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Volumn 163, Issue 2, 2003, Pages 288-299

Dipolar waves as NMR maps of helices in proteins

Author keywords

[No Author keywords available]

Indexed keywords

MOLECULAR STRUCTURE; OSCILLATIONS; PROTEINS; TRAVELING WAVE TUBES;

EID: 0042029753     PISSN: 10907807     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1090-7807(03)00119-8     Document Type: Article
Times cited : (71)

References (70)
  • 3
    • 0035142956 scopus 로고    scopus 로고
    • A simple approach to membrane protein secondary structure and topology based on NMR spectroscopy
    • Marassi F.M. A simple approach to membrane protein secondary structure and topology based on NMR spectroscopy. Biophys. J. 80:2001;994-1003.
    • (2001) Biophys. J. , vol.80 , pp. 994-1003
    • Marassi, F.M.1
  • 4
    • 0025346254 scopus 로고
    • Transmembrane protein-structure - Spin labeling of Bacteriorhodopsin mutants
    • Altenbach C., Marti T., Khorana H.G., Hubbell W.J. Transmembrane protein-structure - Spin labeling of Bacteriorhodopsin mutants. Science. 248:1990;1088-1092.
    • (1990) Science , vol.248 , pp. 1088-1092
    • Altenbach, C.1    Marti, T.2    Khorana, H.G.3    Hubbell, W.J.4
  • 5
    • 0032042825 scopus 로고    scopus 로고
    • An NMR investigation of the conformational effect of nitroxide spin labels on Ala-rich helical peptides
    • Bolin K.A., Hanson P., Wright S.J., Millhauser G.L. An NMR investigation of the conformational effect of nitroxide spin labels on Ala-rich helical peptides. J. Magn. Reson. 131:1998;248-253.
    • (1998) J. Magn. Reson. , vol.131 , pp. 248-253
    • Bolin, K.A.1    Hanson, P.2    Wright, S.J.3    Millhauser, G.L.4
  • 6
    • 0029115328 scopus 로고
    • Determination of the distance between 2 spin labels attached to a macromolecule
    • Rabenstein M.D., Shin Y.K. Determination of the distance between 2 spin labels attached to a macromolecule. Proc. Natl. Acad. Sci. USA. 92:1995;8239-8243.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8239-8243
    • Rabenstein, M.D.1    Shin, Y.K.2
  • 7
    • 0021105573 scopus 로고
    • Protein conformation and proton NMR chemical-shifts
    • Pardi A., Wagner G., Wuthrich K. Protein conformation and proton NMR chemical-shifts. Eur. J. Biochem. 137:1983;445-454.
    • (1983) Eur. J. Biochem. , vol.137 , pp. 445-454
    • Pardi, A.1    Wagner, G.2    Wuthrich, K.3
  • 8
    • 0000701932 scopus 로고
    • α-Proton chemical-shifts and secondary structure in proteins
    • Szilagyi L., Jardetzky O. α-Proton chemical-shifts and secondary structure in proteins. J. Magn. Reson. 83:1989;441-449.
    • (1989) J. Magn. Reson. , vol.83 , pp. 441-449
    • Szilagyi, L.1    Jardetzky, O.2
  • 9
    • 0025328818 scopus 로고
    • Secondary-structure dependent chemical-shifts in proteins
    • Williamson M.P. Secondary-structure dependent chemical-shifts in proteins. Biopolymers. 29:1990;1428-1431.
    • (1990) Biopolymers , vol.29 , pp. 1428-1431
    • Williamson, M.P.1
  • 10
    • 0027308278 scopus 로고
    • Secondary and tertiary structural effects on protein NMR chemical-shifts - An ab initio approach
    • De Dios A.C., Pearson J.G., Oldfield E. Secondary and tertiary structural effects on protein NMR chemical-shifts - an ab initio approach. Science. 260:1993;1491-1496.
    • (1993) Science , vol.260 , pp. 1491-1496
    • De Dios, A.C.1    Pearson, J.G.2    Oldfield, E.3
  • 11
    • 0026029051 scopus 로고
    • Amide chemical-shifts in many helices in peptides and proteins are periodic
    • Kuntz I.D., Kosen P.A., Craig E.C. Amide chemical-shifts in many helices in peptides and proteins are periodic. J. Am. Chem. Soc. 113:1991;1406-1408.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 1406-1408
    • Kuntz, I.D.1    Kosen, P.A.2    Craig, E.C.3
  • 15
    • 0008875441 scopus 로고
    • Carbon-13 chemical shielding tensors in single-crystal durene
    • Pausak S., Pines A., Waugh J.S. Carbon-13 chemical shielding tensors in single-crystal durene. J. Chem. Phys. 59:1973;599-612.
    • (1973) J. Chem. Phys. , vol.59 , pp. 599-612
    • Pausak, S.1    Pines, A.2    Waugh, J.S.3
  • 16
    • 36749111635 scopus 로고
    • 2-Dimensional C-13 NMR of highly oriented polyethylene
    • Opella S.J., Waugh J.S. 2-Dimensional C-13 NMR of highly oriented polyethylene. J. Chem. Phys. 66:1977;4919-4924.
    • (1977) J. Chem. Phys. , vol.66 , pp. 4919-4924
    • Opella, S.J.1    Waugh, J.S.2
  • 17
    • 0034919243 scopus 로고    scopus 로고
    • Dipolar couplings in macromolecular structure determination
    • Bax A., Kontaxis G., Tjandra N. Dipolar couplings in macromolecular structure determination. Meth. Enzymol. 339:2001;127-174.
    • (2001) Meth. Enzymol. , vol.339 , pp. 127-174
    • Bax, A.1    Kontaxis, G.2    Tjandra, N.3
  • 18
    • 84967789667 scopus 로고
    • Recent results in the field of liquid crystals
    • Saupe A. Recent results in the field of liquid crystals. Angew. Chem. Intl. Ed. 7:1968;97-112.
    • (1968) Angew. Chem. Intl. Ed. , vol.7 , pp. 97-112
    • Saupe, A.1
  • 20
    • 0030861070 scopus 로고    scopus 로고
    • NMR and membrane proteins
    • Opella S.J. NMR and membrane proteins. Nat. Struct. Biol. 4:1997;845-848.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 845-848
    • Opella, S.J.1
  • 22
    • 0034293196 scopus 로고    scopus 로고
    • Lanthanide ions bind specifically to an added "EF-hand" and orient a membrane protein in micelles for solution NMR spectroscopy
    • Ma C., Opella S.J. Lanthanide ions bind specifically to an added "EF-hand" and orient a membrane protein in micelles for solution NMR spectroscopy. J. Magn. Reson. 146:2000;381-384.
    • (2000) J. Magn. Reson. , vol.146 , pp. 381-384
    • Ma, C.1    Opella, S.J.2
  • 23
    • 0034731004 scopus 로고    scopus 로고
    • Lanthanide ion binding to adventitious sites aligns membrane proteins in micelles for solution NMR spectroscopy
    • Veglia G., Opella S.J. Lanthanide ion binding to adventitious sites aligns membrane proteins in micelles for solution NMR spectroscopy. J. Am. Chem. Soc. 122:2000;11733-11734.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 11733-11734
    • Veglia, G.1    Opella, S.J.2
  • 24
    • 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., Grzesiek S. Solution NMR of proteins within polyacrylamide gels: diffusional properties and residual alignment by mechanical stress or embedding of oriented purple membranes. J. Biomol. NMR. 18:2000;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
  • 25
    • 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., Tycko R. Controlling residual dipolar couplings in high-resolution NMR of proteins by strain induced alignment in a gel. J. Biomol. NMR. 21:2001;141-151.
    • (2001) J. Biomol. NMR , vol.21 , pp. 141-151
    • Ishii, Y.1    Markus, M.A.2    Tycko, R.3
  • 26
    • 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., Bax A. A simple apparatus for generating stretched polyacrylamide gels, yielding uniform alignment of proteins and detergent micelles. J. Biomol. NMR. 21:2001;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
  • 27
    • 0042689882 scopus 로고    scopus 로고
    • http://www-lecb.ncifcrf.gov/̃kumarsan/HELANAL/helanal.html.
  • 29
    • 0001675109 scopus 로고
    • Relationship between amide proton chemical-shifts and hydrogen-bonding in amphipathic α-helical peptides
    • Zhou N.E., Zhu B.Y., Sykes B.D., Hodges R.S. Relationship between amide proton chemical-shifts and hydrogen-bonding in amphipathic α-helical peptides. J. Am. Chem. Soc. 114:1992;4320-4326.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 4320-4326
    • Zhou, N.E.1    Zhu, B.Y.2    Sykes, B.D.3    Hodges, R.S.4
  • 30
    • 0037263087 scopus 로고    scopus 로고
    • Myristoylation as a general method for immobilization and alignment of soluble proteins for solid-state NMR structural studies
    • Mesleh M.F., Valentine K.G., Opella S.J., Louis J.M., Gronenborn A.M. Myristoylation as a general method for immobilization and alignment of soluble proteins for solid-state NMR structural studies. J. Biomol. NMR. 25:2003;55-61.
    • (2003) J. Biomol. NMR , vol.25 , pp. 55-61
    • Mesleh, M.F.1    Valentine, K.G.2    Opella, S.J.3    Louis, J.M.4    Gronenborn, A.M.5
  • 31
    • 0026223896 scopus 로고
    • A relational database for sequence-specific NMR data
    • http://www.bmrb.wisc.edu/ Seavey B.R., Farr E.A., Westler W.M., Markley J.L. A relational database for sequence-specific NMR data. J. Biomol. NMR. 1(1):1991;217-236.
    • (1991) J. Biomol. NMR , vol.1 , Issue.1 , pp. 217-236
    • Seavey, B.R.1    Farr, E.A.2    Westler, W.M.3    Markley, J.L.4
  • 34
    • 0032541335 scopus 로고    scopus 로고
    • The solution structure of ribosomal protein S4 δ 41 reveals two subdomains and a positively charged surface that may interact with RNA
    • Markus M.A., Gerstner R.B., Draper R.B., Torchia D.A. The solution structure of ribosomal protein S4 δ 41 reveals two subdomains and a positively charged surface that may interact with RNA. EMBO J. 17:1998;4559-4571.
    • (1998) EMBO J. , vol.17 , pp. 4559-4571
    • Markus, M.A.1    Gerstner, R.B.2    Draper, R.B.3    Torchia, D.A.4
  • 35
    • 0032478114 scopus 로고    scopus 로고
    • Solution structure of calcium-bound rat S100B(ββ) as determined by nuclear magnetic resonance spectroscopy
    • Drohat A.C., Baldisseri D.M., Rustandi R.R., Weber D.J. Solution structure of calcium-bound rat S100B(. ββ) as determined by nuclear magnetic resonance spectroscopy Biochemistry. 37:1998;2729-2740.
    • (1998) Biochemistry , vol.37 , pp. 2729-2740
    • Drohat, A.C.1    Baldisseri, D.M.2    Rustandi, R.R.3    Weber, D.J.4
  • 36
    • 0032939176 scopus 로고    scopus 로고
    • Solution structure of the 40,000 M-r phosphoryl transfer complex between the N-terminal domain of enzyme I and Hpr
    • Garrett D.S., Seok Y.J., Peterkofsky A., Gronenborn A.M., Clore G.M. Solution structure of the 40,000 M-r phosphoryl transfer complex between the N-terminal domain of enzyme I and Hpr. Nat. Struct. Biol. 6:1999;166-173.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 166-173
    • Garrett, D.S.1    Seok, Y.J.2    Peterkofsky, A.3    Gronenborn, A.M.4    Clore, G.M.5
  • 37
    • 1542563746 scopus 로고    scopus 로고
    • NMR structure of the N-terminal domain of E. coli DNAb helicase: Implications for structure rearrangements in the helicase hexamer
    • Weigelt J., Brown S.E., Miles C.S., Dixon N.E., Otting G. NMR structure of the N-terminal domain of E. coli DNAb helicase: implications for structure rearrangements in the helicase hexamer. Struct. Fold. Des. 7:1999;681-690.
    • (1999) Struct. Fold. Des. , vol.7 , pp. 681-690
    • Weigelt, J.1    Brown, S.E.2    Miles, C.S.3    Dixon, N.E.4    Otting, G.5
  • 41
    • 0032113480 scopus 로고    scopus 로고
    • A robust method for determining the magnitude of the fully asymmetric alignment tensor of oriented macromolecules in the absence of structural information
    • Clore G.M., Gronenborn A.M., Bax A. A robust method for determining the magnitude of the fully asymmetric alignment tensor of oriented macromolecules in the absence of structural information. J. Magn. Reson. 133:1998;216-221.
    • (1998) J. Magn. Reson. , vol.133 , pp. 216-221
    • Clore, G.M.1    Gronenborn, A.M.2    Bax, A.3
  • 42
    • 0034884233 scopus 로고    scopus 로고
    • A novel interactive tool for rigid-body modeling of multi-domain macromolecules using residual dipolar couplings
    • Dosset P., Hus J.C., Marion D., Blackledge M. A novel interactive tool for rigid-body modeling of multi-domain macromolecules using residual dipolar couplings. J. Biomol. NMR. 20:2001;223-231.
    • (2001) J. Biomol. NMR , vol.20 , pp. 223-231
    • Dosset, P.1    Hus, J.C.2    Marion, D.3    Blackledge, M.4
  • 43
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi R., Billeter M., Wuthrich K. MOLMOL: A program for display and analysis of macromolecular structures. J. Mol. Graph. 14:1996;51-55.
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 44
    • 0030239753 scopus 로고    scopus 로고
    • Algorithms for finding the axis of a helix: Fast rotational and parametric least-squares methods
    • Christopher N.A., Swanson R., Baldwin T.O. Algorithms for finding the axis of a helix: fast rotational and parametric least-squares methods. Comp. Chem. 20:1996;339-345.
    • (1996) Comp. Chem. , vol.20 , pp. 339-345
    • Christopher, N.A.1    Swanson, R.2    Baldwin, T.O.3
  • 45
    • 0036213784 scopus 로고    scopus 로고
    • 15N]-labeled membrane proteins in oriented lipid bilayers
    • 15N ]-labeled membrane proteins in oriented lipid bilayers J. Biomol. NMR. 22:2002;225-247.
    • (2002) J. Biomol. NMR , vol.22 , pp. 225-247
    • Vosegaard, T.1    Nielsen, N.2
  • 46
    • 0036787577 scopus 로고    scopus 로고
    • Uniformity, ideality, and hydrogen bonds in transmembrane α-helices
    • Kim S., Cross T.A. Uniformity, ideality, and hydrogen bonds in transmembrane α-helices. Biophys. J. 83:2002;2084-2095.
    • (2002) Biophys. J. , vol.83 , pp. 2084-2095
    • Kim, S.1    Cross, T.A.2
  • 47
    • 0034186215 scopus 로고    scopus 로고
    • A solid-state NMR index of helical membrane protein structure and topology
    • Marassi F.M., Opella S.J. A solid-state NMR index of helical membrane protein structure and topology. J. Magn. Reson. 144:2000;150-155.
    • (2000) J. Magn. Reson. , vol.144 , pp. 150-155
    • Marassi, F.M.1    Opella, S.J.2
  • 49
    • 0036361158 scopus 로고    scopus 로고
    • Using Pisa pies to resolve ambiguities in angular constraints from PISEMA spectra of aligned proteins
    • Marassi F.M., Opella S.J. Using Pisa pies to resolve ambiguities in angular constraints from PISEMA spectra of aligned proteins. J. Biomol. NMR. 23:2002;239-242.
    • (2002) J. Biomol. NMR , vol.23 , pp. 239-242
    • Marassi, F.M.1    Opella, S.J.2
  • 50
  • 53
    • 0034684181 scopus 로고    scopus 로고
    • Measurement of proton, nitrogen, and carbonyl chemical shielding anisotropies in a protein dissolved in a dilute liquid crystalline phase
    • Cornilescu G., Bax A. Measurement of proton, nitrogen, and carbonyl chemical shielding anisotropies in a protein dissolved in a dilute liquid crystalline phase. J. Am. Chem. Soc. 122:2000;10143-10154.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 10143-10154
    • Cornilescu, G.1    Bax, A.2
  • 54
    • 0032719896 scopus 로고    scopus 로고
    • Calculations of NMR dipolar coupling strengths in model peptides
    • Case D.A. Calculations of NMR dipolar coupling strengths in model peptides. J. Biomol. NMR. 15:1999;95-102.
    • (1999) J. Biomol. NMR , vol.15 , pp. 95-102
    • Case, D.A.1
  • 55
    • 0030767003 scopus 로고    scopus 로고
    • 15N -enriched proteins, correlation with hydrogen bond length
    • 15N -enriched proteins, correlation with hydrogen bond length J. Am. Chem. Soc. 119:1997;8076-8082.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 8076-8082
    • Tjandra, N.1    Bax, A.2
  • 56
    • 0027588286 scopus 로고
    • 2H NMR lineshapes of immobilized uniaxially oriented membrane-proteins
    • 2H NMR lineshapes of immobilized uniaxially oriented membrane-proteins Solid State Nucl. Magn. Reson. 2:1993;21-36.
    • (1993) Solid State Nucl. Magn. Reson. , vol.2 , pp. 21-36
    • Ulrich, A.S.1    Watts, A.2
  • 57
    • 0034102297 scopus 로고    scopus 로고
    • Assessment of zinc finger orientations by residual dipolar coupling constants
    • Tsui V., Zhu L.M., Huang T.H., Wright P.E., Case D.A. Assessment of zinc finger orientations by residual dipolar coupling constants. J. Biomol. NMR. 16:2000;9-21.
    • (2000) J. Biomol. NMR , vol.16 , pp. 9-21
    • Tsui, V.1    Zhu, L.M.2    Huang, T.H.3    Wright, P.E.4    Case, D.A.5
  • 58
    • 0034486021 scopus 로고    scopus 로고
    • Solution structure of DinI provides insight into its mode of RecA inactivation
    • Ramirez B.E., Voloshin O.N., Camerini-Otero R.D., Bax A. Solution structure of DinI provides insight into its mode of RecA inactivation. Prot. Sci. 9:2000;2161-2169.
    • (2000) Prot. Sci. , vol.9 , pp. 2161-2169
    • Ramirez, B.E.1    Voloshin, O.N.2    Camerini-Otero, R.D.3    Bax, A.4
  • 59
    • 0033145058 scopus 로고    scopus 로고
    • Order matrix analysis of residual dipolar couplings using singular value decomposition
    • Losonczi J.A., Andrec M., Fischer M.W.F., Prestegard J.H. Order matrix analysis of residual dipolar couplings using singular value decomposition. J. Magn. Reson. 138:1999;334-342.
    • (1999) J. Magn. Reson. , vol.138 , pp. 334-342
    • Losonczi, J.A.1    Andrec, M.2    Fischer, M.W.F.3    Prestegard, J.H.4
  • 60
    • 0034167156 scopus 로고    scopus 로고
    • Variation of molecular alignment as a means of resolving orientational ambiguities in protein structures from dipolar couplings
    • Al-Hashimi H.M., Valafar H., Terrell M., Zartler E.R., Eidsness M.K., Prestegard J.H. Variation of molecular alignment as a means of resolving orientational ambiguities in protein structures from dipolar couplings. J. Magn. Reson. 143:2000;402-406.
    • (2000) J. Magn. Reson. , vol.143 , pp. 402-406
    • Al-Hashimi, H.M.1    Valafar, H.2    Terrell, M.3    Zartler, E.R.4    Eidsness, M.K.5    Prestegard, J.H.6
  • 61
    • 0033551495 scopus 로고    scopus 로고
    • Domain orientation and dynamics in multidomain proteins from residual dipolar couplings
    • Fischer M.W.F., Losonczi J.A., Weaver J.L., Prestegard J.H. Domain orientation and dynamics in multidomain proteins from residual dipolar couplings. Biochemistry. 38:1999;9013-9022.
    • (1999) Biochemistry , vol.38 , pp. 9013-9022
    • Fischer, M.W.F.1    Losonczi, J.A.2    Weaver, J.L.3    Prestegard, J.H.4
  • 63
    • 0029738679 scopus 로고    scopus 로고
    • Structural and sequence characteristics in long α-helices of globular proteins
    • Kumar S., Bansal M. Structural and sequence characteristics in long α-helices of globular proteins. Biophys. J. 71:1998;1574-1586.
    • (1998) Biophys. J. , vol.71 , pp. 1574-1586
    • Kumar, S.1    Bansal, M.2
  • 64
    • 0032879507 scopus 로고    scopus 로고
    • R-factor, free R, and complete cross-validation for dipolar coupling refinement of NMR structures
    • Clore G.M., Garrett D.S. R-factor, free R, and complete cross-validation for dipolar coupling refinement of NMR structures. J. Am. Chem. Soc. 121:1999;9008-9012.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 9008-9012
    • Clore, G.M.1    Garrett, D.S.2
  • 65
    • 0035996721 scopus 로고    scopus 로고
    • Evaluation of uncertainty in alignment tensors obtained from dipolar couplings
    • Zweckstetter M., Bax A. Evaluation of uncertainty in alignment tensors obtained from dipolar couplings. J. Biomol. NMR. 23:2002;127-137.
    • (2002) J. Biomol. NMR , vol.23 , pp. 127-137
    • Zweckstetter, M.1    Bax, A.2
  • 68
    • 0036008215 scopus 로고    scopus 로고
    • Structure refinement of flexible proteins using dipolar couplings: Application to the protein p8MTCP1
    • Demene H., Ducat T., Barthe P., Delsuc M.A., Roumestand C. Structure refinement of flexible proteins using dipolar couplings: application to the protein p8MTCP1. J. Biomol. NMR. 22:2002;47-56.
    • (2002) J. Biomol. NMR , vol.22 , pp. 47-56
    • Demene, H.1    Ducat, T.2    Barthe, P.3    Delsuc, M.A.4    Roumestand, C.5
  • 70
    • 0036018868 scopus 로고    scopus 로고
    • Using conjoined rigid body/torsion angle simulated annealing to determine the relative orientation of covalently linked protein domains from dipolar couplings
    • Clore G.M., Bewley C.A. Using conjoined rigid body/torsion angle simulated annealing to determine the relative orientation of covalently linked protein domains from dipolar couplings. J. Magn. Reson. 154:2002;329-335.
    • (2002) J. Magn. Reson. , vol.154 , pp. 329-335
    • Clore, G.M.1    Bewley, C.A.2


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