메뉴 건너뛰기




Volumn 44, Issue 13, 2005, Pages 5196-5206

NMR structure determination of a membrane protein with two transmembrane helices in micelles: MerF of the bacterial mercury detoxification system

Author keywords

[No Author keywords available]

Indexed keywords

MATHEMATICAL MODELS; MEMBRANES; MERCURY (METAL); MICELLES; NUCLEAR MAGNETIC RESONANCE; POLYPEPTIDES;

EID: 16344376576     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi048095v     Document Type: Article
Times cited : (87)

References (84)
  • 1
    • 4344704702 scopus 로고    scopus 로고
    • Structure determination of membrane proteins by NMR spectroscopy
    • Opella, S. J., and Marassi, F. M. (2004) Structure determination of membrane proteins by NMR spectroscopy, Chem. Rev. 104, 3587-3606.
    • (2004) Chem. Rev. , vol.104 , pp. 3587-3606
    • Opella, S.J.1    Marassi, F.M.2
  • 2
    • 0027360175 scopus 로고
    • High-resolution conformation of gramicidin a in a lipid bilayer by solid-state NMR
    • Ketchem, R. R., Hu, W., and Cross, T. A. (1993) High-resolution conformation of gramicidin a in a lipid bilayer by solid-state NMR, Science 261, 1457-1460.
    • (1993) Science , vol.261 , pp. 1457-1460
    • Ketchem, R.R.1    Hu, W.2    Cross, T.A.3
  • 3
    • 0032919444 scopus 로고    scopus 로고
    • Structures of the m2 channel-lining segments from nicotinic acetylcholine and nmda receptors by NMR spectroscopy
    • Opella, S. J., Marassi, F. M., Gesell, J. J., Valente, A. P., Kim, Y., Oblatt-Montal, M., and Montal, M. (1999) Structures of the m2 channel-lining segments from nicotinic acetylcholine and nmda receptors by NMR spectroscopy, Nat. Struct. Biol. 6, 374-379.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 374-379
    • Opella, S.J.1    Marassi, F.M.2    Gesell, J.J.3    Valente, A.P.4    Kim, Y.5    Oblatt-Montal, M.6    Montal, M.7
  • 4
    • 0034775070 scopus 로고    scopus 로고
    • Structure of the transmembrane region of the m2 protein h(+) channel
    • Wang, J., Kim, S., Kovacs, F., and Cross, T. A. (2001) Structure of the transmembrane region of the m2 protein h(+) channel, Protein Sci. 10, 2241-2250.
    • (2001) Protein Sci. , vol.10 , pp. 2241-2250
    • Wang, J.1    Kim, S.2    Kovacs, F.3    Cross, T.A.4
  • 5
    • 0035813019 scopus 로고    scopus 로고
    • Structure and topology of a peptide segment of the 6th transmembrane domain of the Saccharomyces cerevisae alpha-factor receptor in phospholipid bilayers
    • Valentine, K. G., Liu, S. F., Marassi, F. M., Veglia, G., Opella, S. J., Ding, F. X., Wang, S. H., Arshava, B., Becker, J. M., and Naider, F. (2001) Structure and topology of a peptide segment of the 6th transmembrane domain of the Saccharomyces cerevisae alpha-factor receptor in phospholipid bilayers, Biopolymers 59, 243-256.
    • (2001) Biopolymers , vol.59 , pp. 243-256
    • Valentine, K.G.1    Liu, S.F.2    Marassi, F.M.3    Veglia, G.4    Opella, S.J.5    Ding, F.X.6    Wang, S.H.7    Arshava, B.8    Becker, J.M.9    Naider, F.10
  • 6
    • 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. (2003) Simultaneous assignment and structure determination of a membrane protein from NMR orientational restraints, Protein Sci. 12, 403-411.
    • (2003) Protein Sci. , vol.12 , pp. 403-411
    • Marassi, F.M.1    Opella, S.J.2
  • 7
    • 0141645622 scopus 로고    scopus 로고
    • Three-dimensional structure of the channel-forming trans-membrane domain of virus protein "u" (vpu) from hiv-1
    • Park, S. H., Mrse, A. A., Nevzorov, A. A., Mesleh, M. F., Oblatt-Montal, M., Montal, M., and Opella, S. J. (2003) Three-dimensional structure of the channel-forming trans-membrane domain of virus protein "u" (vpu) from hiv-1, J. Mol. Biol. 333, 409-424.
    • (2003) J. Mol. Biol. , vol.333 , pp. 409-424
    • Park, S.H.1    Mrse, A.A.2    Nevzorov, A.A.3    Mesleh, M.F.4    Oblatt-Montal, M.5    Montal, M.6    Opella, S.J.7
  • 8
    • 0029996040 scopus 로고    scopus 로고
    • Structure and dynamics of bacteriophage ike major coat protein in mpg micelles by solution NMR
    • Williams, K. A., Farrow, N. A., Deber, C. M., and Kay, L. E. (1996) Structure and dynamics of bacteriophage ike major coat protein in mpg micelles by solution NMR, Biochemistry 35, 5145-5157.
    • (1996) Biochemistry , vol.35 , pp. 5145-5157
    • Williams, K.A.1    Farrow, N.A.2    Deber, C.M.3    Kay, L.E.4
  • 9
    • 0031577283 scopus 로고    scopus 로고
    • Fd coat protein structure in membrane environments: Structural dynamics of the loop between the hydrophobic trans-membrane helix and the amphipathic in-plane helix
    • Almeida, F. C., and Opella, S. J. (1997) Fd coat protein structure in membrane environments: Structural dynamics of the loop between the hydrophobic trans-membrane helix and the amphipathic in-plane helix, J. Mol. Biol. 270, 481-495.
    • (1997) J. Mol. Biol. , vol.270 , pp. 481-495
    • Almeida, F.C.1    Opella, S.J.2
  • 10
    • 0030932407 scopus 로고    scopus 로고
    • A transmembrane helix dimer: Structure and implications
    • MacKenzie, K. R., Prestegard, J. H., and Engelman, D. M. (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
  • 11
    • 0032544545 scopus 로고    scopus 로고
    • Solution structure of the m13 major coat protein in detergent micelles: A basis for a model of phage assembly involving specific residues
    • Papavoine, C. H., Christiaans, B. E., Folmer, R. H., Konings, R. N., and Hilbers, C. W. (1998) Solution structure of the m13 major coat protein in detergent micelles: A basis for a model of phage assembly involving specific residues, J. Mol. Biol. 282, 401-419.
    • (1998) J. Mol. Biol. , vol.282 , pp. 401-419
    • Papavoine, C.H.1    Christiaans, B.E.2    Folmer, R.H.3    Konings, R.N.4    Hilbers, C.W.5
  • 12
    • 0035797933 scopus 로고    scopus 로고
    • Structures of gramicidins a, b, and c incorporated into sodium dodecyl sulfate micelles
    • Townsley, L. E., Tucker, W. A., Sham, S., and Hinton, J. F. (2001) Structures of gramicidins a, b, and c incorporated into sodium dodecyl sulfate micelles, Biochemistry 40, 11676-11686.
    • (2001) Biochemistry , vol.40 , pp. 11676-11686
    • Townsley, L.E.1    Tucker, W.A.2    Sham, S.3    Hinton, J.F.4
  • 14
    • 0141530952 scopus 로고    scopus 로고
    • NMR solution structure and topological orientation of monomeric phospholamban in dodecylphosphocholine micelles
    • Zamoon, J., Mascioni, A., Thomas, D. D., and Veglia, G. (2003) NMR solution structure and topological orientation of monomeric phospholamban in dodecylphosphocholine micelles, Biophys. J. 85, 2589-2598.
    • (2003) Biophys. J. , vol.85 , pp. 2589-2598
    • Zamoon, J.1    Mascioni, A.2    Thomas, D.D.3    Veglia, G.4
  • 15
    • 0037426353 scopus 로고    scopus 로고
    • NMR structure and backbone dynamics of the extended second transmembrane domain of the human neuronal glycine receptor alphal subunit
    • Yushmanov, V. E., Mandal, P. K., Liu, Z., Tang, P., and Xu, Y. (2003) NMR structure and backbone dynamics of the extended second transmembrane domain of the human neuronal glycine receptor alphal subunit, Biochemistry 42, 3989-3995.
    • (2003) Biochemistry , vol.42 , pp. 3989-3995
    • Yushmanov, V.E.1    Mandal, P.K.2    Liu, Z.3    Tang, P.4    Xu, Y.5
  • 16
    • 0242507446 scopus 로고    scopus 로고
    • NMR structure and dynamics of the second transmembrane domain of the neuronal acetylcholine receptor beta 2 subunit
    • Yushmanov, V. E., Xu, Y., Tang, P., Mandal, P. K., and Liu, Z. (2003) NMR structure and dynamics of the second transmembrane domain of the neuronal acetylcholine receptor beta 2 subunit, Biochemistry 42, 13058-13065.
    • (2003) Biochemistry , vol.42 , pp. 13058-13065
    • Yushmanov, V.E.1    Xu, Y.2    Tang, P.3    Mandal, P.K.4    Liu, Z.5
  • 17
    • 0031062621 scopus 로고    scopus 로고
    • 1H NMR experiments show that the 23-residue magainin antibiotic peptide is an alpha-helix in dodecylphosphocholine micelles, sodium dodecyl sulfate micelles, and trifluoroethanol/water solution
    • 1H NMR experiments show that the 23-residue magainin antibiotic peptide is an alpha-helix in dodecylphosphocholine micelles, sodium dodecyl sulfate micelles, and trifluoroethanol/water solution, J. Biomol. NMR 9, 127-135.
    • (1997) J. Biomol. NMR , vol.9 , pp. 127-135
    • Gesell, J.1    Zasloff, M.2    Opella, S.J.3
  • 18
    • 0037139592 scopus 로고    scopus 로고
    • Micelle-induced curvature in a water-insoluble hiv-1 env peptide revealed by NMR dipolar coupling measurement in stretched polyacrylamide gel
    • Chou, J. J., Kaufman, J. D., Stahl, S. J., Wingfield, P. T., and Bax, A. (2002) Micelle-induced curvature in a water-insoluble hiv-1 env peptide revealed by NMR dipolar coupling measurement in stretched polyacrylamide gel, J. Am. Chem. Soc. 124, 2450-2451.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 2450-2451
    • Chou, J.J.1    Kaufman, J.D.2    Stahl, S.J.3    Wingfield, P.T.4    Bax, A.5
  • 19
    • 0037165652 scopus 로고    scopus 로고
    • Heteronuclear NMR studies of human serum apolipoprotein a-i. Part i. Secondary structure in lipid-mimetic solution
    • Okon, M., Frank, P. G., Marcel, Y. L., and Cushley, R. J. (2002) Heteronuclear NMR studies of human serum apolipoprotein a-i. Part i. Secondary structure in lipid-mimetic solution, FEBS Lett. 517 (1-3), 139-143.
    • (2002) FEBS Lett. , vol.517 , Issue.1-3 , pp. 139-143
    • Okon, M.1    Frank, P.G.2    Marcel, Y.L.3    Cushley, R.J.4
  • 21
    • 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., and Schmieder, (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    Schmieder5
  • 27
    • 0347985776 scopus 로고    scopus 로고
    • Subunit a of the E. coli ATP synthase: Reconstitution and high-resolution NMR with protein purified in a mixed polarity solvent
    • Dmitriev, O. Y., Altendorf, K., and Fillingame, R. H. (2004) Subunit a of the E. coli ATP synthase: Reconstitution and high-resolution NMR with protein purified in a mixed polarity solvent, FEBS Lett. 556, 35-38.
    • (2004) FEBS Lett. , vol.556 , pp. 35-38
    • Dmitriev, O.Y.1    Altendorf, K.2    Fillingame, R.H.3
  • 28
    • 0033560680 scopus 로고    scopus 로고
    • NMR studies of subunit c of the ATP synthase from Propionigenium modestum in dodecylsulphate micelles
    • Matthey, U., Kaim, G., Braun, D., Wuthrich, K., and Dimroth (1999) NMR studies of subunit c of the ATP synthase from Propionigenium modestum in dodecylsulphate micelles, Eur. J. Biochem. 261, 459-467.
    • (1999) Eur. J. Biochem. , vol.261 , pp. 459-467
    • Matthey, U.1    Kaim, G.2    Braun, D.3    Wuthrich, K.4    Dimroth5
  • 29
    • 0032060715 scopus 로고    scopus 로고
    • On choosing a detergent for solution NMR studies of membrane proteins
    • Vinogradova, O., Sonnichsen, F., and Sanders, C. R., II (1998) On choosing a detergent for solution NMR studies of membrane proteins, J. Biomol. NMR 11, 381-386.
    • (1998) J. Biomol. NMR , vol.11 , pp. 381-386
    • Vinogradova, O.1    Sonnichsen, F.2    Sanders II, C.R.3
  • 33
    • 0030861070 scopus 로고    scopus 로고
    • NMR and membrane proteins
    • Opella, S. J. (1997) NMR and membrane proteins, Nat. Struct. Biol. 4 (Suppl.), 845-848.
    • (1997) Nat. Struct. Biol. , vol.4 , Issue.SUPPL. , pp. 845-848
    • Opella, S.J.1
  • 36
    • 0042029753 scopus 로고    scopus 로고
    • Dipolar waves as NMR maps of helices in proteins
    • Mesleh, M. F., and Opella, S. J. (2003) Dipolar waves as NMR maps of helices in proteins, J. Magn. Reson. 163, 288-299.
    • (2003) J. Magn. Reson. , vol.163 , pp. 288-299
    • Mesleh, M.F.1    Opella, S.J.2
  • 37
    • 0038575449 scopus 로고    scopus 로고
    • Structure and dynamics of a membrane protein in micelles from three solution NMR experiments
    • Lee, S., Mesleh, M. F., and Opella, S. J. (2003) Structure and dynamics of a membrane protein in micelles from three solution NMR experiments, J. Biomol. NMR 26, 327-334.
    • (2003) J. Biomol. NMR , vol.26 , pp. 327-334
    • Lee, S.1    Mesleh, M.F.2    Opella, S.J.3
  • 38
    • 0031954925 scopus 로고    scopus 로고
    • Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms
    • Wallin, E., and von Heijne, G. (1998) Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms, Protein Sci. 7, 1029-1038.
    • (1998) Protein Sci. , vol.7 , pp. 1029-1038
    • Wallin, E.1    Von Heijne, G.2
  • 40
    • 0038240633 scopus 로고    scopus 로고
    • Bacterial mercury resistance from atoms to ecosystems
    • Barkay, T., Miller, S. M., and Summers, A. O. (2003) Bacterial mercury resistance from atoms to ecosystems, FEMS Microbiol. Rev. 27, 355-384.
    • (2003) FEMS Microbiol. Rev. , vol.27 , pp. 355-384
    • Barkay, T.1    Miller, S.M.2    Summers, A.O.3
  • 42
    • 0030971055 scopus 로고    scopus 로고
    • Structures of the reduced and mercury-bound forms of merp, the periplasmic protein from the bacterial mercury detoxification system
    • Steele, R. A., and Opella, S. J. (1997) Structures of the reduced and mercury-bound forms of merp, the periplasmic protein from the bacterial mercury detoxification system, Biochemistry 36, 6885-6895.
    • (1997) Biochemistry , vol.36 , pp. 6885-6895
    • Steele, R.A.1    Opella, S.J.2
  • 43
    • 0023253810 scopus 로고
    • Role of the mert and merp gene products of transposon tn501 in the induction and expression of resistance to mercuric ions
    • Lund, P. A., and Brown, N. L. (1987) Role of the mert and merp gene products of transposon tn501 in the induction and expression of resistance to mercuric ions, Gene 52 (2-3), 207-214.
    • (1987) Gene , vol.52 , Issue.2-3 , pp. 207-214
    • Lund, P.A.1    Brown, N.L.2
  • 44
    • 0028133510 scopus 로고
    • The sequence of the mer operon of pmer327/419 and transposon ends of pmer327/419, 330 and 05
    • Hobman, J., Kholodii, G., Nikiforov, V., Ritchie, D. A., Strike, P., and Yurieva, O. (1994) The sequence of the mer operon of pmer327/419 and transposon ends of pmer327/419, 330 and 05, Gene 146, 73-78.
    • (1994) Gene , vol.146 , pp. 73-78
    • Hobman, J.1    Kholodii, G.2    Nikiforov, V.3    Ritchie, D.A.4    Strike, P.5    Yurieva, O.6
  • 45
    • 0034697083 scopus 로고    scopus 로고
    • Merf is a mercury transport protein: Different structures but a common mechanism for mercuric ion transporters?
    • Wilson, J. R., Leang, C., Morby, A. P., Hobman, J. L., and Brown, N. L. (2000) Merf is a mercury transport protein: Different structures but a common mechanism for mercuric ion transporters?, FEBS Lett. 472, 78-82.
    • (2000) FEBS Lett. , vol.472 , pp. 78-82
    • Wilson, J.R.1    Leang, C.2    Morby, A.P.3    Hobman, J.L.4    Brown, N.L.5
  • 46
    • 0029149131 scopus 로고
    • The role of cysteine residues in the transport of mercuric ions by the tn501 mert and merp mercury-resistance proteins
    • Morby, A. P., Hobman, J. L., and Brown, N. L. (1995) The role of cysteine residues in the transport of mercuric ions by the tn501 mert and merp mercury-resistance proteins, Mol. Microbiol. 17, 25-35.
    • (1995) Mol. Microbiol. , vol.17 , pp. 25-35
    • Morby, A.P.1    Hobman, J.L.2    Brown, N.L.3
  • 48
    • 0842269101 scopus 로고    scopus 로고
    • Biophysical characterization of the merp-like amino-terminal extension of the mercuric reductase from ralstonia metallidurans ch34
    • Rossy, E., Champier, L., Bersch, B., Bratscher, B., Blackledge, M., and Coves, J. (2004) Biophysical characterization of the merp-like amino-terminal extension of the mercuric reductase from ralstonia metallidurans ch34, J. Biol. Inorg. Chem. 9, 49-58.
    • (2004) J. Biol. Inorg. Chem. , vol.9 , pp. 49-58
    • Rossy, E.1    Champier, L.2    Bersch, B.3    Bratscher, B.4    Blackledge, M.5    Coves, J.6
  • 49
    • 0034731004 scopus 로고    scopus 로고
    • Lanthanide ion binding to adventitious sites aligns membrane proteins in micelles for solution NMR spectroscopy
    • Veglia, G., and Opella, S. J. (2000) Lanthanide ion binding to adventitious sites aligns membrane proteins in micelles for solution NMR spectroscopy, J. Am. Chem. Soc. 122, 11733-11734.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 11733-11734
    • Veglia, G.1    Opella, S.J.2
  • 50
    • 0032500340 scopus 로고    scopus 로고
    • Modulation of the alignment tensor of macromolecules dissolved in a dilute liquid crystalline medium
    • Ramirez, B. E., and Bax, A. (1998) Modulation of the alignment tensor of macromolecules dissolved in a dilute liquid crystalline medium, J. Am. Chem. Soc. 120, 9106-9107.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 9106-9107
    • Ramirez, B.E.1    Bax, A.2
  • 51
    • 0035925135 scopus 로고    scopus 로고
    • Determination of protein backbone structure using only residual dipolar couplings
    • Hus, J. C., Marion, D., and Blackledge, M. (2001) Determination of protein backbone structure using only residual dipolar couplings, J. Am. Chem. Soc. 123, 1541-1542.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 1541-1542
    • Hus, J.C.1    Marion, D.2    Blackledge, M.3
  • 52
    • 0036217488 scopus 로고    scopus 로고
    • Deuterium/hydrogen exchange factors measured by solution nuclear magnetic resonance spectroscopy as indicators of the structure and topology of membrane proteins
    • Veglia, G., Zeri, A. C., Ma, C., and Opella, S. J. (2002) Deuterium/hydrogen exchange factors measured by solution nuclear magnetic resonance spectroscopy as indicators of the structure and topology of membrane proteins, Biophys. J. 82, 2176-2183.
    • (2002) Biophys. J. , vol.82 , pp. 2176-2183
    • Veglia, G.1    Zeri, A.C.2    Ma, C.3    Opella, S.J.4
  • 53
    • 0034814745 scopus 로고    scopus 로고
    • Structural evaluation of phospholipid bicelles for solution-state studies of membrane-associated biomolecules
    • Glover, K. J., Whiles, J. A., Wu, G., Yu, N., Deems, R., Struppe, J. O., Stark, R. E., Komives, E. A., and Void, R. R. (2001) Structural evaluation of phospholipid bicelles for solution-state studies of membrane-associated biomolecules, Biophys. J. 81, 2163-2171.
    • (2001) Biophys. J. , vol.81 , pp. 2163-2171
    • Glover, K.J.1    Whiles, J.A.2    Wu, G.3    Yu, N.4    Deems, R.5    Struppe, J.O.6    Stark, R.E.7    Komives, E.A.8    Void, R.R.9
  • 54
    • 0031112791 scopus 로고    scopus 로고
    • Isotropic solutions of phospholipid bicelles: A new membrane mimetic for high-resolution NMR studies of polypeptides
    • Vold, R. R., Prosser, R. S., and Deese, A. J. (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
  • 55
    • 9544219695 scopus 로고    scopus 로고
    • Weak alignment of membrane proteins in stressed polyacrylamide gels
    • Jones, D. H., and Opella, S. J. (2004) Weak alignment of membrane proteins in stressed polyacrylamide gels, J. Magn. Reson. 171, 258-269.
    • (2004) J. Magn. Reson. , vol.171 , pp. 258-269
    • Jones, D.H.1    Opella, S.J.2
  • 56
    • 0034501042 scopus 로고    scopus 로고
    • Solution NMR of proteins within polyacrylamide gels: Diffusional properties and residual alignment by mechanical stress or embedding of oriented purple membranes
    • Sass, H. J., Musco, G., Stahl, S. J., Wingfield, P. T., and Grzesiek, S. (2000) Solution NMR of proteins within polyacrylamide gels: Diffusional properties and residual alignment by mechanical stress or embedding of oriented purple membranes. J. Biomol. NMR 18, 303-309.
    • (2000) J. Biomol. NMR , vol.18 , pp. 303-309
    • Sass, H.J.1    Musco, G.2    Stahl, S.J.3    Wingfield, P.T.4    Grzesiek, S.5
  • 57
    • 0034755357 scopus 로고    scopus 로고
    • Controlling residual dipolar couplings in high-resolution NMR of proteins by strain induced alignment in a gel
    • Ishii, Y., Markus, M. A., and Tycko, R. (2001) Controlling residual dipolar couplings in high-resolution NMR of proteins by strain induced alignment in a gel, J. Biomol. NMR 21, 141-151.
    • (2001) J. Biomol. NMR , vol.21 , pp. 141-151
    • Ishii, Y.1    Markus, M.A.2    Tycko, R.3
  • 58
    • 0035692486 scopus 로고    scopus 로고
    • A simple apparatus for generating stretched polyacrylamide gels, yielding uniform alignment of proteins and detergent micelles
    • Chou, J. J., Gaemers, S., Howder, B., Louis, J. M., and Bax, A. (2001) A simple apparatus for generating stretched polyacrylamide gels, yielding uniform alignment of proteins and detergent micelles, J. Biomol. NMR 21, 377-382.
    • (2001) J. Biomol. NMR , vol.21 , pp. 377-382
    • Chou, J.J.1    Gaemers, S.2    Howder, B.3    Louis, J.M.4    Bax, A.5
  • 60
    • 0029338320 scopus 로고
    • Improved sensitivity of HSQC spectra of exchanging protons at short interscan delays using a new fast HSQC (fhsqc) detection scheme that avoids water saturation
    • Mori, S., Abeygunawardana, C., Johnson, M. O., and van Zijl, P. C. (1995) Improved sensitivity of HSQC spectra of exchanging protons at short interscan delays using a new fast HSQC (fhsqc) detection scheme that avoids water saturation, J. Magn. Reson. B 108, 94-98.
    • (1995) J. Magn. Reson. B , vol.108 , pp. 94-98
    • Mori, S.1    Abeygunawardana, C.2    Johnson, M.O.3    Van Zijl, P.C.4
  • 62
    • 0347722841 scopus 로고    scopus 로고
    • Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients
    • Sattler, M., Schleucher, J., and Griesinger, C. (1999) Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients, Prog. Nucl. Magn. Reson. Spectrosc. 34, 93-158.
    • (1999) Prog. Nucl. Magn. Reson. Spectrosc. , vol.34 , pp. 93-158
    • Sattler, M.1    Schleucher, J.2    Griesinger, C.3
  • 63
    • 0000382336 scopus 로고
    • Detection of proton homonuclear NOE between amide sites in proteins with proton/nitrogen-15 heteronuclear correlation spectroscopy
    • Shon, K., and Opella, S. J. (1989) Detection of proton homonuclear NOE between amide sites in proteins with proton/nitrogen-15 heteronuclear correlation spectroscopy, J. Magn. Reson. 82, 193-197.
    • (1989) J. Magn. Reson. , vol.82 , pp. 193-197
    • Shon, K.1    Opella, S.J.2
  • 64
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on unix pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: a multidimensional spectral processing system based on unix pipes, J. Biomol. NMR 6, 277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 65
    • 0043032433 scopus 로고    scopus 로고
    • Sensitivity-enhanced 2D IPAP, TROSY-anti-TROSY, and E. Cosy experiments: Alternatives for measuring dipolar N-15-H-1(N) couplings
    • Ding, K. Y., and Gronenborn, A. M. (2003) Sensitivity-enhanced 2D IPAP, TROSY-anti-TROSY, and E. Cosy experiments: alternatives for measuring dipolar N-15-H-1(N) couplings, J. Magn. Reson. 163, 208-214.
    • (2003) J. Magn. Reson. , vol.163 , pp. 208-214
    • Ding, K.Y.1    Gronenborn, A.M.2
  • 66
    • 0033577269 scopus 로고    scopus 로고
    • Improving the packing and accuracy of NMR structures with a pseudopotential for the radius of gyration
    • Kuszewski, J., Gronenborn, A. M., and Clore, G. M. (1999) Improving the packing and accuracy of NMR structures with a pseudopotential for the radius of gyration, J. Am. Chem. Soc. 121, 2337-2338.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 2337-2338
    • Kuszewski, J.1    Gronenborn, A.M.2    Clore, G.M.3
  • 67
    • 0031575423 scopus 로고    scopus 로고
    • Monsster: A method for folding globular proteins with a small number of distance restraints
    • Skolnick, J., Kolinski, A., and Ortiz, A. R. (1997) Monsster: A method for folding globular proteins with a small number of distance restraints, J. Mol. Biol. 265, 217-241.
    • (1997) J. Mol. Biol. , vol.265 , pp. 217-241
    • Skolnick, J.1    Kolinski, A.2    Ortiz, A.R.3
  • 68
    • 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. (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
  • 69
    • 0034296491 scopus 로고    scopus 로고
    • Sources of and solutions to problems in the refinement of protein NMR structures against torsion angle potentials of mean force
    • Kuszewski, J., and Clore, G. M. (2000) Sources of and solutions to problems in the refinement of protein NMR structures against torsion angle potentials of mean force, J. Magn. Reson. 146, 249-254.
    • (2000) J. Magn. Reson. , vol.146 , pp. 249-254
    • Kuszewski, J.1    Clore, G.M.2
  • 70
    • 0023927904 scopus 로고
    • Identification of structural motifs from protein coordinate data: Secondary structure and first level supersecondary structure
    • Richards, F. M., and Kundrot, C. E. (1988) Identification of structural motifs from protein coordinate data: Secondary structure and first level supersecondary structure, Proteins 3, 71-84.
    • (1988) Proteins , vol.3 , pp. 71-84
    • Richards, F.M.1    Kundrot, C.E.2
  • 72
    • 43949165935 scopus 로고
    • Effect of detergent concentration on multidimensional solution NMR spectra of membrane proteins in micelles
    • McDonnell, P. A., and Opella, S. J. (1993) Effect of detergent concentration on multidimensional solution NMR spectra of membrane proteins in micelles, J. Magn. Reson. 102, 120-125.
    • (1993) J. Magn. Reson. , vol.102 , pp. 120-125
    • McDonnell, P.A.1    Opella, S.J.2
  • 75
    • 0034899781 scopus 로고    scopus 로고
    • Evaluation of methods for the prediction of membrane spanning regions
    • Moller, S., Croning, M. D., and Apweiler, R. (2001) Evaluation of methods for the prediction of membrane spanning regions, Bioinformatics 17, 646-653.
    • (2001) Bioinformatics , vol.17 , pp. 646-653
    • Moller, S.1    Croning, M.D.2    Apweiler, R.3
  • 77
  • 78
    • 3042807889 scopus 로고    scopus 로고
    • Site-specific labelling with a metal chelator for protein-structure refinement
    • Pintacuda, G., Moshref, A., Leonchiks, A., Sharipo, A., and Otting, G. (2004) Site-specific labelling with a metal chelator for protein-structure refinement, J. Biol. NMR 29, 351-361.
    • (2004) J. Biol. NMR , vol.29 , pp. 351-361
    • Pintacuda, G.1    Moshref, A.2    Leonchiks, A.3    Sharipo, A.4    Otting, G.5
  • 80
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • Wimley, W. C., and White, S. H. (1996) Experimentally determined hydrophobicity scale for proteins at membrane interfaces, Nat. Struct. Biol. 3, 842-848.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2
  • 81
    • 0036430199 scopus 로고    scopus 로고
    • Proline-induced distortions of transmembrane helices
    • Cordes, F. S., Bright, J. N., and Sansom, M. S. (2002) Proline-induced distortions of transmembrane helices, J. Mol. Biol. 323, 951-960.
    • (2002) J. Mol. Biol. , vol.323 , pp. 951-960
    • Cordes, F.S.1    Bright, J.N.2    Sansom, M.S.3
  • 82
    • 0031563818 scopus 로고    scopus 로고
    • Helix packing in membrane proteins
    • Bowie, J. U. (1997) Helix packing in membrane proteins, J. Mol. Biol. 272, 780-789.
    • (1997) J. Mol. Biol. , vol.272 , pp. 780-789
    • Bowie, J.U.1
  • 83
    • 0442276416 scopus 로고    scopus 로고
    • Structural features of transmembrane helices
    • Hildebrand, P. W., Preissner, R., and Frömmel, C. (2004) Structural features of transmembrane helices, FEBS Lett. 559, 145-151.
    • (2004) FEBS Lett. , vol.559 , pp. 145-151
    • Hildebrand, P.W.1    Preissner, R.2    Frömmel, C.3
  • 84
    • 0029149131 scopus 로고
    • The role of cysteine residues in the transport of mercuric ions by the tn501 mert and merp mercury-resistance proteins
    • Morby, A. P., Hobman, J. L., and Brown, N. L. (1995) The role of cysteine residues in the transport of mercuric ions by the tn501 mert and merp mercury-resistance proteins, Mol. Microbiol. 17, 25-35.
    • (1995) Mol. Microbiol. , vol.17 , pp. 25-35
    • Morby, A.P.1    Hobman, J.L.2    Brown, N.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.