메뉴 건너뛰기




Volumn 42, Issue 4, 2008, Pages 257-269

Biosynthesis and NMR-studies of a double transmembrane domain from the Y4 receptor, a human GPCR

Author keywords

Detergents; G protein coupled receptor (GPCR); Solution NMR; Transmembrane domain; Y receptor

Indexed keywords

DODECYLPHOSPHORYLCHOLINE; G PROTEIN COUPLED RECEPTOR; NEUROPEPTIDE Y4 RECEPTOR;

EID: 55949115886     PISSN: 09252738     EISSN: 15735001     Source Type: Journal    
DOI: 10.1007/s10858-008-9281-z     Document Type: Article
Times cited : (16)

References (87)
  • 1
    • 0037648337 scopus 로고    scopus 로고
    • Structure-based analysis of GPCR function: Conformational adaptation of both agonist and receptor upon leukotriene B4 binding to recombinant BLT1
    • Baneres JL, Martin A, Hullot P, Girard JP, Rossi JC, Parello J (2003) Structure-based analysis of GPCR function: Conformational adaptation of both agonist and receptor upon leukotriene B4 binding to recombinant BLT1. J Mol Biol 329:801-814
    • (2003) J Mol Biol , vol.329 , pp. 801-814
    • Baneres, J.L.1    Martin, A.2    Hullot, P.3    Girard, J.P.4    Rossi, J.C.5    Parello, J.6
  • 2
    • 20144385917 scopus 로고    scopus 로고
    • Molecular characterization of a purified 5-HT4 receptor: A structural basis for drug efficacy
    • Banères JL, Mesnier D, Martin A, Joubert L, Dumuis A, Bockaert J (2005) Molecular characterization of a purified 5-HT4 receptor: A structural basis for drug efficacy. J Biol Chem 280:20253-20260
    • (2005) J Biol Chem , vol.280 , pp. 20253-20260
    • Banères, J.L.1    Mesnier, D.2    Martin, A.3    Joubert, L.4    Dumuis, A.5    Bockaert, J.6
  • 4
    • 0031892162 scopus 로고    scopus 로고
    • How many membrane proteins are there?
    • Boyd D, Schierle C, Beckwith J (1998) How many membrane proteins are there? Protein Sci 7:201-205
    • (1998) Protein Sci , vol.7 , pp. 201-205
    • Boyd, D.1    Schierle, C.2    Beckwith, J.3
  • 7
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • Cornilescu G, Delaglio F, Bax A (1999) Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J Biomol NMR 13:289-302
    • (1999) J Biomol NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 8
    • 0037450542 scopus 로고    scopus 로고
    • Assembly and overexpression of membrane proteins in Escherichia coli
    • Drew D, Froderberg L, Baars L, De Gier JW (2003) Assembly and overexpression of membrane proteins in Escherichia coli. Biochim Biophys Acta 1610:3-10
    • (2003) Biochim Biophys Acta , vol.1610 , pp. 3-10
    • Drew, D.1    Froderberg, L.2    Baars, L.3    De Gier, J.W.4
  • 10
    • 28444437064 scopus 로고    scopus 로고
    • Membranes are more mosaic than fluid
    • Engelman DM (2005) Membranes are more mosaic than fluid. Nature 438:578-580
    • (2005) Nature , vol.438 , pp. 578-580
    • Engelman, D.M.1
  • 11
    • 0036791447 scopus 로고    scopus 로고
    • Receptor classification: Post genome
    • Foord SM (2002) Receptor classification: Post genome. Curr Opin Pharmacol 2:561-566
    • (2002) Curr Opin Pharmacol , vol.2 , pp. 561-566
    • Foord, S.M.1
  • 15
    • 26444581283 scopus 로고    scopus 로고
    • Large-scale expression and purification of a G-protein-coupled receptor for structure determination-an overview
    • Grisshammer R, White JF, Trinh LB, Shiloach J (2005) Large-scale expression and purification of a G-protein-coupled receptor for structure determination-an overview. J Struct Funct Genomics 6:159-163
    • (2005) J Struct Funct Genomics , vol.6 , pp. 159-163
    • Grisshammer, R.1    White, J.F.2    Trinh, L.B.3    Shiloach, J.4
  • 16
    • 0035716295 scopus 로고    scopus 로고
    • Family-B G-protein-coupled receptors
    • Harmar AJ (2001) Family-B G-protein-coupled receptors. Genome Biol 2:30131-3013.10
    • (2001) Genome Biol , vol.2
    • Harmar, A.J.1
  • 20
    • 16344376576 scopus 로고    scopus 로고
    • NMR structure determination of a membrane protein with two transmembrane helices in micelles: MerF of the bacterial mercury detoxification system
    • Howell SC, Mesleh MF, Opella SJ (2005) NMR structure determination of a membrane protein with two transmembrane helices in micelles: MerF of the bacterial mercury detoxification system. Biochemistry 44:5196-5206
    • (2005) Biochemistry , vol.44 , pp. 5196-5206
    • Howell, S.C.1    Mesleh, M.F.2    Opella, S.J.3
  • 21
    • 0019887931 scopus 로고
    • Refolding of an integral membrane protein. Denaturation, renaturation, and reconstitution of intact bacteriorhodopsin and two proteolytic fragments
    • Huang KS, Bayley H, Liao MJ, London E, Khorana HG (1981) Refolding of an integral membrane protein. Denaturation, renaturation, and reconstitution of intact bacteriorhodopsin and two proteolytic fragments. J Biol Chem 256:3802-3809
    • (1981) J Biol Chem , vol.256 , pp. 3802-3809
    • Huang, K.S.1    Bayley, H.2    Liao, M.J.3    London, E.4    Khorana, H.G.5
  • 23
    • 0026642866 scopus 로고
    • Bacteriorhodopsin can be refolded from two independently stable transmembrane helices and the complementary five-helix fragment
    • Kahn TW, Engelman DM (1992) Bacteriorhodopsin can be refolded from two independently stable transmembrane helices and the complementary five-helix fragment. Biochemistry 31:6144-6151
    • (1992) Biochemistry , vol.31 , pp. 6144-6151
    • Kahn, T.W.1    Engelman, D.M.2
  • 24
    • 0034909370 scopus 로고    scopus 로고
    • Assembly of a polytopic membrane protein structure from the solution structures of overlapping peptide fragments of bacteriorhodopsin
    • Katragadda M, Alderfer JL, Yeagle PL (2001a) Assembly of a polytopic membrane protein structure from the solution structures of overlapping peptide fragments of bacteriorhodopsin. Biophys J 81:1029-1036
    • (2001) Biophys J , vol.81 , pp. 1029-1036
    • Katragadda, M.1    Alderfer, J.L.2    Yeagle, P.L.3
  • 26
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced heteronuclear single-quantum correlation sepctroscopy with improved sensitivity
    • Kay LE, Keifer P, Saarien T (1992) Pure absorption gradient enhanced heteronuclear single-quantum correlation sepctroscopy with improved sensitivity. J Am Chem Soc 114:10663-10665
    • (1992) J Am Chem Soc , vol.114 , pp. 10663-10665
    • Kay, L.E.1    Keifer, P.2    Saarien, T.3
  • 29
    • 0030467888 scopus 로고    scopus 로고
    • Expression of an olfactory receptor in Escherichia coli: Purification, reconstitution, and ligand binding
    • Kiefer H, Krieger J, Olszewski JD, Von Heijne G, Prestwich GD, Breer H (1996) Expression of an olfactory receptor in Escherichia coli: purification, reconstitution, and ligand binding. Biochemistry 35:16077-16084
    • (1996) Biochemistry , vol.35 , pp. 16077-16084
    • Kiefer, H.1    Krieger, J.2    Olszewski, J.D.3    Von Heijne, G.4    Prestwich, G.D.5    Breer, H.6
  • 30
    • 34347391677 scopus 로고    scopus 로고
    • Functional analysis of cell-free-produced human endothelin B receptor reveals transmembrane segment 1 as an essential area for ET-1 binding and homodimer formation
    • Klammt C, Srivastava A, Eifler N, Junge F, Beyermann M, Schwarz D, Michel H, Dötsch V, Bernhard F (2007) Functional analysis of cell-free-produced human endothelin B receptor reveals transmembrane segment 1 as an essential area for ET-1 binding and homodimer formation. FEBS J 274:3257-3269
    • (2007) FEBS J , vol.274 , pp. 3257-3269
    • Klammt, C.1    Srivastava, A.2    Eifler, N.3    Junge, F.4    Beyermann, M.5    Schwarz, D.6    Michel, H.7    Dötsch, V.8    Bernhard, F.9
  • 31
    • 0037133661 scopus 로고    scopus 로고
    • Solution NMR spectroscopy of [alpha- 15 N]lysine-labeled rhodopsin: The single peak observed in both conventional and TROSY-type HSQC spectra is ascribed to Lys-339 in the carboxyl-terminal peptide sequence
    • Klein-Seetharaman J, Reeves PJ, Loewen MC, Getmanova EV, Chung J, Schwalbe H, Wright PE, Khorana HG (2002) Solution NMR spectroscopy of [alpha- 15 N]lysine-labeled rhodopsin: The single peak observed in both conventional and TROSY-type HSQC spectra is ascribed to Lys-339 in the carboxyl-terminal peptide sequence. Proc Natl Acad Sci USA 99:3452-3457
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 3452-3457
    • Klein-Seetharaman, J.1    Reeves, P.J.2    Loewen, M.C.3    Getmanova, E.V.4    Chung, J.5    Schwalbe, H.6    Wright, P.E.7    Khorana, H.G.8
  • 34
    • 41449108071 scopus 로고    scopus 로고
    • Structure of the integrin beta3 transmembrane segment in phospholipid bicelles and detergent micelles
    • Lau TL, Partridge AW, Ginsberg MH, Ulmer TS (2008) Structure of the integrin beta3 transmembrane segment in phospholipid bicelles and detergent micelles. Biochemistry 47:4008-4016
    • (2008) Biochemistry , vol.47 , pp. 4008-4016
    • Lau, T.L.1    Partridge, A.W.2    Ginsberg, M.H.3    Ulmer, T.S.4
  • 37
    • 20544431791 scopus 로고    scopus 로고
    • Structure and dynamics of the second and third transmembrane domains of human glycine receptor
    • Ma D, Liu Z, Li L, Tang P, Xu Y (2005) Structure and dynamics of the second and third transmembrane domains of human glycine receptor. Biochemistry 44:8790-8800
    • (2005) Biochemistry , vol.44 , pp. 8790-8800
    • Ma, D.1    Liu, Z.2    Li, L.3    Tang, P.4    Xu, Y.5
  • 38
    • 0030932407 scopus 로고    scopus 로고
    • A transmembrane helix dimer-structure and implications
    • Mackenzie KR, Prestegard JH, Engelman DM (1997) A transmembrane helix dimer-structure and implications. Science 276:131-133
    • (1997) Science , vol.276 , pp. 131-133
    • Mackenzie, K.R.1    Prestegard, J.H.2    Engelman, D.M.3
  • 39
    • 0033547819 scopus 로고    scopus 로고
    • Assembly of G protein-coupled receptors from fragments: Identification of functional receptors with discontinuities in each of the loops connecting transmembrane segments
    • Martin NP, Leavitt LM, Sommers CM, Dumont ME (1999) Assembly of G protein-coupled receptors from fragments: Identification of functional receptors with discontinuities in each of the loops connecting transmembrane segments. Biochemistry 38:682-695
    • (1999) Biochemistry , vol.38 , pp. 682-695
    • Martin, N.P.1    Leavitt, L.M.2    Sommers, C.M.3    Dumont, M.E.4
  • 40
    • 0037450572 scopus 로고    scopus 로고
    • G protein-coupled receptor overexpression with the baculovirus-insect cell system: A tool for structural and functional studies
    • Massotte D (2003) G protein-coupled receptor overexpression with the baculovirus-insect cell system: A tool for structural and functional studies. Biochim Biophys Acta 1610:77-89
    • (2003) Biochim Biophys Acta , vol.1610 , pp. 77-89
    • Massotte, D.1
  • 41
    • 0030593468 scopus 로고    scopus 로고
    • Over-production of proteins in Escherichia coli: Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels
    • Miroux B, Walker JE (1996) Over-production of proteins in Escherichia coli: Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels. J Mol Biol 260:289-298
    • (1996) J Mol Biol , vol.260 , pp. 289-298
    • Miroux, B.1    Walker, J.E.2
  • 42
    • 34848892779 scopus 로고    scopus 로고
    • Purification and initiation of structural characterization of human peripheral myelin protein 22, an integral membrane protein linked to peripheral neuropathies
    • Mobley CK, Myers JK, Hadziselimovic A, Ellis CD, Sanders CR (2007) Purification and initiation of structural characterization of human peripheral myelin protein 22, an integral membrane protein linked to peripheral neuropathies. Biochemistry 46:11185-11195
    • (2007) Biochemistry , vol.46 , pp. 11185-11195
    • Mobley, C.K.1    Myers, J.K.2    Hadziselimovic, A.3    Ellis, C.D.4    Sanders, C.R.5
  • 43
    • 43749109187 scopus 로고    scopus 로고
    • Crystal structure of squid rhodopsin
    • Murakami M, Kouyama T (2008) Crystal structure of squid rhodopsin. Nature 453:363-367
    • (2008) Nature , vol.453 , pp. 363-367
    • Murakami, M.1    Kouyama, T.2
  • 45
    • 34447340552 scopus 로고    scopus 로고
    • NMR studies in dodecylphosphocholine of a fragment containing the seventh transmembrane helix of a G-protein-coupled receptor from Saccharomyces cerevisiae
    • Neumoin A, Arshava B, Becker J, Zerbe O, Naider F (2007) NMR studies in dodecylphosphocholine of a fragment containing the seventh transmembrane helix of a G-protein-coupled receptor from Saccharomyces cerevisiae. Biophys J 93:467-482
    • (2007) Biophys J , vol.93 , pp. 467-482
    • Neumoin, A.1    Arshava, B.2    Becker, J.3    Zerbe, O.4    Naider, F.5
  • 51
    • 47049130668 scopus 로고    scopus 로고
    • Crystal structure of the ligand-free G-protein-coupled receptor opsin
    • Park JH, Scheerer P, Hofmann KP, Choe HW, Ernst OP (2008) Crystal structure of the ligand-free G-protein-coupled receptor opsin. Nature 454:183-187
    • (2008) Nature , vol.454 , pp. 183-187
    • Park, J.H.1    Scheerer, P.2    Hofmann, K.P.3    Choe, H.W.4    Ernst, O.P.5
  • 52
    • 0030612833 scopus 로고    scopus 로고
    • Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution
    • Pervushin K, Riek R, Wider G, Wüthrich K (1997) Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution. Proc Natl Acad Sci USA 94:12366-12371
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 12366-12371
    • Pervushin, K.1    Riek, R.2    Wider, G.3    Wüthrich, K.4
  • 53
    • 36849088540 scopus 로고    scopus 로고
    • Solution NMR of membrane proteins in bilayer mimics: Small is beautiful, but sometimes bigger is better
    • Poget SF, Girvin ME (2007) Solution NMR of membrane proteins in bilayer mimics: Small is beautiful, but sometimes bigger is better. Biochim Biophys Acta 1768:3098-3106
    • (2007) Biochim Biophys Acta , vol.1768 , pp. 3098-3106
    • Poget, S.F.1    Girvin, M.E.2
  • 54
    • 0025249842 scopus 로고
    • Membrane protein folding and oligomerization: The two-stage model
    • Popot JL, Engelman DM (1990) Membrane protein folding and oligomerization: The two-stage model. Biochemistry 29:4031-4037
    • (1990) Biochemistry , vol.29 , pp. 4031-4037
    • Popot, J.L.1    Engelman, D.M.2
  • 55
    • 0033790343 scopus 로고    scopus 로고
    • Helical membrane protein folding, stability, and evolution
    • Popot JL, Engelman DM (2000) Helical membrane protein folding, stability, and evolution. Annu Rev Biochem 69:881-922
    • (2000) Annu Rev Biochem , vol.69 , pp. 881-922
    • Popot, J.L.1    Engelman, D.M.2
  • 56
    • 0033581879 scopus 로고    scopus 로고
    • Structural changes linked to proton translocation by subunit c of the ATP synthase
    • Rastogi VK, Girvin ME (1999) Structural changes linked to proton translocation by subunit c of the ATP synthase. Nature 402:263-268
    • (1999) Nature , vol.402 , pp. 263-268
    • Rastogi, V.K.1    Girvin, M.E.2
  • 57
    • 0028931922 scopus 로고
    • In vivo assembly of rhodopsin from expressed polypeptide fragments
    • Ridge KD, Lee SS, Yao LL (1995) In vivo assembly of rhodopsin from expressed polypeptide fragments. Proc Natl Acad Sci USA 92:3204-3208
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 3204-3208
    • Ridge, K.D.1    Lee, S.S.2    Yao, L.L.3
  • 59
    • 0032506009 scopus 로고    scopus 로고
    • TROSY in triple-resonance experiments: New perspectives for sequential NMR assignment of large proteins
    • Salzmann M, Pervushin K, Wider G, Senn H, Wüthrich K (1998) TROSY in triple-resonance experiments: New perspectives for sequential NMR assignment of large proteins. Proc Natl Acad Sci USA 95:13585-13590
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 13585-13590
    • Salzmann, M.1    Pervushin, K.2    Wider, G.3    Senn, H.4    Wüthrich, K.5
  • 60
    • 0033518575 scopus 로고    scopus 로고
    • TROSY-type triple-resonance experiments for sequential NMR assignments of large proteins
    • Salzmann M, Wider G, Pervushin K, Senn H, Wüthrich K (1999) TROSY-type triple-resonance experiments for sequential NMR assignments of large proteins. J Am Chem Soc 121:844-848
    • (1999) J Am Chem Soc , vol.121 , pp. 844-848
    • Salzmann, M.1    Wider, G.2    Pervushin, K.3    Senn, H.4    Wüthrich, K.5
  • 61
    • 0034707084 scopus 로고    scopus 로고
    • Customizing model membranes and samples for NMR spectroscopic studies of complex membrane proteins
    • Sanders CR, Oxenoid K (2000) Customizing model membranes and samples for NMR spectroscopic studies of complex membrane proteins. Biochim Biophys Acta 1508:129-145
    • (2000) Biochim Biophys Acta , vol.1508 , pp. 129-145
    • Sanders, C.R.1    Oxenoid, K.2
  • 62
    • 33746217557 scopus 로고    scopus 로고
    • Solution NMR of membrane proteins: Practice and challenges
    • Sanders CR, Sönnichsen F (2006) Solution NMR of membrane proteins: practice and challenges. Magn Reson Chem 44:S24-S40
    • (2006) Magn Reson Chem , vol.44
    • Sanders, C.R.1    Sönnichsen, F.2
  • 64
    • 0041876269 scopus 로고    scopus 로고
    • Heterologous expression of G-protein-coupled receptors: Comparison of expression systems fron the standpoint of large-scale production and purification
    • Sarramegna V, Talmont F, Demange P, Milon A (2003) Heterologous expression of G-protein-coupled receptors: Comparison of expression systems fron the standpoint of large-scale production and purification. Cell Mol Life Sci 60:1529-1546
    • (2003) Cell Mol Life Sci , vol.60 , pp. 1529-1546
    • Sarramegna, V.1    Talmont, F.2    Demange, P.3    Milon, A.4
  • 65
    • 33745293916 scopus 로고    scopus 로고
    • Recombinant G protein-coupled receptors from expression to renaturation: A challenge towards structure
    • Sarramegn V, Muller I, Milon A, Talmont F (2006) Recombinant G protein-coupled receptors from expression to renaturation: A challenge towards structure. Cell Mol Life Sci 63:1149-1164
    • (2006) Cell Mol Life Sci , vol.63 , pp. 1149-1164
    • Sarramegn, V.1    Muller, I.2    Milon, A.3    Talmont, F.4
  • 66
    • 0037020298 scopus 로고    scopus 로고
    • Heteronuclear multidimensional NMR spectroscopy of solubilized membrane proteins: Resonance assignment of native bacteriorhodopsin
    • Schubert M, Kolbe M, Kessler B, Oesterhelt D, Schmieder P (2002) Heteronuclear multidimensional NMR spectroscopy of solubilized membrane proteins: Resonance assignment of native bacteriorhodopsin. ChemBioChem 3:1019-1023
    • (2002) ChemBioChem , vol.3 , pp. 1019-1023
    • Schubert, M.1    Kolbe, M.2    Kessler, B.3    Oesterhelt, D.4    Schmieder, P.5
  • 67
    • 0029934934 scopus 로고    scopus 로고
    • Assignment of N-15, C-13(alpha), C-13(beta), and HN resonances in an N-15, C-13, H-2 labeled 64 kDa trp repressor-operator complex using triple-resonance NMR spectroscopy and H-2-decoupling
    • Shan X, Gardner K, Muhandiram D, Rao NS, Arrowsmith C, Kay LE (1996) Assignment of N-15, C-13(alpha), C-13(beta), and HN resonances in an N-15, C-13, H-2 labeled 64 kDa trp repressor-operator complex using triple-resonance NMR spectroscopy and H-2-decoupling. J Am Chem Soc 118:6570-6579
    • (1996) J Am Chem Soc , vol.118 , pp. 6570-6579
    • Shan, X.1    Gardner, K.2    Muhandiram, D.3    Rao, N.S.4    Arrowsmith, C.5    Kay, L.E.6
  • 68
    • 0034213573 scopus 로고    scopus 로고
    • Do more complex organisms have a greater proportion of membrane proteins in their genomes?
    • Stevens TJ, Arkin IT (2000) Do more complex organisms have a greater proportion of membrane proteins in their genomes? Proteins 39:417-420
    • (2000) Proteins , vol.39 , pp. 417-420
    • Stevens, T.J.1    Arkin, I.T.2
  • 70
    • 35348847305 scopus 로고    scopus 로고
    • Preparation, functional characterization, and NMR studies of human KCNE1, a voltage-gated potassium channel accessory subunit associated with deafness and long QT syndrome
    • Tian C, Vanoye CG, Kang C, Welch RC, Kim HJ, George AL, Sanders CR (2007) Preparation, functional characterization, and NMR studies of human KCNE1, a voltage-gated potassium channel accessory subunit associated with deafness and long QT syndrome. Biochemistry 46:11459-11472
    • (2007) Biochemistry , vol.46 , pp. 11459-11472
    • Tian, C.1    Vanoye, C.G.2    Kang, C.3    Welch, R.C.4    Kim, H.J.5    George, A.L.6    Sanders, C.R.7
  • 72
    • 0031112791 scopus 로고    scopus 로고
    • Isotropic solutions of phospholipid bicelles-a new membrane mimetic for high-resolution NMR studies of polypeptides
    • Vold RR, Prosser RS, Deese AJ (1997) Isotropic solutions of phospholipid bicelles-a new membrane mimetic for high-resolution NMR studies of polypeptides. J Biomol NMR 9:329-335
    • (1997) J Biomol NMR , vol.9 , pp. 329-335
    • Vold, R.R.1    Prosser, R.S.2    Deese, A.J.3
  • 74
    • 33749987003 scopus 로고    scopus 로고
    • Optimization of the human adenosine A2a receptor yields in Saccharomyces cerevisiae
    • Wedekind A, O'malley MA, Niebauer RT, Robinson AS (2006) Optimization of the human adenosine A2a receptor yields in Saccharomyces cerevisiae. Biotechnol Prog 22:1249-1255
    • (2006) Biotechnol Prog , vol.22 , pp. 1249-1255
    • Wedekind, A.1    O'malley, M.A.2    Niebauer, R.T.3    Robinson, A.S.4
  • 75
    • 0032556228 scopus 로고    scopus 로고
    • Single scan, sensitivity- and gradient-enhanced TROSY for multidimensional NMR experiments
    • Weigelt J (1998) Single scan, sensitivity- and gradient-enhanced TROSY for multidimensional NMR experiments. J Am Chem Soc 120:10778-10779
    • (1998) J Am Chem Soc , vol.120 , pp. 10778-10779
    • Weigelt, J.1
  • 76
    • 37849009111 scopus 로고    scopus 로고
    • Isotope labeling of mammalian GPCRs in HEK293 cells and characterization of the C-terminus of bovine rhodopsin by high resolution liquid NMR spectroscopy
    • Werner K, Richter C, Klein-Seetharaman J, Schwalbe H (2008) Isotope labeling of mammalian GPCRs in HEK293 cells and characterization of the C-terminus of bovine rhodopsin by high resolution liquid NMR spectroscopy. J Biomol NMR 40:49-53
    • (2008) J Biomol NMR , vol.40 , pp. 49-53
    • Werner, K.1    Richter, C.2    Klein-Seetharaman, J.3    Schwalbe, H.4
  • 77
    • 0032987478 scopus 로고    scopus 로고
    • Membrane protein folding and stability: Physical principles
    • White SH, Wimley WC (1999) Membrane protein folding and stability: physical principles. Annu Rev Biophys Biomol Struct 28:319-365
    • (1999) Annu Rev Biophys Biomol Struct , vol.28 , pp. 319-365
    • White, S.H.1    Wimley, W.C.2
  • 78
    • 0028393784 scopus 로고
    • The 13C chemical-shift index: A simple method for the identification of protein secondary structure using 13 C chemical-shift data
    • Wishart DS, Sykes BD (1994) The 13C chemical-shift index: A simple method for the identification of protein secondary structure using 13 C chemical-shift data. J Biomol NMR 4:171-180
    • (1994) J Biomol NMR , vol.4 , pp. 171-180
    • Wishart, D.S.1    Sykes, B.D.2
  • 79
    • 0026410969 scopus 로고
    • Relationship between nuclear magnetic resonance chemical shift and protein secondary structure
    • Wishart D, Sykes B, Richards F (1991) Relationship between nuclear magnetic resonance chemical shift and protein secondary structure. J Mol Biol 222:311-333
    • (1991) J Mol Biol , vol.222 , pp. 311-333
    • Wishart, D.1    Sykes, B.2    Richards, F.3
  • 80
    • 43949167657 scopus 로고
    • HNCACB, a high-sensitivity 3D NMR experiment to correlate amide-proton and nitrogen resonances with the alpha-carbon and beta-carbon resonances in proteins
    • Wittekind M, Mueller L (1993) HNCACB, a high-sensitivity 3D NMR experiment to correlate amide-proton and nitrogen resonances with the alpha-carbon and beta-carbon resonances in proteins. J Magn Reson Ser B 101:201-205
    • (1993) J Magn Reson Ser B , vol.101 , pp. 201-205
    • Wittekind, M.1    Mueller, L.2
  • 81
    • 0028122679 scopus 로고
    • Construction and in vivo analysis of new split lactose permeases
    • Wrubel W, Stochaj U, Ehring R (1994) Construction and in vivo analysis of new split lactose permeases. FEBS Lett 349:433-438
    • (1994) FEBS Lett , vol.349 , pp. 433-438
    • Wrubel, W.1    Stochaj, U.2    Ehring, R.3
  • 82
    • 0028578764 scopus 로고
    • A suite of triple-resonance NMR experiments for the backbone assignment of N-15, C-13, H2-labeled proteins with high sensitivity
    • Yamazaki T, Lee W, Arrowsmith C, Muhandiram D, Kay LE (1994) A suite of triple-resonance NMR experiments for the backbone assignment of N-15, C-13, H2-labeled proteins with high sensitivity. J Am Chem Soc 116:11655-11666
    • (1994) J Am Chem Soc , vol.116 , pp. 11655-11666
    • Yamazaki, T.1    Lee, W.2    Arrowsmith, C.3    Muhandiram, D.4    Kay, L.E.5
  • 85
    • 33748363914 scopus 로고    scopus 로고
    • A transmembrane helix-bundle from G-protein coupled receptor CB2: Biosynthesis, purification, and NMR characterization
    • Zheng H, Zhao J, Sheng W, Xie XQ (2006) A transmembrane helix-bundle from G-protein coupled receptor CB2: Biosynthesis, purification, and NMR characterization. Biopolymers 83:46-61
    • (2006) Biopolymers , vol.83 , pp. 46-61
    • Zheng, H.1    Zhao, J.2    Sheng, W.3    Xie, X.Q.4
  • 86
  • 87
    • 54349118443 scopus 로고    scopus 로고
    • Studies of the structure of the N-terminal domain from the Y4 receptor, a G-protein coupled receptor, and its interaction with hormones from the NPY family
    • Zou C, Kumaran S, Markovic S, Walser R, Zerbe O (2008) Studies of the structure of the N-terminal domain from the Y4 receptor, a G-protein coupled receptor, and its interaction with hormones from the NPY family. ChemBioChem 9:2276-2284
    • (2008) ChemBioChem , vol.9 , pp. 2276-2284
    • Zou, C.1    Kumaran, S.2    Markovic, S.3    Walser, R.4    Zerbe, O.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.