. Magn. Reson. 185 (2006) 59-70
    • (2006) J. Magn. Reson. , vol.185 , pp. 59-70
    • Nevzorov, A.A.1    Opella, S.J.2
  • 153
    • 31544481382 scopus 로고    scopus 로고
    • Separated local field NMR spectroscopy by windowless isotropic mixing
    • Dvinskikh S.V., Yamamoto K., and Ramamoorthy A. Separated local field NMR spectroscopy by windowless isotropic mixing. Chem. Phys. Lett. 419 (2006) 168-173
    • (2006) Chem. Phys. Lett. , vol.419 , pp. 168-173
    • Dvinskikh, S.V.1    Yamamoto, K.2    Ramamoorthy, A.3
  • 154
    • 32344436173 scopus 로고    scopus 로고
    • Measurement of heteronuclear dipolar couplings using a rotating frame solid-state NMR experiment
    • Yamamoto K., Dvinskikh S.V., and Ramamoorthy A. Measurement of heteronuclear dipolar couplings using a rotating frame solid-state NMR experiment. Chem. Phys. Lett. 419 (2006) 533-536
    • (2006) Chem. Phys. Lett. , vol.419 , pp. 533-536
    • Yamamoto, K.1    Dvinskikh, S.V.2    Ramamoorthy, A.3
  • 155
    • 33746317772 scopus 로고    scopus 로고
    • Heteronuclear isotropic mixing separated local field NMR spectroscopy
    • Dvinskikh S.V., Yamamoto K., and Ramamoorthy A. Heteronuclear isotropic mixing separated local field NMR spectroscopy. J. Chem. Phys. 125 (2006) 034507
    • (2006) J. Chem. Phys. , vol.125 , pp. 034507
    • Dvinskikh, S.V.1    Yamamoto, K.2    Ramamoorthy, A.3
  • 156
    • 19944387677 scopus 로고    scopus 로고
    • Frequency offset refocused PISEMA-type sequences
    • Dvinskikh S.V., and Sandström D. Frequency offset refocused PISEMA-type sequences. J. Magn. Reson. 175 (2005) 163-169
    • (2005) J. Magn. Reson. , vol.175 , pp. 163-169
    • Dvinskikh, S.V.1    Sandström, D.2
  • 158
    • 0042944212 scopus 로고    scopus 로고
    • Heteronuclear dipolar recoupling in liquid crystals and solids by PISEMA-type pulse sequences
    • Dvinskikh S.V., Zimmermann H., Maliniak A., and Sandström D. Heteronuclear dipolar recoupling in liquid crystals and solids by PISEMA-type pulse sequences. J. Magn. Reson. 164 (2003) 165-170
    • (2003) J. Magn. Reson. , vol.164 , pp. 165-170
    • Dvinskikh, S.V.1    Zimmermann, H.2    Maliniak, A.3    Sandström, D.4
  • 159
    • 18844438694 scopus 로고    scopus 로고
    • PITANSEMA-MAS, a solid-state NMR method to measure heteronuclear dipolar couplings under MAS
    • Yamamoto K., Ermakov V.L., Lee D.-K., and Ramamoorthy A. PITANSEMA-MAS, a solid-state NMR method to measure heteronuclear dipolar couplings under MAS. Chem. Phys. Lett. 408 (2005) 118-122
    • (2005) Chem. Phys. Lett. , vol.408 , pp. 118-122
    • Yamamoto, K.1    Ermakov, V.L.2    Lee, D.-K.3    Ramamoorthy, A.4
  • 160
    • 0036213784 scopus 로고    scopus 로고
    • 15N]-labeled membrane proteins in oriented lipid bilayers
    • 15N]-labeled membrane proteins in oriented lipid bilayers. J. Biomol. NMR 22 (2007) 225-247
    • (2007) J. Biomol. NMR , vol.22 , pp. 225-247
    • Vosegaard, T.1    Nielsen, N.C.2
  • 161
    • 0034003022 scopus 로고    scopus 로고
    • 13C-labeled peptide crystal: toward spectral resolution, assignment, and structure determination of oriented molecules in solid-state NMR
    • 13C-labeled peptide crystal: toward spectral resolution, assignment, and structure determination of oriented molecules in solid-state NMR. J. Am. Chem. Soc. 122 (2000) 1443-1455
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 1443-1455
    • Ishii, Y.1    Tycko, R.2
  • 162
    • 0000883563 scopus 로고    scopus 로고
    • Solid-state NMR triple-resonance backbone assignments in a protein
    • Tan W.M., Gu Z., Zeri A.C., and Opella S.J. Solid-state NMR triple-resonance backbone assignments in a protein. J. Biomol. NMR 13 (1999) 337-342
    • (1999) J. Biomol. NMR , vol.13 , pp. 337-342
    • Tan, W.M.1    Gu, Z.2    Zeri, A.C.3    Opella, S.J.4
  • 163
    • 0033208602 scopus 로고    scopus 로고
    • 13C PISEMA experiments and their application to backbone and side chain sites of amino acids and peptides
    • 13C PISEMA experiments and their application to backbone and side chain sites of amino acids and peptides. J. Magn. Reson. 140 (1999) 340-346
    • (1999) J. Magn. Reson. , vol.140 , pp. 340-346
    • Gu, Z.1    Opella, S.J.2
  • 164
    • 0033144286 scopus 로고    scopus 로고
    • 15N shift solid-state NMR correlation spectroscopy
    • 15N shift solid-state NMR correlation spectroscopy. J. Magn. Reson. 138 (1999) 193-198
    • (1999) J. Magn. Reson. , vol.138 , pp. 193-198
    • Gu, Z.1    Opella, S.J.2
  • 165
    • 33846466434 scopus 로고    scopus 로고
    • Three-dimensional experiment for solid-state NMR of aligned protein samples in high field magnets
    • Nevzorov A.A., Park S.H., and Opella S.J. Three-dimensional experiment for solid-state NMR of aligned protein samples in high field magnets. J. Biomol. NMR 37 (2007) 113-116
    • (2007) J. Biomol. NMR , vol.37 , pp. 113-116
    • Nevzorov, A.A.1    Park, S.H.2    Opella, S.J.3
  • 166
    • 33749511249 scopus 로고    scopus 로고
    • Three-dimensional structure of the trans-membrane domain of Vpu from HIV-1 in aligned phospholipid bicelles
    • Park S.H., De Angelis A.A., Nevzorov A.A., Wu C.H., and Opella S.J. Three-dimensional structure of the trans-membrane domain of Vpu from HIV-1 in aligned phospholipid bicelles. Biophys. J. 91 (2006) 3032-3042
    • (2006) Biophys. J. , vol.91 , pp. 3032-3042
    • Park, S.H.1    De Angelis, A.A.2    Nevzorov, A.A.3    Wu, C.H.4    Opella, S.J.5
  • 167
    • 33748775215 scopus 로고    scopus 로고
    • Structure determination of a membrane protein with two trans-membrane helices in aligned phospholipid bicelles by solid-state NMR spectroscopy
    • De Angelis A.A., Howell S.C., Nevzorov A.A., and Opella S.J. Structure determination of a membrane protein with two trans-membrane helices in aligned phospholipid bicelles by solid-state NMR spectroscopy. J. Am. Chem. Soc. 128 (2006) 12256-12267
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 12256-12267
    • De Angelis, A.A.1    Howell, S.C.2    Nevzorov, A.A.3    Opella, S.J.4
  • 168
    • 0142210121 scopus 로고    scopus 로고
    • Initial structural and dynamic characterization of the M2 protein transmembrane and amphipathic helices in lipid bilayers
    • Tian C., Fei Gao P., Pinto L.H., Lamb R.A., and Cross T.A. Initial structural and dynamic characterization of the M2 protein transmembrane and amphipathic helices in lipid bilayers. Protein Sci. 12 (2003) 2597-2605
    • (2003) Protein Sci. , vol.12 , pp. 2597-2605
    • Tian, C.1    Fei Gao, P.2    Pinto, L.H.3    Lamb, R.A.4    Cross, T.A.5
  • 169
    • 34250334756 scopus 로고    scopus 로고
    • Backbone structure of the amantadin-blocked trans-membrane domain M2 proton channel from influenza A virus
    • Hu J., Asbury T., Achuthan S., Li C., Bertram R., Quine J.R., Fu R., and Cross T.A. Backbone structure of the amantadin-blocked trans-membrane domain M2 proton channel from influenza A virus. Biophys. J. 92 (2007) 4335-4343
    • (2007) Biophys. J. , vol.92 , pp. 4335-4343
    • Hu, J.1    Asbury, T.2    Achuthan, S.3    Li, C.4    Bertram, R.5    Quine, J.R.6    Fu, R.7    Cross, T.A.8
  • 172
    • 36849095399 scopus 로고    scopus 로고
    • Nuclear magnetic resonance structural studies of the FXYD familiy membrane proteins in lipid bilayers
    • Ramamoorthy A. (Ed), CRC Press, New York
    • Franzin C.M., Yu J., and Marassi F.M. Nuclear magnetic resonance structural studies of the FXYD familiy membrane proteins in lipid bilayers. In: Ramamoorthy A. (Ed). NMR Spectroscopy of Biological Solids (2006), CRC Press, New York 191-236
    • (2006) NMR Spectroscopy of Biological Solids , pp. 191-236
    • Franzin, C.M.1    Yu, J.2    Marassi, F.M.3
  • 173
    • 33947171594 scopus 로고    scopus 로고
    • NMR of membrane proteins in micelles and bilayers: the FXYD family of proteins
    • Franzin C.M., Gong X.-M., Thai K., Yu J., and Marassi F.M. NMR of membrane proteins in micelles and bilayers: the FXYD family of proteins. Methods 41 (2007) 398-408
    • (2007) Methods , vol.41 , pp. 398-408
    • Franzin, C.M.1    Gong, X.-M.2    Thai, K.3    Yu, J.4    Marassi, F.M.5
  • 174
    • 32344432998 scopus 로고    scopus 로고
    • Reconstitution and alignment by a magnetic field of a β-barrel membrane protein in bicelles
    • Triba M.N., Zoonens M., Popot J.-L., Devaux P.F., and Warschawski D.E. Reconstitution and alignment by a magnetic field of a β-barrel membrane protein in bicelles. Eur. Biophys. J. 35 (2005) 268-275
    • (2005) Eur. Biophys. J. , vol.35 , pp. 268-275
    • Triba, M.N.1    Zoonens, M.2    Popot, J.-L.3    Devaux, P.F.4    Warschawski, D.E.5
  • 175
    • 33947388784 scopus 로고    scopus 로고
    • Probing the molecular dynamics of the ABC multidrug transporter LmrA by deuterium solid-state nuclear magnetic resonance
    • Siarheyeva A., Lopez J.J., Lehner I., Hellmich U.A., van Veen H.W., and Glaubitz C. Probing the molecular dynamics of the ABC multidrug transporter LmrA by deuterium solid-state nuclear magnetic resonance. Biochemistry 46 (2007) 3075-3083
    • (2007) Biochemistry , vol.46 , pp. 3075-3083
    • Siarheyeva, A.1    Lopez, J.J.2    Lehner, I.3    Hellmich, U.A.4    van Veen, H.W.5    Glaubitz, C.6
  • 177
    • 49149141788 scopus 로고
    • Net polarization transfer via a J-ordered state for signal enhancement of low-sensitivity nuclei
    • Burum D.P., and Ernst R.R. Net polarization transfer via a J-ordered state for signal enhancement of low-sensitivity nuclei. J. Magn. Reson. 39 (1980) 163-168
    • (1980) J. Magn. Reson. , vol.39 , pp. 163-168
    • Burum, D.P.1    Ernst, R.R.2
  • 178
    • 0344603844 scopus 로고    scopus 로고
    • The hydrogen exchange core and protein folding
    • Li R., and Woodward C. The hydrogen exchange core and protein folding. Protein Sci. 8 (1999) 1571-1591
    • (1999) Protein Sci. , vol.8 , pp. 1571-1591
    • Li, R.1    Woodward, C.2
  • 179
    • 0036298953 scopus 로고    scopus 로고
    • Specification and visualization of anisotropic interaction tensors in polypeptides and numerical simulations in biological solid-state NMR
    • Bak M., Schultz R., Vosegaard T., and Nielsen N.C. Specification and visualization of anisotropic interaction tensors in polypeptides and numerical simulations in biological solid-state NMR. J. Magn. Reson. 154 (2002) 28-45
    • (2002) J. Magn. Reson. , vol.154 , pp. 28-45
    • Bak, M.1    Schultz, R.2    Vosegaard, T.3    Nielsen, N.C.4
  • 180
    • 0031214521 scopus 로고    scopus 로고
    • Thermodynamic model of secondary structure for alpha-helical peptides and proteins
    • Lomize A.L., and Mosberg H.I. Thermodynamic model of secondary structure for alpha-helical peptides and proteins. Biopolymers 42 (1997) 239-269
    • (1997) Biopolymers , vol.42 , pp. 239-269
    • Lomize, A.L.1    Mosberg, H.I.2
  • 181
    • 68149121932 scopus 로고    scopus 로고
    • Solid-state nuclear magnetic resonance spectroscopic studies of magnetically aligned phospholipid bilayers
    • Ramamoorthy A. (Ed), CRC Press, New York
    • Lorigan G.A. Solid-state nuclear magnetic resonance spectroscopic studies of magnetically aligned phospholipid bilayers. In: Ramamoorthy A. (Ed). NMR Spectroscopy of Biological Solids (2006), CRC Press, New York 237-259
    • (2006) NMR Spectroscopy of Biological Solids , pp. 237-259
    • Lorigan, G.A.1
  • 182
    • 0014307971 scopus 로고
    • The use of helical net-diagrams to represent protein structures
    • Dunnill P. The use of helical net-diagrams to represent protein structures. Biophys. J. 8 (1968) 865-875
    • (1968) Biophys. J. , vol.8 , pp. 865-875
    • Dunnill, P.1
  • 183
    • 0027764344 scopus 로고
    • Protein sequence alignments: a strategy for the hierarchical analysis of residue conservation
    • Livingstone C.D., and Barton G.J. Protein sequence alignments: a strategy for the hierarchical analysis of residue conservation. Comput. Appl. Biosci. 9 (1993) 745-756
    • (1993) Comput. Appl. Biosci. , vol.9 , pp. 745-756
    • Livingstone, C.D.1    Barton, G.J.2
  • 184
    • 0036430199 scopus 로고    scopus 로고
    • Proline-induced distortions of transmembrane helices
    • Cordes F.S., Bright J.N., and Sansom M.S.P. Proline-induced distortions of transmembrane helices. J. Mol. Biol. 323 (2002) 951-960
    • (2002) J. Mol. Biol. , vol.323 , pp. 951-960
    • Cordes, F.S.1    Bright, J.N.2    Sansom, M.S.P.3
  • 185
    • 0042931286 scopus 로고    scopus 로고
    • Sequence motifs, polar interactions and conformational changes in helical membrane proteins
    • Curran A.R., and Engelman D.M. Sequence motifs, polar interactions and conformational changes in helical membrane proteins. Curr. Opin. Struct. Biol. 13 (2003) 412-417
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 412-417
    • Curran, A.R.1    Engelman, D.M.2
  • 186
    • 4143085058 scopus 로고    scopus 로고
    • Folding of helical membrane proteins: the role of polar, GxxxG-like and proline motifs
    • Senes A., Engel D.E., and DeGrado W.F. Folding of helical membrane proteins: the role of polar, GxxxG-like and proline motifs. Curr. Opin. Struct. Biol. 14 (2004) 465-479
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 465-479
    • Senes, A.1    Engel, D.E.2    DeGrado, W.F.3
  • 187
    • 33746082078 scopus 로고    scopus 로고
    • Lipid solvation effects contribute to the affinity of Gly-xxx-Gly motif-mediated helix-helix interactions
    • Johnson R.M., Rath A., Melnyk R.A., and Deber C.M. Lipid solvation effects contribute to the affinity of Gly-xxx-Gly motif-mediated helix-helix interactions. Biochemistry 45 (2006) 8507-8515
    • (2006) Biochemistry , vol.45 , pp. 8507-8515
    • Johnson, R.M.1    Rath, A.2    Melnyk, R.A.3    Deber, C.M.4
  • 188
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: a program for display and analysis of macromolecular structures
    • Koradi R., Billeter M., and Wüthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14 (1996) 51-55
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 189
    • 0031853671 scopus 로고    scopus 로고
    • Dipolar recoupling in MAS spectra of biological solids
    • Griffin R.G. Dipolar recoupling in MAS spectra of biological solids. Nat. Struct. Biol. 5 Suppl (1998) 512
    • (1998) Nat. Struct. Biol. , vol.5 SUPPL , pp. 512
    • Griffin, R.G.1
  • 192
    • 0000953276 scopus 로고    scopus 로고
    • 1H dipolar-assisted rotational resonance in magic-angle spinning NMR
    • 1H dipolar-assisted rotational resonance in magic-angle spinning NMR. Chem. Phys. Lett. 344 (2001) 631-637
    • (2001) Chem. Phys. Lett. , vol.344 , pp. 631-637
    • Takegoshi, K.1    Nakamura, S.2    Terao, T.3
  • 194
    • 0033170449 scopus 로고    scopus 로고
    • 13C labeling and two-dimensional solid-state NMR
    • 13C labeling and two-dimensional solid-state NMR. J. Magn. Reson. 139 (1999) 389-401
    • (1999) J. Magn. Reson. , vol.139 , pp. 389-401
    • Hong, M.1
  • 196
    • 0344393786 scopus 로고    scopus 로고
    • High-resolution solid-state NMR applied to polypeptides and membrane proteins
    • Luca S., Heise H., and Baldus M. High-resolution solid-state NMR applied to polypeptides and membrane proteins. Acc. Chem. Res. 36 (2003) 858-865
    • (2003) Acc. Chem. Res. , vol.36 , pp. 858-865
    • Luca, S.1    Heise, H.2    Baldus, M.3
  • 197
    • 4744357287 scopus 로고    scopus 로고
    • Structural and dynamic studies of proteins by solid-state NMR spectroscopy: rapid movement forward
    • McDermott A.E. Structural and dynamic studies of proteins by solid-state NMR spectroscopy: rapid movement forward. Curr. Opin. Struct. Biol. 14 (2004) 554-561
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 554-561
    • McDermott, A.E.1
  • 199
    • 13444259506 scopus 로고    scopus 로고
    • 3D NMR spectroscopy for resonance assignment and structure elucidation of proteins under MAS: novel pulse schemes and sensitivity considerations
    • Heise H., Seidel K., Etzkorn M., Becker S., and Baldus M. 3D NMR spectroscopy for resonance assignment and structure elucidation of proteins under MAS: novel pulse schemes and sensitivity considerations. J. Magn. Reson. 173 (2005) 64-74
    • (2005) J. Magn. Reson. , vol.173 , pp. 64-74
    • Heise, H.1    Seidel, K.2    Etzkorn, M.3    Becker, S.4    Baldus, M.5
  • 200
    • 0034167578 scopus 로고    scopus 로고
    • Sample optimization and identification of signal patterns of amino acid side chains in 2D RFDR spectra of the α-spectrin SH3 domain
    • Pauli J., van Rossum B., Förster H., de Groot H.J.M., and Oschkinat H. Sample optimization and identification of signal patterns of amino acid side chains in 2D RFDR spectra of the α-spectrin SH3 domain. J. Magn. Reson. 143 (2000) 411-416
    • (2000) J. Magn. Reson. , vol.143 , pp. 411-416
    • Pauli, J.1    van Rossum, B.2    Förster, H.3    de Groot, H.J.M.4    Oschkinat, H.5
  • 205
    • 1942489080 scopus 로고    scopus 로고
    • Assignment of the backbone resonances for microcrystalline ubiquitin
    • Igumenova I., Wand A.J., and McDermott A.E. Assignment of the backbone resonances for microcrystalline ubiquitin. J. Am. Chem. Soc. 126 (2004) 5323-5331
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 5323-5331
    • Igumenova, I.1    Wand, A.J.2    McDermott, A.E.3
  • 206
  • 207
    • 33846430490 scopus 로고    scopus 로고
    • Secondary structure, dynamics and topology of a seven-helix receptor in native membranes, studied by solid-state NMR spectroscopy
    • Etzkorn M., Martell S., Andronesi O.C., Seidel K., Engelhard M., and Baldus M. Secondary structure, dynamics and topology of a seven-helix receptor in native membranes, studied by solid-state NMR spectroscopy. Angew. Chem., Int. Ed. 46 (2007) 459-462
    • (2007) Angew. Chem., Int. Ed. , vol.46 , pp. 459-462
    • Etzkorn, M.1    Martell, S.2    Andronesi, O.C.3    Seidel, K.4    Engelhard, M.5    Baldus, M.6
  • 208
    • 25144453329 scopus 로고    scopus 로고
    • Determination of membrane protein structure and dynamics by magic-angle-spinning solid-state NMR spectroscopy
    • Andronesi O.C., Becker S., Seidel K., Heise H., Young H.S., and Baldus M. Determination of membrane protein structure and dynamics by magic-angle-spinning solid-state NMR spectroscopy. J. Am. Chem. Soc. 127 (2005) 12965-12974
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 12965-12974
    • Andronesi, O.C.1    Becker, S.2    Seidel, K.3    Heise, H.4    Young, H.S.5    Baldus, M.6
  • 209
    • 33748479782 scopus 로고    scopus 로고
    • Structural dynamics and topology of phospholamban in oriented lipid bilayers using multi-dimensional solid-state NMR
    • Traaseth N.J., Buffy J.J., Zamoon J., and Veglia G. Structural dynamics and topology of phospholamban in oriented lipid bilayers using multi-dimensional solid-state NMR. Biochemistry 45 (2006) 13827-13834
    • (2006) Biochemistry , vol.45 , pp. 13827-13834
    • Traaseth, N.J.1    Buffy, J.J.2    Zamoon, J.3    Veglia, G.4
  • 210
    • 16344378243 scopus 로고    scopus 로고
    • Mapping the interaction surface of a membrane protein: unveiling the conformational switch of phospholamban in calcium pump regulation
    • Zamoon J., Nitu F., Karim C., Thomas D.D., and Veglia G. Mapping the interaction surface of a membrane protein: unveiling the conformational switch of phospholamban in calcium pump regulation. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 4747-4752
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 4747-4752
    • Zamoon, J.1    Nitu, F.2    Karim, C.3    Thomas, D.D.4    Veglia, G.5
  • 211
    • 4143073485 scopus 로고    scopus 로고
    • 15N Heteronuclear NMR spectroscopy shows four dynamic domains for phospholamban reconstituted in dodecylphosphocholine micelles
    • 15N Heteronuclear NMR spectroscopy shows four dynamic domains for phospholamban reconstituted in dodecylphosphocholine micelles. Biophys. J. 87 (2004) 1205-1214
    • (2004) Biophys. J. , vol.87 , pp. 1205-1214
    • Metcalfe, E.E.1    Zamoon, J.2    Thomas, D.D.3    Veglia, G.4
  • 212
    • 34247848052 scopus 로고    scopus 로고
    • 15N chemical-shift assignments of the disulfide-bond-forming enzyme DsbB by 3D magic-angle spinning NMR spectroscopy
    • 15N chemical-shift assignments of the disulfide-bond-forming enzyme DsbB by 3D magic-angle spinning NMR spectroscopy. Chembiochem 8 (2007) 434-442
    • (2007) Chembiochem , vol.8 , pp. 434-442
    • Li, Y.1    Berthold, D.A.2    Frericks, H.L.3    Gennis, R.B.4    Rienstra, C.M.5
  • 216
    • 33751237696 scopus 로고    scopus 로고
    • Structural analysis of nanoscale self-assembled discoidal lipid bilayers by solid-state NMR spectroscopy
    • Li Y., Kijac A.Z., Sligar S.G., and Rienstra C.M. Structural analysis of nanoscale self-assembled discoidal lipid bilayers by solid-state NMR spectroscopy. Biophys. J. 91 (2006) 3819-3828
    • (2006) Biophys. J. , vol.91 , pp. 3819-3828
    • Li, Y.1    Kijac, A.Z.2    Sligar, S.G.3    Rienstra, C.M.4
  • 217
    • 21844474558 scopus 로고    scopus 로고
    • Investigation of ligand-receptor systems by high-resolution solid-state NMR: recent progress and perspectives
    • Luca S., Heise H., Lange A., and Baldus M. Investigation of ligand-receptor systems by high-resolution solid-state NMR: recent progress and perspectives. Arch. Pharm. Chem. Life Sci. 338 (2005) 217-228
    • (2005) Arch. Pharm. Chem. Life Sci. , vol.338 , pp. 217-228
    • Luca, S.1    Heise, H.2    Lange, A.3    Baldus, M.4
  • 218
    • 24144475875 scopus 로고    scopus 로고
    • Probing conformational disorder in neurotensin by two-dimensional solid-state NMR and comparison to molecular dynamics simulations
    • Heise H., Luca S., de Groot B.L., Grubmüller H., and Baldus M. Probing conformational disorder in neurotensin by two-dimensional solid-state NMR and comparison to molecular dynamics simulations. Biophys. J. 89 (2005) 2113-2120
    • (2005) Biophys. J. , vol.89 , pp. 2113-2120
    • Heise, H.1    Luca, S.2    de Groot, B.L.3    Grubmüller, H.4    Baldus, M.5
  • 223
    • 33748344482 scopus 로고    scopus 로고
    • Conformational flexibility of a microcrystalline globular protein: order parameters by solid-state NMR spectroscopy
    • Lorieau J.L., and McDermott A.E. Conformational flexibility of a microcrystalline globular protein: order parameters by solid-state NMR spectroscopy. J. Am. Chem. Soc. 128 (2006) 11505-11512
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 11505-11512
    • Lorieau, J.L.1    McDermott, A.E.2
  • 224
    • 0033578349 scopus 로고    scopus 로고
    • Deuterium magic angle spinning studies of substrates bound to cytochrome P450
    • Lee H., Ortiz de Montellano P.R., and McDermott A.E. Deuterium magic angle spinning studies of substrates bound to cytochrome P450. Biochemistry 38 (1999) 10808-10813
    • (1999) Biochemistry , vol.38 , pp. 10808-10813
    • Lee, H.1    Ortiz de Montellano, P.R.2    McDermott, A.E.3
  • 225
    • 26444481982 scopus 로고    scopus 로고
    • Observation of ligand binding to cytochrome P450 BM-3 by means of solid-state NMR spectroscopy
    • Jovanovic T., and McDermott A.E. Observation of ligand binding to cytochrome P450 BM-3 by means of solid-state NMR spectroscopy. J. Am. Chem. Soc. 127 (2005) 13816-13821
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 13816-13821
    • Jovanovic, T.1    McDermott, A.E.2
  • 226
    • 25844447810 scopus 로고    scopus 로고
    • Thermal equilibrium of high- and low-spin forms of cytochrome P450 BM-3: repositioning of the substrate?
    • Jovanovic T., Farid R., Friesner R.A., and McDermott A.E. Thermal equilibrium of high- and low-spin forms of cytochrome P450 BM-3: repositioning of the substrate?. J. Am. Chem. Soc. 127 (2005) 13548-13552
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 13548-13552
    • Jovanovic, T.1    Farid, R.2    Friesner, R.A.3    McDermott, A.E.4
  • 227
    • 33646588326 scopus 로고    scopus 로고
    • Conformational equilibrium of cytochrome P450 BM-3 complexed with N-palmitoylglycine: a replica exchange molecular dynamics study
    • Ravindranathan K.P., Gallicchio E., Friesner R.A., McDermott A.E., and Levy R.M. Conformational equilibrium of cytochrome P450 BM-3 complexed with N-palmitoylglycine: a replica exchange molecular dynamics study. J. Am. Chem. Soc. 128 (2006) 5786-5791
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 5786-5791
    • Ravindranathan, K.P.1    Gallicchio, E.2    Friesner, R.A.3    McDermott, A.E.4    Levy, R.M.5
  • 228
    • 33846453575 scopus 로고    scopus 로고
    • Conformational dynamics of substrate in the active site of cytochrome P450 BM-3/NPG complex: insights from NMR order parameters
    • Ravindranathan K.P., Gallicchio E., McDermott A.E., and Levy R.M. Conformational dynamics of substrate in the active site of cytochrome P450 BM-3/NPG complex: insights from NMR order parameters. J. Am. Chem. Soc. 129 (2007) 474-475
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 474-475
    • Ravindranathan, K.P.1    Gallicchio, E.2    McDermott, A.E.3    Levy, R.M.4
  • 229
    • 0037076392 scopus 로고    scopus 로고
    • Single-molecule height measurements on microsomal cytochrome P450 in nanometer-scale phospholipid bilayer disks
    • Bayburt T.H., and Sligar S.G. Single-molecule height measurements on microsomal cytochrome P450 in nanometer-scale phospholipid bilayer disks. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 6725-6730
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 6725-6730
    • Bayburt, T.H.1    Sligar, S.G.2
  • 230
    • 0042691480 scopus 로고    scopus 로고
    • Direct solubilization of heterologously expressed membrane proteins by incorporation into nanoscale lipid bilayers
    • Civjan N.R., Bayburt T.H., Schuler M.A., and Sligar S.G. Direct solubilization of heterologously expressed membrane proteins by incorporation into nanoscale lipid bilayers. Biotechniques 35 (2003) 556-560
    • (2003) Biotechniques , vol.35 , pp. 556-560
    • Civjan, N.R.1    Bayburt, T.H.2    Schuler, M.A.3    Sligar, S.G.4
  • 231
    • 0032170742 scopus 로고    scopus 로고
    • Reconstitution and imaging of a membrane protein in a nanometer-size phospholipid bilayer
    • Bayburt T.H., Carlson J.W., and Sligar S.G. Reconstitution and imaging of a membrane protein in a nanometer-size phospholipid bilayer. J. Struct. Biol. 123 (1998) 37-44
    • (1998) J. Struct. Biol. , vol.123 , pp. 37-44
    • Bayburt, T.H.1    Carlson, J.W.2    Sligar, S.G.3
  • 235
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • Cornilescu G., Delaglio F., and Bax A. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR 13 (1999) 289-302
    • (1999) J. Biomol. NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 236
    • 0347610773 scopus 로고
    • Empirical correlation between protein backbone conformation and Cα and Cβ nuclear magnetic resonance chemical shifts
    • Spera S., and Bax A. Empirical correlation between protein backbone conformation and Cα and Cβ nuclear magnetic resonance chemical shifts. J. Am. Chem. Soc. 113 (1991) 5490-5492
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 5490-5492
    • Spera, S.1    Bax, A.2
  • 237
    • 34248583208 scopus 로고    scopus 로고
    • All-atom molecular dynamics simulations using orientational constraints from anisotropic NMR samples
    • Sternberg U., Witter R., and Ulrich A.S. All-atom molecular dynamics simulations using orientational constraints from anisotropic NMR samples. J. Biomol. NMR 38 (2007) 23-39
    • (2007) J. Biomol. NMR , vol.38 , pp. 23-39
    • Sternberg, U.1    Witter, R.2    Ulrich, A.S.3
  • 241
    • 33646594751 scopus 로고    scopus 로고
    • A high-resolution solid-state NMR approach for the structural studies of bicelles
    • Dvinskikh S.V., Dürr U.H.N., Yamamoto K., and Ramamoorthy A. A high-resolution solid-state NMR approach for the structural studies of bicelles. J. Am. Chem. Soc. 128 (2006) 6326-6327
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 6326-6327
    • Dvinskikh, S.V.1    Dürr, U.H.N.2    Yamamoto, K.3    Ramamoorthy, A.4
  • 242
    • 33846609269 scopus 로고    scopus 로고
    • High-resolution 2D NMR spectroscopy of bicelles to measure the membrane interaction of ligands
    • Dvinskikh S.V., Dürr U.H.N., Yamamoto K., and Ramamoorthy A. High-resolution 2D NMR spectroscopy of bicelles to measure the membrane interaction of ligands. J. Am. Chem. Soc. 129 (2007) 794-802
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 794-802
    • Dvinskikh, S.V.1    Dürr, U.H.N.2    Yamamoto, K.3    Ramamoorthy, A.4
  • 244
    • 33846625059 scopus 로고    scopus 로고
    • Sensitivity and resolution enhancement in solid-state NMR spectroscopy of bicelles
    • Dvinskikh S.V., Yamamoto K., Dürr U.H.N., and Ramamoorthy A. Sensitivity and resolution enhancement in solid-state NMR spectroscopy of bicelles. J. Magn. Reson. 184 (2007) 228-235
    • (2007) J. Magn. Reson. , vol.184 , pp. 228-235
    • Dvinskikh, S.V.1    Yamamoto, K.2    Dürr, U.H.N.3    Ramamoorthy, A.4
  • 245
    • 14644399800 scopus 로고    scopus 로고
    • Efficient solid-state NMR methods for measuring heteronuclear dipolar couplings in unoriented lipid membrane systems
    • Dvinskikh S.V., Castro V., and Sandström D. Efficient solid-state NMR methods for measuring heteronuclear dipolar couplings in unoriented lipid membrane systems. Phys. Chem. Chem. Phys. 7 (2005) 607-613
    • (2005) Phys. Chem. Chem. Phys. , vol.7 , pp. 607-613
    • Dvinskikh, S.V.1    Castro, V.2    Sandström, D.3
  • 246
    • 26244434597 scopus 로고    scopus 로고
    • Probing segmental order in lipid bilayers at variable hydration levels by amplitude- and phase-modulated cross-polarization NMR
    • Dvinskikh S.V., Castro V., and Sandström D. Probing segmental order in lipid bilayers at variable hydration levels by amplitude- and phase-modulated cross-polarization NMR. Phys. Chem. Chem. Phys. 7 (2005) 3255-3257
    • (2005) Phys. Chem. Chem. Phys. , vol.7 , pp. 3255-3257
    • Dvinskikh, S.V.1    Castro, V.2    Sandström, D.3


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