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Volumn 105, Issue 24, 2008, Pages 8262-8267

Transmembrane segment enhanced labeling as a tool for the backbone assignment of α-helical membrane proteins

Author keywords

Cell free expression; NMR; Peak overlap; Protein structure analysis; Stable isotope labeling

Indexed keywords

AMINO ACID; CARBON 13; MEMBRANE PROTEIN; NITROGEN 15;

EID: 46149100051     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0710843105     Document Type: Article
Times cited : (31)

References (27)
  • 1
    • 0024297305 scopus 로고
    • A continuous cell-free translation system capable of producing polypeptides in high yield
    • Spirin AS, Baranov VI, Ryabova LA, Ovodov SY, Alakhov YB (1988) A continuous cell-free translation system capable of producing polypeptides in high yield. Science 242:1162-1164.
    • (1988) Science , vol.242 , pp. 1162-1164
    • Spirin, A.S.1    Baranov, V.I.2    Ryabova, L.A.3    Ovodov, S.Y.4    Alakhov, Y.B.5
  • 2
    • 0029365773 scopus 로고
    • Cell-free synthesis and amino acid-selective stable isotope labeling of proteins for NMR analysis
    • Kigawa T, Muto Y, Yokoyama S (1995) Cell-free synthesis and amino acid-selective stable isotope labeling of proteins for NMR analysis. J Biomol NMR 6:129-134.
    • (1995) J Biomol NMR , vol.6 , pp. 129-134
    • Kigawa, T.1    Muto, Y.2    Yokoyama, S.3
  • 3
    • 27444447384 scopus 로고    scopus 로고
    • Cell-free synthesis of 15N-labeled proteins for NMR studies
    • Ozawa K, Dixon NE, Otting G (2005) Cell-free synthesis of 15N-labeled proteins for NMR studies. IUBMB Life 57:615-622.
    • (2005) IUBMB Life , vol.57 , pp. 615-622
    • Ozawa, K.1    Dixon, N.E.2    Otting, G.3
  • 4
    • 0842265773 scopus 로고    scopus 로고
    • High level cell-free expression and specific labeling of integral membrane proteins
    • Klammt C, et al. (2004) High level cell-free expression and specific labeling of integral membrane proteins. Eur J Biochem 271:568-580.
    • (2004) Eur J Biochem , vol.271 , pp. 568-580
    • Klammt, C.1
  • 5
    • 28244458078 scopus 로고    scopus 로고
    • Evaluation of detergents for the soluble expression of alpha-helical and beta-barrel-type integral membrane proteins by a preparative scale individual cell-free expression system
    • Klammt C, et al. (2005) Evaluation of detergents for the soluble expression of alpha-helical and beta-barrel-type integral membrane proteins by a preparative scale individual cell-free expression system. FEBS J 272:6024-6038.
    • (2005) FEBS J , vol.272 , pp. 6024-6038
    • Klammt, C.1
  • 6
    • 33748307399 scopus 로고    scopus 로고
    • Cell-free expression as an emerging technique for the large scale production of integral membrane protein
    • Klammt C, et al. (2006) Cell-free expression as an emerging technique for the large scale production of integral membrane protein. FEBS J 273:4141-4153.
    • (2006) FEBS J , vol.273 , pp. 4141-4153
    • Klammt, C.1
  • 7
    • 15744391469 scopus 로고    scopus 로고
    • Expression of G protein coupled receptors in a cell-free translational system using detergents and thioredoxin-fusion vectors
    • Ishihara G, et al. (2005) Expression of G protein coupled receptors in a cell-free translational system using detergents and thioredoxin-fusion vectors. Protein Expression Purif 41:27-37.
    • (2005) Protein Expression Purif , vol.41 , pp. 27-37
    • Ishihara, G.1
  • 8
    • 4744351698 scopus 로고    scopus 로고
    • Cell-free synthesis of a functional ion channel in the absence of a membrane and in the presence of detergent
    • Berrier C, et al. (2004) Cell-free synthesis of a functional ion channel in the absence of a membrane and in the presence of detergent. Biochemistry 43:12585-12591.
    • (2004) Biochemistry , vol.43 , pp. 12585-12591
    • Berrier, C.1
  • 9
    • 37649009221 scopus 로고    scopus 로고
    • X-ray structure of EmrE supports dual topology model
    • Chen YJ, et al. (2007) X-ray structure of EmrE supports dual topology model. Proc Natl Acad Sci USA 104:18999-19004.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 18999-19004
    • Chen, Y.J.1
  • 10
    • 39749126981 scopus 로고    scopus 로고
    • GPCR Proteomics: Mass spectrometric and functional analysis of histamine H1 receptor after baculovirus-driven and in vitro cell free expression
    • Sansuk K, et al. (2008) GPCR Proteomics: Mass spectrometric and functional analysis of histamine H1 receptor after baculovirus-driven and in vitro cell free expression. J Proteome Res 7:621-629.
    • (2008) J Proteome Res , vol.7 , pp. 621-629
    • Sansuk, K.1
  • 11
    • 42049096315 scopus 로고    scopus 로고
    • Cell free-expression and functional reconstitution of eucaryotic drug transporters
    • Keller T, et al. (2008) Cell free-expression and functional reconstitution of eucaryotic drug transporters. Biochemistry, 47:4552-4564.
    • (2008) Biochemistry , vol.47 , pp. 4552-4564
    • Keller, T.1
  • 13
    • 25844528201 scopus 로고    scopus 로고
    • Efficient strategy for the rapid backbone assignment of membrane proteins
    • Trbovic N, et al. (2005) Efficient strategy for the rapid backbone assignment of membrane proteins. J Am Chem Soc 127:13504-13505.
    • (2005) J Am Chem Soc , vol.127 , pp. 13504-13505
    • Trbovic, N.1
  • 14
    • 85164044831 scopus 로고    scopus 로고
    • Koglin A, et al. (2006) Combination of cell-free expression and NMR spectroscopy as a new approach for structural investigation of membrane proteins. Magn Reson Chem 44(Spec No):S17-S23.
    • Koglin A, et al. (2006) Combination of cell-free expression and NMR spectroscopy as a new approach for structural investigation of membrane proteins. Magn Reson Chem 44(Spec No):S17-S23.
  • 15
    • 1242272915 scopus 로고    scopus 로고
    • Protein signal assignments using specific labeling and cell-free synthesis
    • Shi J, Pelton JG, Cho HS, Wemmer DE (2004) Protein signal assignments using specific labeling and cell-free synthesis. J Biomol NMR 28:235-247.
    • (2004) J Biomol NMR , vol.28 , pp. 235-247
    • Shi, J.1    Pelton, J.G.2    Cho, H.S.3    Wemmer, D.E.4
  • 16
    • 1942489643 scopus 로고    scopus 로고
    • A combinatorial selective labeling method for the assignment of backbone amide NMR resonances
    • Parker MJ, Aulton-Jones M, Hounslow AM, Craven CJ (2004) A combinatorial selective labeling method for the assignment of backbone amide NMR resonances. J Am Chem Soc 126:5020-5021.
    • (2004) J Am Chem Soc , vol.126 , pp. 5020-5021
    • Parker, M.J.1    Aulton-Jones, M.2    Hounslow, A.M.3    Craven, C.J.4
  • 17
    • 0020406958 scopus 로고
    • Assignment of the three methionyl carbonyl carbon resonances in Streptomyces subtilisin inhibitor by a carbon-13 and nitrogen-15 double-labeling technique. A new strategy for structural studies of proteins in solution
    • Kainosho M, Tsuji T (1982) Assignment of the three methionyl carbonyl carbon resonances in Streptomyces subtilisin inhibitor by a carbon-13 and nitrogen-15 double-labeling technique. A new strategy for structural studies of proteins in solution. Biochemistry 21:6273-6279.
    • (1982) Biochemistry , vol.21 , pp. 6273-6279
    • Kainosho, M.1    Tsuji, T.2
  • 18
    • 0034711958 scopus 로고    scopus 로고
    • Statistical analysis of amino acid patterns in transmembrane helices: The GxxxG motif occurs frequently and in association with beta-branched residues at neighboring positions
    • Senes A, Gerstein M, Engelman DM (2000) Statistical analysis of amino acid patterns in transmembrane helices: The GxxxG motif occurs frequently and in association with beta-branched residues at neighboring positions. J Mol Biol 296:921-936.
    • (2000) J Mol Biol , vol.296 , pp. 921-936
    • Senes, A.1    Gerstein, M.2    Engelman, D.M.3
  • 19
    • 34547560098 scopus 로고    scopus 로고
    • Crystal structure of inhibitor-bound human 5-lipoxygenase-activating protein
    • Ferguson AD, McKeever BM, Xu S, Wisniewski D, Miller DK, et al. (2007) Crystal structure of inhibitor-bound human 5-lipoxygenase-activating protein. Science 317:510-512.
    • (2007) Science , vol.317 , pp. 510-512
    • Ferguson, A.D.1    McKeever, B.M.2    Xu, S.3    Wisniewski, D.4    Miller, D.K.5
  • 20
    • 1242340504 scopus 로고    scopus 로고
    • An evaluation of detergents for NMR structural studies of membrane proteins
    • Krueger-Koplin RD, et al. (2004) An evaluation of detergents for NMR structural studies of membrane proteins. J Biomol NMR 28:43-57.
    • (2004) J Biomol NMR , vol.28 , pp. 43-57
    • Krueger-Koplin, R.D.1
  • 22
  • 23
    • 33645504750 scopus 로고    scopus 로고
    • NMR study of the tetrameric KcsA potassium channel in detergent micelles
    • Chill JH, Louis JM, Miller C, Bax A (2006) NMR study of the tetrameric KcsA potassium channel in detergent micelles. Protein Sci 15:684-698.
    • (2006) Protein Sci , vol.15 , pp. 684-698
    • Chill, J.H.1    Louis, J.M.2    Miller, C.3    Bax, A.4
  • 24
    • 3242655534 scopus 로고    scopus 로고
    • Membrane protein-lipid interactions in mixed micelles studied by NMR spectroscopy with the use of paramagnetic reagents
    • Hilty C, Wider G, Fernandez C, Wüthrich K (2004) Membrane protein-lipid interactions in mixed micelles studied by NMR spectroscopy with the use of paramagnetic reagents. ChemBioChem 5:467-473.
    • (2004) ChemBioChem , vol.5 , pp. 467-473
    • Hilty, C.1    Wider, G.2    Fernandez, C.3    Wüthrich, K.4
  • 25
    • 28844480494 scopus 로고    scopus 로고
    • Effective rotational correlation times of proteins from NMR relaxation interference
    • Lee D, Hilty C, Wider G, Wüthrich K (2006) Effective rotational correlation times of proteins from NMR relaxation interference. J Magn Reson 178:72-76.
    • (2006) J Magn Reson , vol.178 , pp. 72-76
    • Lee, D.1    Hilty, C.2    Wider, G.3    Wüthrich, K.4
  • 26
    • 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
  • 27
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.