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Volumn 23, Issue 5, 2013, Pages 740-747

Fluorine-19 NMR of integral membrane proteins illustrated with studies of GPCRs

Author keywords

[No Author keywords available]

Indexed keywords

2,2,2 TRIFLUOROETHANETHIOL; 3 BROMO 1,1,1 TRIFLUOROACETONE; 4 (PERFLUORO TERT BUTYL)PHENYLIODOCETAMIDE; AMINO ACID; AMINO ACID DERIVATIVE; BACTERIORHODOPSIN; BETA 2 ADRENERGIC RECEPTOR; CIC EC1 CHLORIDE PROTEIN ANTIPORTER; DEXTRO LACTATE DEHYDROGENASE; DIACYLGLYCEROL KINASE; FLUORINE; G PROTEIN COUPLED RECEPTOR; GRAMICIDIN A; M13 PHAGE COAT PROTEIN; MEMBRANE PROTEIN; POLYPEPTIDE; REAGENT; RHODOPSIN; S ETHYL TRIFLUOROTHIOACETATE; TRIFLUOROETHANOL; UNCLASSIFIED DRUG;

EID: 84885846349     PISSN: 0959440X     EISSN: 1879033X     Source Type: Journal    
DOI: 10.1016/j.sbi.2013.07.011     Document Type: Review
Times cited : (80)

References (56)
  • 1
    • 77956864617 scopus 로고
    • Fluorine-19 nuclear magnetic resonance spectroscopy
    • Mooney E., Winson P. Fluorine-19 nuclear magnetic resonance spectroscopy. Annu Rep NMR Spectrosc 1968, 1:243-311.
    • (1968) Annu Rep NMR Spectrosc , vol.1 , pp. 243-311
    • Mooney, E.1    Winson, P.2
  • 4
    • 0017908546 scopus 로고
    • Fluorine nuclear magnetic resonance studies of proteins
    • Sykes B.D., Hull W.E. Fluorine nuclear magnetic resonance studies of proteins. Methods Enzymol 1978, 49:270-295.
    • (1978) Methods Enzymol , vol.49 , pp. 270-295
    • Sykes, B.D.1    Hull, W.E.2
  • 5
    • 58649124492 scopus 로고    scopus 로고
    • F-19 NMR applications in chemical biology
    • Cobb S.L., Murphy C.D. F-19 NMR applications in chemical biology. J Fluorine Chem 2009, 130:132-143.
    • (2009) J Fluorine Chem , vol.130 , pp. 132-143
    • Cobb, S.L.1    Murphy, C.D.2
  • 6
    • 84857625337 scopus 로고    scopus 로고
    • Current applications of F-19 NMR to studies of protein structure and dynamics
    • Kitevski-LeBlanc J.L., Prosser R.S. Current applications of F-19 NMR to studies of protein structure and dynamics. Prog Nucl Mag Res Spectrosc 2012, 62:1-33.
    • (2012) Prog Nucl Mag Res Spectrosc , vol.62 , pp. 1-33
    • Kitevski-LeBlanc, J.L.1    Prosser, R.S.2
  • 7
    • 0018072054 scopus 로고
    • Fluorotyrosine M13 coat protein: fluorine-19 nuclear magnetic resonance study of the motional properties of an integral membrane protein in phospholipid vesicles
    • Hagen D.S., Weiner J.H., Sykes B.D. Fluorotyrosine M13 coat protein: fluorine-19 nuclear magnetic resonance study of the motional properties of an integral membrane protein in phospholipid vesicles. Biochemistry 1978, 17:3860-3866.
    • (1978) Biochemistry , vol.17 , pp. 3860-3866
    • Hagen, D.S.1    Weiner, J.H.2    Sykes, B.D.3
  • 8
    • 0021814407 scopus 로고
    • Membrane protein conformational change dependent on the hydrophobic environment
    • Wilson M.L., Dahlquist F.W. Membrane protein conformational change dependent on the hydrophobic environment. Biochemistry 1985, 24:1920-1928.
    • (1985) Biochemistry , vol.24 , pp. 1920-1928
    • Wilson, M.L.1    Dahlquist, F.W.2
  • 10
    • 0022434753 scopus 로고
    • Conformation of the gramicidin A channel in phospholipid vesicles: a fluorine-19 nuclear magnetic resonance study
    • Weinstein S., Durkin J.T., Veatch W.R., Blout E.R. Conformation of the gramicidin A channel in phospholipid vesicles: a fluorine-19 nuclear magnetic resonance study. Biochemistry 1985, 24:4374-4382.
    • (1985) Biochemistry , vol.24 , pp. 4374-4382
    • Weinstein, S.1    Durkin, J.T.2    Veatch, W.R.3    Blout, E.R.4
  • 11
    • 0022632505 scopus 로고
    • Nuclear magnetic resonance, biochemical, and molecular genetic studies of the membrane-bound d-lactate dehydrogenase of Escherichia coli
    • Ho C., Rule G.S., Pratt E.A. Nuclear magnetic resonance, biochemical, and molecular genetic studies of the membrane-bound d-lactate dehydrogenase of Escherichia coli. Biophys J 1986, 49:113-115.
    • (1986) Biophys J , vol.49 , pp. 113-115
    • Ho, C.1    Rule, G.S.2    Pratt, E.A.3
  • 12
    • 0030300157 scopus 로고    scopus 로고
    • 19F-NMR study of the equilibrium unfolding of membrane-associated d-lactate dehydrogenase of Escherichia coli
    • 19F-NMR study of the equilibrium unfolding of membrane-associated d-lactate dehydrogenase of Escherichia coli. Biochemistry 1996, 35:16502-16509.
    • (1996) Biochemistry , vol.35 , pp. 16502-16509
    • Sun, Z.Y.1    Pratt, E.A.2    Simplaceanu, V.3    Ho, C.4
  • 16
    • 0037181061 scopus 로고    scopus 로고
    • Oxygen as a paramagnetic probe of membrane protein structure by cysteine mutagenesis and F-19 NMR spectroscopy
    • Luchette P.A., Prosser R.S., Sanders C.R. Oxygen as a paramagnetic probe of membrane protein structure by cysteine mutagenesis and F-19 NMR spectroscopy. J Am Chem Soc 2002, 124:1778-1781.
    • (2002) J Am Chem Soc , vol.124 , pp. 1778-1781
    • Luchette, P.A.1    Prosser, R.S.2    Sanders, C.R.3
  • 17
    • 70350304561 scopus 로고    scopus 로고
    • Substrate-driven conformational changes in ClC-ec1 observed by fluorine NMR
    • Elvington S.M., Liu C.W., Maduke M.C. Substrate-driven conformational changes in ClC-ec1 observed by fluorine NMR. EMBO J 2009, 28:3090-3102.
    • (2009) EMBO J , vol.28 , pp. 3090-3102
    • Elvington, S.M.1    Liu, C.W.2    Maduke, M.C.3
  • 19
    • 84867793026 scopus 로고    scopus 로고
    • Role of detergents in conformational exchange of a G protein-coupled receptor
    • Chung K.Y., Kim T.H., Manglik A., Alvares R., Kobilka B.K., Prosser R.S. Role of detergents in conformational exchange of a G protein-coupled receptor. J Biol Chem 2012, 287:36305-36311.
    • (2012) J Biol Chem , vol.287 , pp. 36305-36311
    • Chung, K.Y.1    Kim, T.H.2    Manglik, A.3    Alvares, R.4    Kobilka, B.K.5    Prosser, R.S.6
  • 20
    • 84885128591 scopus 로고    scopus 로고
    • β2-adrenergic receptor activation by agonists studied with 19F-NMR
    • Horst R., Liu J.J., Stevens R.C., Wüthrich K. β2-adrenergic receptor activation by agonists studied with 19F-NMR. Angew Chem 2013, 10.1002/anie.201305286.
    • (2013) Angew Chem
    • Horst, R.1    Liu, J.J.2    Stevens, R.C.3    Wüthrich, K.4
  • 23
    • 66249121383 scopus 로고    scopus 로고
    • Biophysical dissection of membrane proteins
    • White S.H. Biophysical dissection of membrane proteins. Nature 2009, 459:344-346.
    • (2009) Nature , vol.459 , pp. 344-346
    • White, S.H.1
  • 25
    • 33646893882 scopus 로고    scopus 로고
    • Fluorine-19 NMR studies on the acid state of the intestinal fatty acid binding protein
    • Li H., Frieden C. Fluorine-19 NMR studies on the acid state of the intestinal fatty acid binding protein. Biochemistry 2006, 45:6272-6278.
    • (2006) Biochemistry , vol.45 , pp. 6272-6278
    • Li, H.1    Frieden, C.2
  • 27
    • 10144227798 scopus 로고    scopus 로고
    • F-19 nuclear magnetic resonance chemical shifts of fluorine containing aliphatic amino acids in proteins: Studies on Lactobacillus casei dihydrofolate reductase containing (2S,4S)-5-fluoroleucine
    • Feeney J., McCormick J.E., Bauer C.J., Birdsall B., Moody C.M., Starkmann B.A., Young D.W., Francis P., Havlin R.H., Arnold W.D., Oldfield E. F-19 nuclear magnetic resonance chemical shifts of fluorine containing aliphatic amino acids in proteins: Studies on Lactobacillus casei dihydrofolate reductase containing (2S,4S)-5-fluoroleucine. J Am Chem Soc 1996, 118:8700-8706.
    • (1996) J Am Chem Soc , vol.118 , pp. 8700-8706
    • Feeney, J.1    McCormick, J.E.2    Bauer, C.J.3    Birdsall, B.4    Moody, C.M.5    Starkmann, B.A.6    Young, D.W.7    Francis, P.8    Havlin, R.H.9    Arnold, W.D.10    Oldfield, E.11
  • 28
    • 67849121879 scopus 로고    scopus 로고
    • A mutagenesis-free approach to assignment of F-19 NMR resonances in biosynthetically labeled proteins
    • Kitevski-LeBlanc J.L., Al-Abdul-Wahid M.S., Prosser R.S. A mutagenesis-free approach to assignment of F-19 NMR resonances in biosynthetically labeled proteins. J Am Chem Soc 2009, 131:2054-2055.
    • (2009) J Am Chem Soc , vol.131 , pp. 2054-2055
    • Kitevski-LeBlanc, J.L.1    Al-Abdul-Wahid, M.S.2    Prosser, R.S.3
  • 29
    • 77954690041 scopus 로고    scopus 로고
    • Approaches to the assignment of F-19 resonances from 3-fluorophenylalanine labeled calmodulin using solution state NMR
    • Kitevski-LeBlanc J.L., Evanics F., Prosser R.S. Approaches to the assignment of F-19 resonances from 3-fluorophenylalanine labeled calmodulin using solution state NMR. J Biomol NMR 2010, 47:113-123.
    • (2010) J Biomol NMR , vol.47 , pp. 113-123
    • Kitevski-LeBlanc, J.L.1    Evanics, F.2    Prosser, R.S.3
  • 31
    • 0018791397 scopus 로고
    • Investigation of solvent accessibility of the fluorotyrosyl residues of M13 coat protein in deoxycholate micelles and phospholipid vesicles
    • Hagen D.S., Weiner J.H., Sykes B.D. Investigation of solvent accessibility of the fluorotyrosyl residues of M13 coat protein in deoxycholate micelles and phospholipid vesicles. Biochemistry 1979, 18:2007-2012.
    • (1979) Biochemistry , vol.18 , pp. 2007-2012
    • Hagen, D.S.1    Weiner, J.H.2    Sykes, B.D.3
  • 33
    • 0034630843 scopus 로고    scopus 로고
    • Origins of fluorine NMR chemical shifts in fluorine-containing proteins
    • Lau E.Y., Gerig J.T. Origins of fluorine NMR chemical shifts in fluorine-containing proteins. J Am Chem Soc 2000, 122:4408-4417.
    • (2000) J Am Chem Soc , vol.122 , pp. 4408-4417
    • Lau, E.Y.1    Gerig, J.T.2
  • 35
    • 0028427909 scopus 로고
    • Fluorinated proteins as potential F-19 magnetic-resonance-imaging and spectroscopy agents
    • Mehta V.D., Kulkarni P.V., Mason R.P., Constantinescu A., Antich P.P. Fluorinated proteins as potential F-19 magnetic-resonance-imaging and spectroscopy agents. Bioconjug Chem 1994, 5:257-261.
    • (1994) Bioconjug Chem , vol.5 , pp. 257-261
    • Mehta, V.D.1    Kulkarni, P.V.2    Mason, R.P.3    Constantinescu, A.4    Antich, P.P.5
  • 36
    • 0016697706 scopus 로고
    • 19F nuclear spin relaxation mechanism in proteins
    • 19F nuclear spin relaxation mechanism in proteins. J Mol Biol 1975, 98:121-153.
    • (1975) J Mol Biol , vol.98 , pp. 121-153
    • Hull, W.E.1    Sykes, B.D.2
  • 37
    • 1542379799 scopus 로고    scopus 로고
    • The preparation of F-19-labeled proteins for NMR studies
    • Frieden C., Hoeltzli S.D., Bann J.G. The preparation of F-19-labeled proteins for NMR studies. Method Enzymol 2004, 380:400-415.
    • (2004) Method Enzymol , vol.380 , pp. 400-415
    • Frieden, C.1    Hoeltzli, S.D.2    Bann, J.G.3
  • 41
    • 33846809165 scopus 로고    scopus 로고
    • Site-specific incorporation of a (19)F-amino acid into proteins as an NMR probe for characterizing protein structure and reactivity
    • Jackson J.C., Hammill J.T., Mehl R.A. Site-specific incorporation of a (19)F-amino acid into proteins as an NMR probe for characterizing protein structure and reactivity. J Am Chem Soc 2007, 129:1160-1166.
    • (2007) J Am Chem Soc , vol.129 , pp. 1160-1166
    • Jackson, J.C.1    Hammill, J.T.2    Mehl, R.A.3
  • 43
    • 78650773762 scopus 로고    scopus 로고
    • Site-specific (19)F NMR chemical shift and side chain relaxation analysis of a membrane protein labeled with an unnatural amino acid
    • Shi P., Wang H., Xi Z., Shi C., Xiong Y., Tian C. Site-specific (19)F NMR chemical shift and side chain relaxation analysis of a membrane protein labeled with an unnatural amino acid. Protein Sci 2011, 20:224-228.
    • (2011) Protein Sci , vol.20 , pp. 224-228
    • Shi, P.1    Wang, H.2    Xi, Z.3    Shi, C.4    Xiong, Y.5    Tian, C.6
  • 45
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes
    • Krogh A., Larsson B., von Heijne G., Sonnhammer E.L. Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J Mol Biol 2001, 305:567-580.
    • (2001) J Mol Biol , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    von Heijne, G.3    Sonnhammer, E.L.4
  • 48
    • 29144531173 scopus 로고    scopus 로고
    • The druggable genome: an update
    • Russ A.P., Lampel S. The druggable genome: an update. Drug Discov Today 2005, 10:1607-1610.
    • (2005) Drug Discov Today , vol.10 , pp. 1607-1610
    • Russ, A.P.1    Lampel, S.2
  • 55
    • 34547545562 scopus 로고    scopus 로고
    • Observation of sequential steps in the folding of intestinal fatty acid binding protein using a slow folding mutant and F-19 NMR
    • Li H.L., Frieden C. Observation of sequential steps in the folding of intestinal fatty acid binding protein using a slow folding mutant and F-19 NMR. Proc Natl Acad Sci U S A 2007, 104:11993-11998.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 11993-11998
    • Li, H.L.1    Frieden, C.2
  • 56
    • 0032516767 scopus 로고    scopus 로고
    • Conformational changes in the crystal structure of rat glutathione transferase M1-1 with global substitution of 3-fluorotyrosine for tyrosine
    • Xiao G.Y., Parsons J.F., Tesh K., Armstrong R.N., Gilliland G.L. Conformational changes in the crystal structure of rat glutathione transferase M1-1 with global substitution of 3-fluorotyrosine for tyrosine. J Mol Biol 1998, 281:323-339.
    • (1998) J Mol Biol , vol.281 , pp. 323-339
    • Xiao, G.Y.1    Parsons, J.F.2    Tesh, K.3    Armstrong, R.N.4    Gilliland, G.L.5


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