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Volumn 992, Issue , 2012, Pages 95-118

Amino acid selective labeling and unlabeling for protein resonance assignments

Author keywords

[No Author keywords available]

Indexed keywords

CARBON 13; GLUTAMIC ACID; ISOLEUCINE; LEUCINE; NITROGEN 15; VALINE;

EID: 84904224974     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-94-007-4954-2_6     Document Type: Article
Times cited : (29)

References (40)
  • 3
    • 4744357287 scopus 로고    scopus 로고
    • Structural and dynamic studies of proteins by solid-state NMR spectroscopy: Rapid movement forward
    • McDermott AE (2004) Structural and dynamic studies of proteins by solid-state NMR spectroscopy: Rapid movement forward. Curr Opin Struct Biol 14:554-561
    • (2004) Curr Opin Struct Biol , vol.14 , pp. 554-561
    • McDermott, A.E.1
  • 4
    • 0031764019 scopus 로고    scopus 로고
    • NMR structural studies of membrane proteins
    • Marassi F, Opella SJ (1998) NMR structural studies of membrane proteins. Curr Opin Struct Biol 8:640-648
    • (1998) Curr Opin Struct Biol , vol.8 , pp. 640-648
    • Marassi, F.1    Opella, S.J.2
  • 5
    • 33746217557 scopus 로고    scopus 로고
    • Solution NMR of membrane proteins: Practice and challenges
    • Sanders CR, Sonnichsen FD (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    Sonnichsen, F.D.2
  • 6
    • 0031851978 scopus 로고    scopus 로고
    • Equilibrium NMR studies of unfolded and partially folded proteins
    • Dyson HJ, Wright PE (1998) Equilibrium NMR studies of unfolded and partially folded proteins. Nat Struct Biol 5:499-503
    • (1998) Nat Struct Biol , vol.5 , pp. 499-503
    • Dyson, H.J.1    Wright, P.E.2
  • 7
    • 0014424848 scopus 로고
    • High resolution nuclear magnetic resonance spectra of selectively deuterated staphylococcal nuclease
    • Markley JL, Putter I, Jardetzky O (1968) High resolution nuclear magnetic resonance spectra of selectively deuterated staphylococcal nuclease. Science 161:1249-1251
    • (1968) Science , vol.161 , pp. 1249-1251
    • Markley, J.L.1    Putter, I.2    Jardetzky, O.3
  • 8
    • 0024836418 scopus 로고
    • Expression and nitrogen-15 labelling of proteins for proton and nitrogen-15 nuclear magnetic resonance
    • Muchmore DD, McIntosh LP, Russell CB, Anderson DE, Dahlquist FW (1989) Expression and nitrogen-15 labelling of proteins for proton and nitrogen-15 nuclear magnetic resonance. Methods Enzymol 177:44-73
    • (1989) Methods Enzymol , vol.177 , pp. 44-73
    • Muchmore, D.D.1    McIntosh, L.P.2    Russell, C.B.3    Anderson, D.E.4    Dahlquist, F.W.5
  • 9
    • 0025193295 scopus 로고
    • Biosynthetic incorporation of 15 N and 13 C for assignment and interpretation of nuclear magnetic resonance spectra of proteins
    • McIntosh LP, Dahlquist FW (1990) Biosynthetic incorporation of 15 N and 13 C for assignment and interpretation of nuclear magnetic resonance spectra of proteins. Q Rev Biophys 23:1-38
    • (1990) Q Rev Biophys , vol.23 , pp. 1-38
    • McIntosh, L.P.1    Dahlquist, F.W.2
  • 10
    • 0030192067 scopus 로고    scopus 로고
    • Amino-acid type identi fi cation for deuterated proteins with a b-carbon edited HNCOCACB experiment
    • Dötsch V, Matsuo H, Wagner G (1996) Amino-acid type identi fi cation for deuterated proteins with a b-carbon edited HNCOCACB experiment. J Magn Reson B 112:95-100
    • (1996) J Magn Reson B , vol.112 , pp. 95-100
    • Dötsch, V.1    Matsuo, H.2    Wagner, G.3
  • 11
    • 0029687651 scopus 로고    scopus 로고
    • Amino acid type selective triple resonance experiments
    • Dötsch V, Oswald RE, Wagner G (1996) Amino acid type selective triple resonance experiments. J Magn Reson B 110:107-111
    • (1996) J Magn Reson B , vol.110 , pp. 107-111
    • Dötsch, V.1    Oswald, R.E.2    Wagner, G.3
  • 12
    • 0030161508 scopus 로고    scopus 로고
    • Editing of amino acid type in CBCA(CO)NH experiments based on the 13 C b - 13 C g coupling
    • Dötsch V, Wagner G (1996) Editing of amino acid type in CBCA(CO)NH experiments based on the 13 C b - 13 C g coupling. J Magn Reson B 111:310-313
    • (1996) J Magn Reson B , vol.111 , pp. 310-313
    • Dötsch, V.1    Wagner, G.2
  • 13
    • 0002086987 scopus 로고    scopus 로고
    • MUSIC in triple-resonance experiments: Amino acid type-selective 15 N/ 1 H correlations
    • Schubert M, Schmalla M, Schmeider P, Oschkinat H (1999) MUSIC in triple-resonance experiments: Amino acid type-selective 15 N/ 1 H correlations. J Magn Reson 141:34-43
    • (1999) J Magn Reson , vol.141 , pp. 34-43
    • Schubert, M.1    Schmalla, M.2    Schmeider, P.3    Oschkinat, H.4
  • 14
    • 0035742302 scopus 로고    scopus 로고
    • MUSIC and aromatic residues: Amino acid type-selective backbone 15 N/ 1 H correlations, part III
    • Schubert M, Oschkinat H, Schmeider P (2001) MUSIC and aromatic residues: Amino acid type-selective backbone 15 N/ 1 H correlations, part III. J Magn Reson 153:186-192
    • (2001) J Magn Reson , vol.153 , pp. 186-192
    • Schubert, M.1    Oschkinat, H.2    Schmeider, P.3
  • 15
    • 0034852448 scopus 로고    scopus 로고
    • Amino acid type-selective backbone 15 N/ 1 H correlations for Arg and Lys
    • Schubert M, Oschkinat H, Schmeider P (2001) Amino acid type-selective backbone 15 N/ 1 H correlations for Arg and Lys. J Biomol NMR 20:379-384
    • (2001) J Biomol NMR , vol.20 , pp. 379-384
    • Schubert, M.1    Oschkinat, H.2    Schmeider, P.3
  • 16
    • 0035744056 scopus 로고    scopus 로고
    • MUSIC selective pulses and tuned amino acid type-selective 15 N/ 1 H correlations, part II
    • Schubert M, Oschkinat H, Schmeider P (2001) MUSIC, selective pulses and tuned amino acid type-selective 15 N/ 1 H correlations, part II. J Magn Reson 148:61-72
    • (2001) J Magn Reson , vol.148 , pp. 61-72
    • Schubert, M.1    Oschkinat, H.2    Schmeider, P.3
  • 17
    • 15844367467 scopus 로고    scopus 로고
    • A modi fi ed strategy for sequence speci fi c assignment of protein NMR spectra based on amino acid type selective experiments
    • Schubert M, Labudde D, Leitner D, Oschkinat H, Schmeider P (2005) A modi fi ed strategy for sequence speci fi c assignment of protein NMR spectra based on amino acid type selective experiments. J Biomol NMR 31:115-128
    • (2005) J Biomol NMR , vol.31 , pp. 115-128
    • Schubert, M.1    Labudde, D.2    Leitner, D.3    Oschkinat, H.4    Schmeider, P.5
  • 18
    • 50349088784 scopus 로고    scopus 로고
    • Identification of C-terminal neighbours of amino acid residues without an aliphatic C-13(gamma) as an aid to NMR assignments in proteins
    • Barnwal RP, Rout AK, Atreya HS, Chary KVR (2008) Identi fi cation of C-terminal neighbours of amino acid residues without an aliphatic C-13(gamma) as an aid to NMR assignments in proteins. J Biomol NMR 41:191-197
    • (2008) J Biomol NMR , vol.41 , pp. 191-197
    • Barnwal, R.P.1    Rout, A.K.2    Atreya, H.S.3    Chary, K.V.R.4
  • 19
    • 0033794450 scopus 로고    scopus 로고
    • New developments in isotope labeling strategies for protein solution NMR spectroscopy
    • Goto NK, Kay LE (2000) New developments in isotope labeling strategies for protein solution NMR spectroscopy. Curr Opin Struct Biol 10:585-592
    • (2000) Curr Opin Struct Biol , vol.10 , pp. 585-592
    • Goto, N.K.1    Kay, L.E.2
  • 20
    • 50249161939 scopus 로고    scopus 로고
    • Stable isotope labeling methods for protein NMR
    • Ohki S, Kainosho M (2008) Stable isotope labeling methods for protein NMR. Prog NMR Spectrosc 53:208-226
    • (2008) Prog NMR Spectrosc , vol.53 , pp. 208-226
    • Ohki, S.1    Kainosho, M.2
  • 21
    • 0028504129 scopus 로고
    • Assignment of amino acid type in 1 H- 15 N correlation spectra by labeling with 14 N-amino acids
    • Shortle D (1994) Assignment of amino acid type in 1 H- 15 N correlation spectra by labeling with 14 N-amino acids. J Magn Reson B105:88-90
    • (1994) J Magn Reson , vol.B105 , pp. 88-90
    • Shortle, D.1
  • 22
    • 0028152571 scopus 로고
    • 2D and 3D NMR-study of phenylalanine residues in proteins by reverse isotopic labeling
    • Vuister GW, Kim SJ, Wu C, Bax A (1994) 2D and 3D NMR-study of phenylalanine residues in proteins by reverse isotopic labeling. J Am Chem Soc 116:9206-9210
    • (1994) J Am Chem Soc , vol.116 , pp. 9206-9210
    • Vuister, G.W.1    Kim, S.J.2    Wu, C.3    Bax, A.4
  • 23
    • 0042705330 scopus 로고    scopus 로고
    • Amino acid selective 'unlabelling' for residue-speci fi c NMR assignments in proteins
    • Atreya HS, Chary KVR (2000) Amino acid selective 'unlabelling' for residue-speci fi c NMR assignments in proteins. Curr Sci 79:504-507
    • (2000) Curr Sci , vol.79 , pp. 504-507
    • Atreya, H.S.1    Chary, K.V.R.2
  • 24
    • 0035072251 scopus 로고    scopus 로고
    • Selective 'unlabeling' of amino acids in fractionally C-13 labeled proteins: An approach for stereospeci fi c NMR assignments of CH3 groups in Val and Leu residues
    • Atreya HS, Chary KVR (2001) Selective 'unlabeling' of amino acids in fractionally C-13 labeled proteins: An approach for stereospeci fi c NMR assignments of CH3 groups in Val and Leu residues. J Biomol NMR 19:267-272
    • (2001) J Biomol NMR , vol.19 , pp. 267-272
    • Atreya, H.S.1    Chary, K.V.R.2
  • 25
    • 79951554115 scopus 로고    scopus 로고
    • Amino acid selective unlabeling for sequence speci fi c resonance assignments in proteins
    • Krishnarjuna B, Jaipuria G, Thakur A, D'Silva P, Atreya HS (2011) Amino acid selective unlabeling for sequence speci fi c resonance assignments in proteins. J Biomol NMR 49:39-51
    • (2011) J Biomol NMR , vol.49 , pp. 39-51
    • Krishnarjuna, B.1    Jaipuria, G.2    Thakur, A.3    D'Silva, P.4    Atreya, H.S.5
  • 27
    • 49649111497 scopus 로고    scopus 로고
    • Cell-free protein synthesis for analysis by NMR spectroscopy
    • Apponyi MA, Ozawa K, Dixon NE, Otting G (2008) Cell-free protein synthesis for analysis by NMR spectroscopy. Methods Mol Biol 426:257-268
    • (2008) Methods Mol Biol , vol.426 , pp. 257-268
    • Apponyi, M.A.1    Ozawa, K.2    Dixon, N.E.3    Otting, G.4
  • 28
    • 3943074512 scopus 로고    scopus 로고
    • Nuclear magnetic resonance spectroscopy of high-molecular-weight proteins
    • Tugarinov V, Hwang PM, Kay LE (2004) Nuclear magnetic resonance spectroscopy of high-molecular-weight proteins. Annu Rev Biochem 73:107-146
    • (2004) Annu Rev Biochem , vol.73 , pp. 107-146
    • Tugarinov, V.1    Hwang, P.M.2    Kay, L.E.3
  • 29
    • 1242308875 scopus 로고    scopus 로고
    • An isotope labeling strategy for methyl TROSY spectroscopy
    • Tugarinov V, Kay LE (2004) An isotope labeling strategy for methyl TROSY spectroscopy. J Biomol NMR 28:165-172
    • (2004) J Biomol NMR , vol.28 , pp. 165-172
    • Tugarinov, V.1    Kay, L.E.2
  • 30
    • 13944274948 scopus 로고    scopus 로고
    • The past, present and future of cell-free protein synthesis
    • Katzen F, Chang G, Kudlicki W (2005) The past, present and future of cell-free protein synthesis. Trends Biotechnol 23:150-156
    • (2005) Trends Biotechnol , vol.23 , pp. 150-156
    • Katzen, F.1    Chang, G.2    Kudlicki, W.3
  • 32
    • 0033121307 scopus 로고    scopus 로고
    • Selective and extensive 13 C labeling of a membrane protein for solid-state NMR investigation
    • Hong M, Jakes K (1999) Selective and extensive 13 C labeling of a membrane protein for solid-state NMR investigation. J Biomol NMR 14:71-74
    • (1999) J Biomol NMR , vol.14 , pp. 71-74
    • Hong, M.1    Jakes, K.2
  • 33
    • 0033136436 scopus 로고    scopus 로고
    • Application of amino acid type-speci fi c 1H and 14N labeling in a 2H-, 15N-labeled background to a 47 kDa homodimer: Potential for NMR structure determination of large proteins
    • Kelly MJS, Krieger C, Ball LJ, Yu Y, Richter G, Schmieder P, Bacher A, Oschkinat H (1999) Application of amino acid type-speci fi c 1H and 14N labeling in a 2H-, 15N-labeled background to a 47 kDa homodimer: Potential for NMR structure determination of large proteins. J Biomol NMR 14:79-83
    • (1999) J Biomol NMR , vol.14 , pp. 79-83
    • Kelly, M.J.S.1    Krieger, C.2    Ball, L.J.3    Yu, Y.4    Richter, G.5    Schmieder, P.6    Bacher, A.7    Oschkinat, H.8
  • 34
    • 78149416435 scopus 로고    scopus 로고
    • High-resolution methyl edited GFT NMR experiments for protein resonance assignments and structure determination
    • Jaipuria G, Thakur A, D'Silva P, Atreya HS (2010) High-resolution methyl edited GFT NMR experiments for protein resonance assignments and structure determination. J Biomol NMR 48:137-145
    • (2010) J Biomol NMR , vol.48 , pp. 137-145
    • Jaipuria, G.1    Thakur, A.2    D'Silva, P.3    Atreya, H.S.4
  • 35
    • 0033121309 scopus 로고    scopus 로고
    • Letter to the editor: Sequence-speci fi c 1 H, 13 C and 15 N assignments of a calcium binding protein from Entamoeba histolytica
    • Sahu SC, Atreya HS, Chauhan S, Bhattacharya A, Chary KVR, Govil G (1999) Letter to the editor: Sequence-speci fi c 1 H, 13 C and 15 N assignments of a calcium binding protein from Entamoeba histolytica. J Biomol NMR 14:93-94
    • (1999) J Biomol NMR , vol.14 , pp. 93-94
    • Sahu, S.C.1    Atreya, H.S.2    Chauhan, S.3    Bhattacharya, A.4    Chary, K.V.R.5    Govil, G.6
  • 36
    • 0035807933 scopus 로고    scopus 로고
    • NMR derived solution structure of an EF-hand calcium-binding protein from Entamoeba histolytica
    • Atreya HS, Sahu SC, Bhattacharya A, Chary KVR, Govil G (2001) NMR derived solution structure of an EF-hand calcium-binding protein from Entamoeba histolytica. Biochemistry 40:14392-14403
    • (2001) Biochemistry , vol.40 , pp. 14392-14403
    • Atreya, H.S.1    Sahu, S.C.2    Bhattacharya, A.3    Chary, K.V.R.4    Govil, G.5
  • 37
    • 0025252231 scopus 로고
    • Heteronuclear fi lters in two-dimensional [1H,1H] NMR spectroscopy: Combined use with isotope labelling for studies of macromolecular conformation and intermolecular interactions
    • Otting G, Wüthrich K (1990) Heteronuclear fi lters in two-dimensional [1H,1H]-NMR spectroscopy: Combined use with isotope labelling for studies of macromolecular conformation and intermolecular interactions. Q Rev Biophys 23:39-96
    • (1990) Q Rev Biophys , vol.23 , pp. 39-96
    • Otting, G.1    Wüthrich, K.2
  • 38
    • 0000112965 scopus 로고    scopus 로고
    • Isotope- fi ltered NMR methds for the study of biomolecular structure and interactions
    • Breeze AL (2000) Isotope- fi ltered NMR methds for the study of biomolecular structure and interactions. Prog NMR Spectrosc 36:323-372
    • (2000) Prog NMR Spectrosc , vol.36 , pp. 323-372
    • Breeze, A.L.1
  • 39
    • 4344648451 scopus 로고    scopus 로고
    • Automated analysis of protein NMR assignments and structures
    • Baran MC, Huang YJ, Moseley HNB, Montelione GT (2004) Automated analysis of protein NMR assignments and structures. Chem Rev 104:3541-3555
    • (2004) Chem Rev , vol.104 , pp. 3541-3555
    • Baran, M.C.1    Huang, Y.J.2    Moseley, H.N.B.3    Montelione, G.T.4
  • 40
    • 84861533498 scopus 로고    scopus 로고
    • Efficient sequential assignments in proteins with reduced dimensionality 3D HN (CA)N.H
    • Chandra K, Jaipuria G, Shet D, Atreya HS (2011) Ef fi cient sequential assignments in proteins with reduced dimensionality 3D HN (CA)NH. J Biomol NMR 52:115-126
    • (2011) J Biomol NMR , vol.52 , pp. 115-126
    • Chandra, K.1    Jaipuria, G.2    Shet, D.3    Atreya, H.S.4


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