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Volumn 566, Issue , 2016, Pages 113-157

Biomolecular Deuteration for Neutron Structural Biology and Dynamics

Author keywords

Contrast variation; Deuteration; Dynamics; Isotope labelling; Neutron crystallography; Neutron reflection; Neutron scattering; SANS; Structural biology

Indexed keywords

AMINO ACID; DEUTERIUM; DNA; LIPID; MEMBRANE PROTEIN; RECOMBINANT PROTEIN; TRANSFER RNA; SOLUTION AND SOLUBILITY;

EID: 84954392033     PISSN: 00766879     EISSN: 15577988     Source Type: Book Series    
DOI: 10.1016/bs.mie.2015.11.001     Document Type: Chapter
Times cited : (77)

References (139)
  • 2
    • 84908657699 scopus 로고    scopus 로고
    • Small-angle neutron scattering reveals the assembly mode and oligomeric architecture of TET, a large, dodecameric aminopeptidase
    • A. Appolaire, E. Girard, M. Colombo, M.A. Durá, M. Moulin, M. Haertlein, and et al. Small-angle neutron scattering reveals the assembly mode and oligomeric architecture of TET, a large, dodecameric aminopeptidase Acta Crystallographica D 70 Pt. 11 2014 2983 2993
    • (2014) Acta Crystallographica D , vol.70 , pp. 2983-2993
    • Appolaire, A.1    Girard, E.2    Colombo, M.3    Durá, M.A.4    Moulin, M.5    Haertlein, M.6
  • 4
    • 58149463865 scopus 로고    scopus 로고
    • An efficient protocol for the complete incorporation of methyl-protonated alanine in perdeuterated protein
    • I. Ayala, R. Sounier, N. Usé, P. Gans, and J. Boisbouvier An efficient protocol for the complete incorporation of methyl-protonated alanine in perdeuterated protein Journal of Biomolecular NMR 43 2 2009 111 119
    • (2009) Journal of Biomolecular NMR , vol.43 , Issue.2 , pp. 111-119
    • Ayala, I.1    Sounier, R.2    Usé, N.3    Gans, P.4    Boisbouvier, J.5
  • 5
    • 0032884573 scopus 로고    scopus 로고
    • Recombinant protein expression in E. Coli
    • F. Baneys Recombinant protein expression in E. coli Current Opinion in Biotechnology 10 1999 411 421
    • (1999) Current Opinion in Biotechnology , vol.10 , pp. 411-421
    • Baneys, F.1
  • 7
    • 70449585313 scopus 로고    scopus 로고
    • Neutron macromolecular crystallography
    • M.P. Blakeley Neutron macromolecular crystallography Crystallography Reviews 15 2009 157 218
    • (2009) Crystallography Reviews , vol.15 , pp. 157-218
    • Blakeley, M.P.1
  • 11
    • 34248580606 scopus 로고    scopus 로고
    • The insertion of the antimicrobial peptide dicynthaurin monomer in model membranes: Thermodynamics and structural characterization
    • F. Bringezu, S. Wen, S. Dante, T. Hauss, M. Majerowicz, and A. Waring The insertion of the antimicrobial peptide dicynthaurin monomer in model membranes: Thermodynamics and structural characterization Biochemistry 46 19 2007 5678 5686
    • (2007) Biochemistry , vol.46 , Issue.19 , pp. 5678-5686
    • Bringezu, F.1    Wen, S.2    Dante, S.3    Hauss, T.4    Majerowicz, M.5    Waring, A.6
  • 12
    • 0035106506 scopus 로고    scopus 로고
    • Physicochemical consequences of the perdeuteriation of glutathione S-Transferase from S. Japonicum
    • D. Brockwell, L. Yu, S. Cooper, S. McCleland, A. Cooper, D. Attwood, and et al. Physicochemical consequences of the perdeuteriation of glutathione S-transferase from S. japonicum Protein Science 10 3 2001 572 580
    • (2001) Protein Science , vol.10 , Issue.3 , pp. 572-580
    • Brockwell, D.1    Yu, L.2    Cooper, S.3    McCleland, S.4    Cooper, A.5    Attwood, D.6
  • 14
    • 34247398259 scopus 로고    scopus 로고
    • Shape and subunit organisation of the DNA methyltransferase M.Ahdl
    • P. Callow, A. Sukhodub, J. Taylor, and G. Kneale Shape and subunit organisation of the DNA methyltransferase M.Ahdl Journal of Molecular Biology 69 1 2007 177 185
    • (2007) Journal of Molecular Biology , vol.69 , Issue.1 , pp. 177-185
    • Callow, P.1    Sukhodub, A.2    Taylor, J.3    Kneale, G.4
  • 16
    • 0014864038 scopus 로고
    • Biosynthesis of deuterated benzylpenicillins. I. Solvent deuterium oxide participation
    • B.C. Carlstedt, H.L. Crespi, M.I. Blake, and J.J. Katz Biosynthesis of deuterated benzylpenicillins. I. Solvent deuterium oxide participation Journal of Pharmaceutical Sciences 59 10 1970 1456 1460
    • (1970) Journal of Pharmaceutical Sciences , vol.59 , Issue.10 , pp. 1456-1460
    • Carlstedt, B.C.1    Crespi, H.L.2    Blake, M.I.3    Katz, J.J.4
  • 17
    • 84904126318 scopus 로고    scopus 로고
    • Heme enzymes. Neutron cryo-crystallography captures the protonation state of ferryl heme in a peroxidase
    • C. Casadei, A. Gumiero, C.L. Metcalfe, E.J. Murphy, J. Basran, M.G. Concilio, and et al. Heme enzymes. Neutron cryo-crystallography captures the protonation state of ferryl heme in a peroxidase Science 345 2014 193 197
    • (2014) Science , vol.345 , pp. 193-197
    • Casadei, C.1    Gumiero, A.2    Metcalfe, C.L.3    Murphy, E.J.4    Basran, J.5    Concilio, M.G.6
  • 19
    • 68449095990 scopus 로고    scopus 로고
    • Deciphering membrane insertion of the diphtheria toxin T domain by specular neutron reflectometry and solid-state NMR spectroscopy
    • A. Chenal, L. Prongidi-Fix, A. Perier, C. Aisenbrey, G. Vernier, S. Lambotte, and et al. Deciphering membrane insertion of the diphtheria toxin T domain by specular neutron reflectometry and solid-state NMR spectroscopy Journal of Molecular Biology 391 5 2009 872 883
    • (2009) Journal of Molecular Biology , vol.391 , Issue.5 , pp. 872-883
    • Chenal, A.1    Prongidi-Fix, L.2    Perier, A.3    Aisenbrey, C.4    Vernier, G.5    Lambotte, S.6
  • 20
    • 76749112920 scopus 로고    scopus 로고
    • Investigation of gamma E-crystallin target protein binding to bovine lens alpha-crystallin by small-angle neutron scattering
    • M.J. Clarke, J.-B. Artero, M. Moulin, P. Callow, J.A. Carver, P.C. Griffiths, and et al. Investigation of gamma E-crystallin target protein binding to bovine lens alpha-crystallin by small-angle neutron scattering Biochimica et Biophysica Acta 1800 3 2010 392 397
    • (2010) Biochimica et Biophysica Acta , vol.1800 , Issue.3 , pp. 392-397
    • Clarke, M.J.1    Artero, J.-B.2    Moulin, M.3    Callow, P.4    Carver, J.A.5    Griffiths, P.C.6
  • 22
    • 84901416016 scopus 로고    scopus 로고
    • Interfacial structure of immobilized antibodies and perdeuterated HSA in model pregnancy tests measured with neutron reflectivity
    • B.J. Cowsill, X. Zhao, T.A. Waigh, S. Eapen, R. Davies, V. Laux, and et al. Interfacial structure of immobilized antibodies and perdeuterated HSA in model pregnancy tests measured with neutron reflectivity Langmuir 30 20 2014 5880 5887
    • (2014) Langmuir , vol.30 , Issue.20 , pp. 5880-5887
    • Cowsill, B.J.1    Zhao, X.2    Waigh, T.A.3    Eapen, S.4    Davies, R.5    Laux, V.6
  • 23
    • 0001078966 scopus 로고
    • Production of foreign proteins in the yeast Pichia pastoris
    • J.M. Cregg, and D.R. Higgins Production of foreign proteins in the yeast Pichia pastoris Canadian Journal of Botany 73 Suppl. 1 1995 S891 S897
    • (1995) Canadian Journal of Botany , vol.73 , pp. S891-S897
    • Cregg, J.M.1    Higgins, D.R.2
  • 24
    • 84872317476 scopus 로고    scopus 로고
    • Near-atomic resolution neutron crystallography on perdeuterated Pyrococcus furiosus rubredoxin: Implication of hydronium ions and protonation state equilibria in redox changes
    • M.G. Cuypers, S.A. Mason, M.P. Blakeley, E.P. Mitchell, M. Haertlein, and V.T. Forsyth Near-atomic resolution neutron crystallography on perdeuterated Pyrococcus furiosus rubredoxin: Implication of hydronium ions and protonation state equilibria in redox changes Angewandte Chemie 52 3 2013 1022 1025
    • (2013) Angewandte Chemie , vol.52 , Issue.3 , pp. 1022-1025
    • Cuypers, M.G.1    Mason, S.A.2    Blakeley, M.P.3    Mitchell, E.P.4    Haertlein, M.5    Forsyth, V.T.6
  • 26
    • 84937605416 scopus 로고    scopus 로고
    • Lipid polyunsaturation determines the extent of membrane structural changes induced by Amphotericin B in Pichia pastoris yeast, BBA
    • A. de Ghellinck, G. Fragneto, V. Laux, M. Haertlein, J. Jouhet, M. Michele Sferrazza, and et al. Lipid polyunsaturation determines the extent of membrane structural changes induced by Amphotericin B in Pichia pastoris yeast, BBA Biomembranes 1848 2015 2317 2325
    • (2015) Biomembranes , vol.1848 , pp. 2317-2325
    • De Ghellinck, A.1    Fragneto, G.2    Laux, V.3    Haertlein, M.4    Jouhet, J.5    Michele Sferrazza, M.6
  • 29
    • 0034805724 scopus 로고    scopus 로고
    • 15N-labeling of the 24-kDa N-terminal domain of the Escherichia coli gyrase B by overexpression in the photoautotrophic cyanobacterium Anabaena sp. PCC 7120
    • 15N-labeling of the 24-kDa N-terminal domain of the Escherichia coli gyrase B by overexpression in the photoautotrophic cyanobacterium Anabaena sp. PCC 7120 Protein Expression and Purification 23 1 2001 207 217
    • (2001) Protein Expression and Purification , vol.23 , Issue.1 , pp. 207-217
    • Desplancq, D.1    Kieffer, B.2    Schmidt, K.3    Posten, C.4    Forster, A.5    Oudet, P.6
  • 32
    • 84933034999 scopus 로고    scopus 로고
    • The pentaplasmic nucleoplasmin fold is present in Drosophila FKBP39 and a large number of chromatin-related proteins
    • C. Edlich-Muth, J.-B. Artero, P. Callow, M.R. Przewloka, A.A. Watson, W. Zhang, and et al. The pentaplasmic nucleoplasmin fold is present in Drosophila FKBP39 and a large number of chromatin-related proteins Journal of Molecular Biology 427 10 2015 1949 1963
    • (2015) Journal of Molecular Biology , vol.427 , Issue.10 , pp. 1949-1963
    • Edlich-Muth, C.1    Artero, J.-B.2    Callow, P.3    Przewloka, M.R.4    Watson, A.A.5    Zhang, W.6
  • 36
    • 42449148364 scopus 로고    scopus 로고
    • An investigation into structural changes due to deuteration
    • S.J. Fisher, and J.R. Helliwell An investigation into structural changes due to deuteration Acta Crystallographica A64 Pt. 3 2008 359 367
    • (2008) Acta Crystallographica , vol.64 A , pp. 359-367
    • Fisher, S.J.1    Helliwell, J.R.2
  • 42
    • 84865127674 scopus 로고    scopus 로고
    • A polymer surfactant corona dynamically replaces water in solvent-free protein liquids and ensures macromolecular flexibility and activity
    • F.X. Gallat, A.P. Brogan, Y. Fichou, N. McGrath, M. Moulin, M. Härtlein, and et al. A polymer surfactant corona dynamically replaces water in solvent-free protein liquids and ensures macromolecular flexibility and activity Journal of the American Chemical Society 134 32 2012 13168 13171
    • (2012) Journal of the American Chemical Society , vol.134 , Issue.32 , pp. 13168-13171
    • Gallat, F.X.1    Brogan, A.P.2    Fichou, Y.3    McGrath, N.4    Moulin, M.5    Härtlein, M.6
  • 43
    • 84863448078 scopus 로고    scopus 로고
    • Dynamical coupling of intrinsically disordered proteins and their hydration water: Comparison with folded soluble and membrane proteins
    • F.X. Gallat, A. Laganowsky, K. Wood, F. Gabel, L. van Eijck, J. Wuttke, and et al. Dynamical coupling of intrinsically disordered proteins and their hydration water: Comparison with folded soluble and membrane proteins Biophysical Journal 103 1 2012 129 136
    • (2012) Biophysical Journal , vol.103 , Issue.1 , pp. 129-136
    • Gallat, F.X.1    Laganowsky, A.2    Wood, K.3    Gabel, F.4    Van Eijck, L.5    Wuttke, J.6
  • 44
    • 0028173324 scopus 로고
    • The production and X-ray structure determination of perdeuterated Staphylococcal nuclease
    • T.R. Gamble, K.R. Clauser, and A.A. Kossiakoff The production and X-ray structure determination of perdeuterated Staphylococcal nuclease Biophysical Chemistry 53 1-2 1994 15 25
    • (1994) Biophysical Chemistry , vol.53 , Issue.1-2 , pp. 15-25
    • Gamble, T.R.1    Clauser, K.R.2    Kossiakoff, A.A.3
  • 45
    • 10844238182 scopus 로고    scopus 로고
    • New insights into the structure of poly(p-phenylene terephthalamide) from neutron fiber diffraction studies
    • K.H. Gardner, A. English, and V.T. Forsyth New insights into the structure of poly(p-phenylene terephthalamide) from neutron fiber diffraction studies Macromolecules 37 2004 9654 9656
    • (2004) Macromolecules , vol.37 , pp. 9654-9656
    • Gardner, K.H.1    English, A.2    Forsyth, V.T.3
  • 47
    • 0347753719 scopus 로고    scopus 로고
    • Use of NMR to study serpin function
    • P.G. Gettins, M. Backovic, and F.C. Peterson Use of NMR to study serpin function Methods 32 2 2004 120 129
    • (2004) Methods , vol.32 , Issue.2 , pp. 120-129
    • Gettins, P.G.1    Backovic, M.2    Peterson, F.C.3
  • 50
    • 84873400562 scopus 로고    scopus 로고
    • Optimized phospholipid bilayer nanodiscs facilitate high-resolution structure determination of membrane proteins
    • F. Hagn, M. Etzkorn, T. Raschle, and G. Wagner Optimized phospholipid bilayer nanodiscs facilitate high-resolution structure determination of membrane proteins Journal of the American Chemical Society 135 5 2013 1919 1925
    • (2013) Journal of the American Chemical Society , vol.135 , Issue.5 , pp. 1919-1925
    • Hagn, F.1    Etzkorn, M.2    Raschle, T.3    Wagner, G.4
  • 52
    • 84938821470 scopus 로고    scopus 로고
    • Binding site asymmetry in human transthyretin: Insights from a joint neutron and X-ray crystallographic analysis using perdeuterated protein
    • M. Haupt, M.P. Blakeley, S.J. Fisher, S.A. Mason, J.B. Cooper, E.P. Mitchell, and et al. Binding site asymmetry in human transthyretin: Insights from a joint neutron and X-ray crystallographic analysis using perdeuterated protein IUCrJ Biology & Medicine 1 2014 429 438
    • (2014) IUCrJ Biology & Medicine , vol.1 , pp. 429-438
    • Haupt, M.1    Blakeley, M.P.2    Fisher, S.J.3    Mason, S.A.4    Cooper, J.B.5    Mitchell, E.P.6
  • 54
    • 32944456230 scopus 로고    scopus 로고
    • High-resolution neutron protein crystallography with radically small crystal volumes: Application of perdeuteration to human aldose reductase
    • I. Hazemann, M.-T. Dauvergne, M.P. Blakeley, F. Meilleur, M. Haertlein, A. Van Dorsselaer, and et al. High-resolution neutron protein crystallography with radically small crystal volumes: Application of perdeuteration to human aldose reductase Acta Crystallographica D 61 2005 1413 1417
    • (2005) Acta Crystallographica D , vol.61 , pp. 1413-1417
    • Hazemann, I.1    Dauvergne, M.-T.2    Blakeley, M.P.3    Meilleur, F.4    Haertlein, M.5    Van Dorsselaer, A.6
  • 55
    • 84886057818 scopus 로고    scopus 로고
    • Adsorption of α-synuclein to supported lipid bilayers: Positioning and role of electrostatics
    • E. Hellstrand, M. Grey, M.L. Ainalem, J. Ankner, V.T. Forsyth, G. Fragneto, and et al. Adsorption of α-synuclein to supported lipid bilayers: Positioning and role of electrostatics ACS Chemical Neuroscience 4 10 2013 1339 1351
    • (2013) ACS Chemical Neuroscience , vol.4 , Issue.10 , pp. 1339-1351
    • Hellstrand, E.1    Grey, M.2    Ainalem, M.L.3    Ankner, J.4    Forsyth, V.T.5    Fragneto, G.6
  • 58
    • 0003939646 scopus 로고
    • Isotopic labeling of specific amino acids as an aid to NMR spectrum assignment of the methionine repressor protein
    • J.J. Villafranca, Academic Press San Diego, CA
    • D.W. Hoffman, and L.D. Spicer Isotopic labeling of specific amino acids as an aid to NMR spectrum assignment of the methionine repressor protein J.J. Villafranca, Techniques in protein chemistry: II 1991 Academic Press San Diego, CA 409 416
    • (1991) Techniques in Protein Chemistry: II , pp. 409-416
    • Hoffman, D.W.1    Spicer, L.D.2
  • 60
    • 0017328923 scopus 로고
    • Comparative neutron small-angle scattering study of small spherical RNA viruses
    • B. Jacrot, C. Chauvin, and J. Witz Comparative neutron small-angle scattering study of small spherical RNA viruses Nature 266 5601 1977 417 421
    • (1977) Nature , vol.266 , Issue.5601 , pp. 417-421
    • Jacrot, B.1    Chauvin, C.2    Witz, J.3
  • 61
    • 47749148081 scopus 로고    scopus 로고
    • In vivo measurement of internal and global macromolecular motions in E. Coli
    • M. Jasnin, M. Moulin, M. Haertlein, G. Zaccai, and M. Tehei In vivo measurement of internal and global macromolecular motions in E. coli Biophysical Journal 95 2 2008 857 864
    • (2008) Biophysical Journal , vol.95 , Issue.2 , pp. 857-864
    • Jasnin, M.1    Moulin, M.2    Haertlein, M.3    Zaccai, G.4    Tehei, M.5
  • 64
    • 0029883811 scopus 로고    scopus 로고
    • In vivo deuteration of transfer RNAs: Overexpression and large-scale purification of deuterated specific tRNAs
    • R. Jünemann, J. Wadzack, F.J. Triana-Alonso, J.U. Bittner, J. Caillet, T. Meinnel, and et al. In vivo deuteration of transfer RNAs: Overexpression and large-scale purification of deuterated specific tRNAs Nucleic Acids Research 24 5 1996 907 913
    • (1996) Nucleic Acids Research , vol.24 , Issue.5 , pp. 907-913
    • Jünemann, R.1    Wadzack, J.2    Triana-Alonso, F.J.3    Bittner, J.U.4    Caillet, J.5    Meinnel, T.6
  • 65
    • 0014012048 scopus 로고
    • Deuterated organisms: Cultivation and uses
    • J.J. Katz, and H.L. Crespi Deuterated organisms: Cultivation and uses Science 151 1966 1187 1194
    • (1966) Science , vol.151 , pp. 1187-1194
    • Katz, J.J.1    Crespi, H.L.2
  • 67
    • 0032923295 scopus 로고    scopus 로고
    • Cell-free production and stable-isotope labeling of milligram quantities of proteins
    • T. Kigawa, T. Yabukia, Y. Yoshida, M. Tsutsuic, Y. Itod, T. Shibatad, and et al. Cell-free production and stable-isotope labeling of milligram quantities of proteins FEBS Letters 442 1999 15 19
    • (1999) FEBS Letters , vol.442 , pp. 15-19
    • Kigawa, T.1    Yabukia, T.2    Yoshida, Y.3    Tsutsuic, M.4    Itod, Y.5    Shibatad, T.6
  • 68
    • 0037731254 scopus 로고    scopus 로고
    • A rapid method to attain isotope labeled small soluble peptides for NMR studies
    • B.W. Koenig, M. Rogowski, and J.M. Louis A rapid method to attain isotope labeled small soluble peptides for NMR studies Journal of Biomolecular NMR 26 3 2003 193 202
    • (2003) Journal of Biomolecular NMR , vol.26 , Issue.3 , pp. 193-202
    • Koenig, B.W.1    Rogowski, M.2    Louis, J.M.3
  • 69
    • 77953546976 scopus 로고    scopus 로고
    • Metal ion roles and the movement of hydrogen during reaction catalyzed by d-xylose isomerase: A joint X-ray and neutron diffraction study
    • A.Y. Kovalevsky, L. Hanson, S.Z. Fisher, M. Mustyakimov, S.A. Mason, V.T. Forsyth, and et al. Metal ion roles and the movement of hydrogen during reaction catalyzed by d-xylose isomerase: a joint X-ray and neutron diffraction study Structure 18 6 2010 688 699
    • (2010) Structure , vol.18 , Issue.6 , pp. 688-699
    • Kovalevsky, A.Y.1    Hanson, L.2    Fisher, S.Z.3    Mustyakimov, M.4    Mason, S.A.5    Forsyth, V.T.6
  • 71
    • 33748517209 scopus 로고    scopus 로고
    • Design of a bacterial host for site-specific incorporation of p-bromophenylalanine into recombinant proteins
    • I. Kwon, P. Wang, and D.A. Tirrell Design of a bacterial host for site-specific incorporation of p-bromophenylalanine into recombinant proteins Journal of the American Chemical Society 128 36 2006 11778 11783
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.36 , pp. 11778-11783
    • Kwon, I.1    Wang, P.2    Tirrell, D.A.3
  • 73
    • 84946560131 scopus 로고    scopus 로고
    • Production, crystallization, and neutron diffraction of fully deuterated human myelin peripheral membrane protein P2
    • S. Laulumaa, M.P. Blakeley, A. Raasakka, M. Moulin, M. Härtlein, and P. Petri Kursula Production, crystallization, and neutron diffraction of fully deuterated human myelin peripheral membrane protein P2 Acta Crystallographica F 71 2015 1391 1395
    • (2015) Acta Crystallographica F , vol.71 , pp. 1391-1395
    • Laulumaa, S.1    Blakeley, M.P.2    Raasakka, A.3    Moulin, M.4    Härtlein, M.5    Petri Kursula, P.6
  • 74
    • 45849138919 scopus 로고    scopus 로고
    • Selective deuteration of tryptophan and methionine residues in maltose binding protein: A model system for neutron scattering
    • V. Laux, P. Callow, D.I. Svergun, P.A. Timmins, V.T. Forsyth, and M. Haertlein Selective deuteration of tryptophan and methionine residues in maltose binding protein: A model system for neutron scattering European Biophysics Journal 37 6 2008 815 822
    • (2008) European Biophysics Journal , vol.37 , Issue.6 , pp. 815-822
    • Laux, V.1    Callow, P.2    Svergun, D.I.3    Timmins, P.A.4    Forsyth, V.T.5    Haertlein, M.6
  • 75
    • 0029196090 scopus 로고
    • A novel method for selective isotope labeling of bacterially expressed proteins
    • K.M. Lee, E.J. Androphy, and J.D. Baleja A novel method for selective isotope labeling of bacterially expressed proteins Journal of Biomolecular NMR 5 1 1995 93 96
    • (1995) Journal of Biomolecular NMR , vol.5 , Issue.1 , pp. 93-96
    • Lee, K.M.1    Androphy, E.J.2    Baleja, J.D.3
  • 76
    • 0032534788 scopus 로고    scopus 로고
    • Predictable deuteration of recombinant protein in Escherichia coli
    • B. Leiting, F. Marsilio, and J.F. O'Connell Predictable deuteration of recombinant protein in Escherichia coli Analytical Biochemistry 265 1998 351 355
    • (1998) Analytical Biochemistry , vol.265 , pp. 351-355
    • Leiting, B.1    Marsilio, F.2    O'Connell, J.F.3
  • 77
    • 84902590056 scopus 로고    scopus 로고
    • Limitations in the use of surface tension and the Gibbs equation to determine surface excesses of cationic surfactants
    • P.X. Li, R.K. Thomas, and J. Penfold Limitations in the use of surface tension and the Gibbs equation to determine surface excesses of cationic surfactants Langmuir 30 23 2014 6739 6747
    • (2014) Langmuir , vol.30 , Issue.23 , pp. 6739-6747
    • Li, P.X.1    Thomas, R.K.2    Penfold, J.3
  • 78
    • 0037306147 scopus 로고    scopus 로고
    • Role of side-chain conformational entropy in transmembrane helix dimerization of glycophorin A
    • W. Liu, E. Crocker, D.J. Siminovitch, and S.O. Smith Role of side-chain conformational entropy in transmembrane helix dimerization of glycophorin A Biophysical Journal 84 2 Pt. 1 2003 1263 1271
    • (2003) Biophysical Journal , vol.84 , Issue.2 , pp. 1263-1271
    • Liu, W.1    Crocker, E.2    Siminovitch, D.J.3    Smith, S.O.4
  • 79
    • 0028988375 scopus 로고
    • Site-directed isotope labeling and ATR-FTIR difference spectroscopy of bacteriorhodopsin: The peptide carbonyl group of Tyr 185 is structurally active during the bR→N transition
    • C.F. Ludlam, S. Sonar, C.P. Lee, M. Coleman, J. Herzfeld, U.L. RajBhandary, and et al. Site-directed isotope labeling and ATR-FTIR difference spectroscopy of bacteriorhodopsin: The peptide carbonyl group of Tyr 185 is structurally active during the bR→N transition Biochemistry 34 1 1995 2 6
    • (1995) Biochemistry , vol.34 , Issue.1 , pp. 2-6
    • Ludlam, C.F.1    Sonar, S.2    Lee, C.P.3    Coleman, M.4    Herzfeld, J.5    RajBhandary, U.L.6
  • 80
    • 0022743221 scopus 로고
    • Time-resolved X-ray diffraction studies of the B to D structural transition in the DNA double helix
    • A. Mahendrasingam, V.T. Forsyth, R. Hussain, R.J. Greenall, W.J. Pigram, and W. Fuller Time-resolved X-ray diffraction studies of the B to D structural transition in the DNA double helix Science 233 1986 195 197
    • (1986) Science , vol.233 , pp. 195-197
    • Mahendrasingam, A.1    Forsyth, V.T.2    Hussain, R.3    Greenall, R.J.4    Pigram, W.J.5    Fuller, W.6
  • 82
    • 84925535388 scopus 로고    scopus 로고
    • Biosynthetic preparation of selectively deuterated phosphatidylcholine in genetically modified Escherichia coli
    • S. Maric, M.B. Thygesen, J. Schiller, M. Marek, M. Moulin, M. Haertlein, and et al. Biosynthetic preparation of selectively deuterated phosphatidylcholine in genetically modified Escherichia coli Applied Microbiology and Biotechnology 99 1 2015 241 254
    • (2015) Applied Microbiology and Biotechnology , vol.99 , Issue.1 , pp. 241-254
    • Maric, S.1    Thygesen, M.B.2    Schiller, J.3    Marek, M.4    Moulin, M.5    Haertlein, M.6
  • 83
    • 84954377871 scopus 로고    scopus 로고
    • Expression and purification of deuterated proteins for neutron crystallography, Chapter 1, 47-60
    • N. Nimura, H. Mizuno, J.R. Helliwell, E. Westhof, Proceedings of Symposium on Development of New Structural Biology including Hydrogen and Hydration, Mito, Japan (2000)
    • H. Masuda, M.S.R.C. Murthy, K. Suto, Y. Takenaka, P.K.R. Kumar, and H. Mizuno Expression and purification of deuterated proteins for neutron crystallography, Chapter 1, 47-60 N. Nimura, H. Mizuno, J.R. Helliwell, E. Westhof, Hydrogen- and hydration-sensitive structural biology Proceedings of Symposium on Development of New Structural Biology including Hydrogen and Hydration, Mito, Japan (2000) 2005
    • (2005) Hydrogen- And Hydration-sensitive Structural Biology
    • Masuda, H.1    Murthy, M.S.R.C.2    Suto, K.3    Takenaka, Y.4    Kumar, P.K.R.5    Mizuno, H.6
  • 84
    • 0026533909 scopus 로고
    • Inter-protein distances within the large subunit from Escherichia coli ribosomes
    • R.P. May, V. Nowotny, P. Nowotny, H. Voss, and K.H. Nierhaus Inter-protein distances within the large subunit from Escherichia coli ribosomes EMBO Journal 11 1991 373 378
    • (1991) EMBO Journal , vol.11 , pp. 373-378
    • May, R.P.1    Nowotny, V.2    Nowotny, P.3    Voss, H.4    Nierhaus, K.H.5
  • 86
    • 40249114708 scopus 로고    scopus 로고
    • X-ray and neutron small-angle scattering analysis of the complex formed by the met receptor and the Listeria monocytogenes invasion protein InlB
    • H.H. Niemann, M.V. Petoukhov, M. Härtlein, M. Moulin, E. Gherardi, P. Timmins, and et al. X-ray and neutron small-angle scattering analysis of the complex formed by the met receptor and the Listeria monocytogenes invasion protein InlB Journal of Molecular Biology 377 2 2008 489 500
    • (2008) Journal of Molecular Biology , vol.377 , Issue.2 , pp. 489-500
    • Niemann, H.H.1    Petoukhov, M.V.2    Härtlein, M.3    Moulin, M.4    Gherardi, E.5    Timmins, P.6
  • 89
    • 53549094650 scopus 로고    scopus 로고
    • Dynamical signature of protein hydration water reveals two populations of amorphous ice like behavior
    • A. Paciaroni, A. Orecchini, E. Cornicchi, M. Marconi, C. Petrillo, M. Haertlein, and et al. Dynamical signature of protein hydration water reveals two populations of amorphous ice like behavior Physical Review Letters 101 14 2008 148104
    • (2008) Physical Review Letters , vol.101 , Issue.14 , pp. 148104
    • Paciaroni, A.1    Orecchini, A.2    Cornicchi, E.3    Marconi, M.4    Petrillo, C.5    Haertlein, M.6
  • 91
    • 0037270065 scopus 로고    scopus 로고
    • Improved methods of cultivation and production of deuteriated proteins from E. Coli strains grown on fully deuteriated minimal medium
    • D. Paliy, D.B. Bloor, P. Gilbert, and J. Barber Improved methods of cultivation and production of deuteriated proteins from E. coli strains grown on fully deuteriated minimal medium Journal of Applied Microbiology 94 4 2003 580 586
    • (2003) Journal of Applied Microbiology , vol.94 , Issue.4 , pp. 580-586
    • Paliy, D.1    Bloor, D.B.2    Gilbert, P.3    Barber, J.4
  • 92
    • 0002659282 scopus 로고    scopus 로고
    • Towards structural investigations on isotope labelled native bacteriorhodopsin in detergent micelles by solution-state NMR spectroscopy
    • H. Patzelt, A.S. Ulrich, H. Egbringhoff, P. Düx, Ashurst J., B. Simon, and et al. Towards structural investigations on isotope labelled native bacteriorhodopsin in detergent micelles by solution-state NMR spectroscopy Journal of Biomolecular NMR 10 1997 95 106
    • (1997) Journal of Biomolecular NMR , vol.10 , pp. 95-106
    • Patzelt, H.1    Ulrich, A.S.2    Egbringhoff, H.3    Düx, P.4    Ashurst, J.5    Simon, B.6
  • 93
    • 84906213542 scopus 로고    scopus 로고
    • Impact of the degree of ethoxylation of the ethoxylated polysorbate nonionic surfactant on the surface self-assembly of hydrophobin-ethoxylated polysorbate surfactant mixtures
    • J. Penfold, R.K. Thomas, P. Li, J.T. Petkov, I. Tucker, A.R. Cox, and et al. Impact of the degree of ethoxylation of the ethoxylated polysorbate nonionic surfactant on the surface self-assembly of hydrophobin-ethoxylated polysorbate surfactant mixtures Langmuir 30 32 2014 9741 9751
    • (2014) Langmuir , vol.30 , Issue.32 , pp. 9741-9751
    • Penfold, J.1    Thomas, R.K.2    Li, P.3    Petkov, J.T.4    Tucker, I.5    Cox, A.R.6
  • 94
    • 84925238571 scopus 로고    scopus 로고
    • Adsorption at air-water and oil-water interfaces and self-assembly in aqueous solution of ethoxylated polysorbate nonionic surfactants
    • J. Penfold, R.K. Thomas, P.X. Li, J.T. Petkov, I. Tucker, J.R.P. Webster, and et al. Adsorption at air-water and oil-water interfaces and self-assembly in aqueous solution of ethoxylated polysorbate nonionic surfactants Langmuir 31 10 2015 3003 3011
    • (2015) Langmuir , vol.31 , Issue.10 , pp. 3003-3011
    • Penfold, J.1    Thomas, R.K.2    Li, P.X.3    Petkov, J.T.4    Tucker, I.5    Webster, J.R.P.6
  • 95
    • 84935015679 scopus 로고    scopus 로고
    • Multivalent-counterion-induced surfactant multilayer formation at hydrophobic and hydrophilic solid-solution interfaces
    • J. Penfold, R.K. Thomas, P. Li, H. Xu, I.M. Tucker, J.T. Petkov, and et al. Multivalent-counterion-induced surfactant multilayer formation at hydrophobic and hydrophilic solid-solution interfaces Langmuir 31 24 2015 6773 6781
    • (2015) Langmuir , vol.31 , Issue.24 , pp. 6773-6781
    • Penfold, J.1    Thomas, R.K.2    Li, P.3    Xu, H.4    Tucker, I.M.5    Petkov, J.T.6
  • 96
    • 0019630079 scopus 로고
    • Estimation of deuteration levels in whole cells and cellular proteins by 1H NMR spectroscopy and neutron scattering
    • S.J. Perkins Estimation of deuteration levels in whole cells and cellular proteins by 1H NMR spectroscopy and neutron scattering Biochemical Journal 199 1981 163 170
    • (1981) Biochemical Journal , vol.199 , pp. 163-170
    • Perkins, S.J.1
  • 97
    • 64149132142 scopus 로고    scopus 로고
    • Perdeuteration, purification, crystallization and preliminary neutron diffraction of an ocean pout type III antifreeze protein
    • I. Petit-Haertlein, M.P. Blakeley, E. Howard, I. Hazemann, A. Mitschler, M. Haertlein, and et al. Perdeuteration, purification, crystallization and preliminary neutron diffraction of an ocean pout type III antifreeze protein Acta Crystallographica F 65 4 2009 406 409
    • (2009) Acta Crystallographica F , vol.65 , Issue.4 , pp. 406-409
    • Petit-Haertlein, I.1    Blakeley, M.P.2    Howard, E.3    Hazemann, I.4    Mitschler, A.5    Haertlein, M.6
  • 98
    • 77953151173 scopus 로고    scopus 로고
    • Incorporation of methyl-protonated valine and leucine residues into deuterated ocean pout Type III anti-freeze protein: Expression, crystallization and preliminary neutron diffraction studies
    • I. Petit-Haertlein, M.P. Blakeley, E. Howard, I. Hazemann, A. Mitschler, A. Podjarny, and et al. Incorporation of methyl-protonated valine and leucine residues into deuterated ocean pout Type III anti-freeze protein: Expression, crystallization and preliminary neutron diffraction studies Acta Crystallographica F 66 6 2010 665 669
    • (2010) Acta Crystallographica F , vol.66 , Issue.6 , pp. 665-669
    • Petit-Haertlein, I.1    Blakeley, M.P.2    Howard, E.3    Hazemann, I.4    Mitschler, A.5    Podjarny, A.6
  • 99
    • 0041524233 scopus 로고    scopus 로고
    • A novel method for the biosynthesis of deuterated proteins with selective protonation at the aromatic rings of Phe, Tyr and Trp
    • S. Rajesh, D. Nietlispach, H. Nakayama, K. Takio, E.D. Laue, T. Shibata, and et al. A novel method for the biosynthesis of deuterated proteins with selective protonation at the aromatic rings of Phe, Tyr and Trp Biomolecular NMR 27 1 2003 81 86
    • (2003) Biomolecular NMR , vol.27 , Issue.1 , pp. 81-86
    • Rajesh, S.1    Nietlispach, D.2    Nakayama, H.3    Takio, K.4    Laue, E.D.5    Shibata, T.6
  • 102
    • 79951556764 scopus 로고    scopus 로고
    • Observing selected domains in multi-domain proteins via sortase-mediated ligation and NMR spectroscopy
    • M.A. Refaei, A. Combs, D.J. Kojetin, J. Cavanagh, C. Caperelli, M. Rance, and et al. Observing selected domains in multi-domain proteins via sortase-mediated ligation and NMR spectroscopy Journal of Biomolecular NMR 49 1 2011 3 7
    • (2011) Journal of Biomolecular NMR , vol.49 , Issue.1 , pp. 3-7
    • Refaei, M.A.1    Combs, A.2    Kojetin, D.J.3    Cavanagh, J.4    Caperelli, C.5    Rance, M.6
  • 104
    • 0035834055 scopus 로고    scopus 로고
    • Expression, purification, characterization, and NMR studies of highly deuterated recombinant cytochrome c peroxidase
    • M.I. Savenkova, J.D. Satterlee, J.E. Erman, W.F. Siems, and G.L. Helms Expression, purification, characterization, and NMR studies of highly deuterated recombinant cytochrome c peroxidase Biochemistry 40 40 2001 12123 12131
    • (2001) Biochemistry , vol.40 , Issue.40 , pp. 12123-12131
    • Savenkova, M.I.1    Satterlee, J.D.2    Erman, J.E.3    Siems, W.F.4    Helms, G.L.5
  • 105
    • 84862513968 scopus 로고    scopus 로고
    • Water in crystalline fibers of dihydrate beta-chitin results in unexpected absence of intramolecular hydrogen bonding
    • D. Sawada, Y. Nishiyama, P. Langan, V.T. Forsyth, S. Kimura, and M. Wada Water in crystalline fibers of dihydrate beta-chitin results in unexpected absence of intramolecular hydrogen bonding PLoS One 7 6 2012 e39376
    • (2012) PLoS One , vol.7 , Issue.6 , pp. e39376
    • Sawada, D.1    Nishiyama, Y.2    Langan, P.3    Forsyth, V.T.4    Kimura, S.5    Wada, M.6
  • 106
    • 84881024298 scopus 로고    scopus 로고
    • Structure and dynamics of a complex of cellulose with EDA: Insights into the action of amines on cellulose
    • D. Sawada, Y. Nishiyama, L. Petridis, R. Parthasarathi, S. Gnanakaran, V.T. Forsyth, and et al. Structure and dynamics of a complex of cellulose with EDA: Insights into the action of amines on cellulose Cellulose 20 2013 1563 1571
    • (2013) Cellulose , vol.20 , pp. 1563-1571
    • Sawada, D.1    Nishiyama, Y.2    Petridis, L.3    Parthasarathi, R.4    Gnanakaran, S.5    Forsyth, V.T.6
  • 107
    • 84928819941 scopus 로고    scopus 로고
    • Translational diffusion of hydration water correlates with functional motions in folded and intrinsically disordered proteins
    • G. Schirò, Y. Fichou, F.-X. Gallat, K. Wood, F. Gabel, M. Moulin, and et al. Translational diffusion of hydration water correlates with functional motions in folded and intrinsically disordered proteins Nature Communications 16 6 2015 6490
    • (2015) Nature Communications , vol.16 , Issue.6 , pp. 6490
    • Schirò, G.1    Fichou, Y.2    Gallat, F.-X.3    Wood, K.4    Gabel, F.5    Moulin, M.6
  • 108
    • 84888366317 scopus 로고    scopus 로고
    • Neutron reflectometry elucidates density profiles of deuterated proteins adsorbed onto surfaces displaying poly(ethylene glycol) brushes: Evidence for primary adsorption
    • E. Schneck, A. Schollier, A. Halperin, M. Moulin, M. Härtlein, M. Sferrazza, and et al. Neutron reflectometry elucidates density profiles of deuterated proteins adsorbed onto surfaces displaying poly(ethylene glycol) brushes: Evidence for primary adsorption Langmuir 29 46 2013 14178 14187
    • (2013) Langmuir , vol.29 , Issue.46 , pp. 14178-14187
    • Schneck, E.1    Schollier, A.2    Halperin, A.3    Moulin, M.4    Härtlein, M.5    Sferrazza, M.6
  • 109
    • 74949100466 scopus 로고    scopus 로고
    • Structural insights into substrate specificity and the anti beta-elimination mechanism of pectate lyase
    • A. Seyedarabi, T.-T. To, S. Ali, S. Hussain, M. Fries, R. Madsen, and et al. Structural insights into substrate specificity and the anti beta-elimination mechanism of pectate lyase Biochemistry 49 3 2010 539 546
    • (2010) Biochemistry , vol.49 , Issue.3 , pp. 539-546
    • Seyedarabi, A.1    To, T.-T.2    Ali, S.3    Hussain, S.4    Fries, M.5    Madsen, R.6
  • 113
    • 79951471489 scopus 로고    scopus 로고
    • Small-angle scattering from phospholipid nanodiscs: Derivation and refinement of a molecular constrained analytical model form factor
    • N. Skar-Gislinge, and L. Arleth Small-angle scattering from phospholipid nanodiscs: Derivation and refinement of a molecular constrained analytical model form factor Physical Chemistry Chemical Physics 13 8 2011 3161 3170
    • (2011) Physical Chemistry Chemical Physics , vol.13 , Issue.8 , pp. 3161-3170
    • Skar-Gislinge, N.1    Arleth, L.2
  • 114
    • 77649188879 scopus 로고    scopus 로고
    • Recent advances in segmental isotope labeling of proteins: NMR applications to large proteins and glycoproteins
    • L. Skrisovska, M. Schubert, and F.H. Allain Recent advances in segmental isotope labeling of proteins: NMR applications to large proteins and glycoproteins Journal of Biomolecular NMR 46 1 2009 51 65
    • (2009) Journal of Biomolecular NMR , vol.46 , Issue.1 , pp. 51-65
    • Skrisovska, L.1    Schubert, M.2    Allain, F.H.3
  • 116
    • 20044376278 scopus 로고    scopus 로고
    • Protocols for production of selenomethionine-labeled proteins in 2-L polyethylene terephthalate bottles using auto-induction medium
    • H.K. Sreenath, C.A. Bingman, B.W. Buchan, K.D. Seder, B.T. Burns, H.V. Geetha, and et al. Protocols for production of selenomethionine-labeled proteins in 2-L polyethylene terephthalate bottles using auto-induction medium Protein Expression and Purification 40 2 2005 256 267
    • (2005) Protein Expression and Purification , vol.40 , Issue.2 , pp. 256-267
    • Sreenath, H.K.1    Bingman, C.A.2    Buchan, B.W.3    Seder, K.D.4    Burns, B.T.5    Geetha, H.V.6
  • 117
    • 0038386883 scopus 로고    scopus 로고
    • Amino-acid-type selective isotope labeling of proteins expressed in Baculovirus-infected insect cells useful for NMR studies
    • A. Strauss, F. Bitsch, B. Cutting, G. Fendrich, P. Graff, J. Liebetanz, and et al. Amino-acid-type selective isotope labeling of proteins expressed in Baculovirus-infected insect cells useful for NMR studies Journal of Biomolecular NMR 26 4 2003 367 372
    • (2003) Journal of Biomolecular NMR , vol.26 , Issue.4 , pp. 367-372
    • Strauss, A.1    Bitsch, F.2    Cutting, B.3    Fendrich, G.4    Graff, P.5    Liebetanz, J.6
  • 118
    • 0242710958 scopus 로고    scopus 로고
    • Selenomethionine and selenocysteine double labeling strategy for crystallographic phasing
    • M.P. Strub, F. Hoh, J.F. Sanchez, J.M. Strub, A. Bock, A. Aumelas, and et al. Selenomethionine and selenocysteine double labeling strategy for crystallographic phasing Structure 11 11 2003 1359 1367
    • (2003) Structure , vol.11 , Issue.11 , pp. 1359-1367
    • Strub, M.P.1    Hoh, F.2    Sanchez, J.F.3    Strub, J.M.4    Bock, A.5    Aumelas, A.6
  • 120
    • 0033152987 scopus 로고    scopus 로고
    • Application of fed-batch fermentation to the preparation of isotopically labelled or selenomethionyl-labelled proteins
    • J.M. Studts, and B.G. Fox Application of fed-batch fermentation to the preparation of isotopically labelled or selenomethionyl-labelled proteins Protein Expression and Purification 16 1 1999 109 119
    • (1999) Protein Expression and Purification , vol.16 , Issue.1 , pp. 109-119
    • Studts, J.M.1    Fox, B.G.2
  • 125
    • 7444237598 scopus 로고    scopus 로고
    • Production and preliminary analysis of perdeuterated yeast inorganic pyrophosphatase crystals suitable for neutron diffraction
    • V.U. Tuominen, D. Myles, M.-T. Dauvergne, R. Lahti, P. Heikinheimo, and A. Goldman Production and preliminary analysis of perdeuterated yeast inorganic pyrophosphatase crystals suitable for neutron diffraction Acta Crystallographica D60 3 2004 606 609
    • (2004) Acta Crystallographica , vol.60 D , Issue.3 , pp. 606-609
    • Tuominen, V.U.1    Myles, D.2    Dauvergne, M.-T.3    Lahti, R.4    Heikinheimo, P.5    Goldman, A.6
  • 126
    • 0027177825 scopus 로고
    • Large-scale preparation of fully deuterated cell components: Ribosomes from Escherichia coli with high biological activity
    • K. Vanatalu, T. Paalme, R. Vilu, N. Burkhardt, R. Junemann, R. May, and et al. Large-scale preparation of fully deuterated cell components: Ribosomes from Escherichia coli with high biological activity European Journal of Biochemistry 216 1 1993 315 321
    • (1993) European Journal of Biochemistry , vol.216 , Issue.1 , pp. 315-321
    • Vanatalu, K.1    Paalme, T.2    Vilu, R.3    Burkhardt, N.4    Junemann, R.5    May, R.6
  • 129
    • 79960284070 scopus 로고    scopus 로고
    • Mammalian pyruvate dehydrogenase complex E2/E3BP core organization: A new variable composition model
    • S. Vijayakrishnan, P. Callow, M.A. Nutley, D. McGow, D. Gilbert, P. Kropholler, and et al. Mammalian pyruvate dehydrogenase complex E2/E3BP core organization: A new variable composition model Biochemical Journal 437 2011 565 574
    • (2011) Biochemical Journal , vol.437 , pp. 565-574
    • Vijayakrishnan, S.1    Callow, P.2    Nutley, M.A.3    McGow, D.4    Gilbert, D.5    Kropholler, P.6
  • 133
    • 41849097415 scopus 로고    scopus 로고
    • Coincidence of dynamical transitions in a soluble protein and its hydration water: Direct measurements by neutron scattering and MD simulations
    • K. Wood, A. Froelich, A. Paciaroni, M. Moulin, M. Härtlein, G. Zaccai, and et al. Coincidence of dynamical transitions in a soluble protein and its hydration water: Direct measurements by neutron scattering and MD simulations Journal of the American Chemical Society 130 14 2008 4586 4587
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.14 , pp. 4586-4587
    • Wood, K.1    Froelich, A.2    Paciaroni, A.3    Moulin, M.4    Härtlein, M.5    Zaccai, G.6
  • 134
    • 84871944566 scopus 로고    scopus 로고
    • Protein surface and core dynamics show concerted hydration-dependent activation
    • K. Wood, F.X. Gallat, R. Otten, A.J. van Heel, M. Lethier, L. van Eijck, and et al. Protein surface and core dynamics show concerted hydration-dependent activation Angewandte Chemie 52 2 2013 665 668
    • (2013) Angewandte Chemie , vol.52 , Issue.2 , pp. 665-668
    • Wood, K.1    Gallat, F.X.2    Otten, R.3    Van Heel, A.J.4    Lethier, M.5    Van Eijck, L.6
  • 137
    • 0032036838 scopus 로고    scopus 로고
    • Dual amino acid-selective and site-directed stable-isotope labeling of the human c-Ha-Ras protein by cell-free synthesis
    • T. Yabuki, T. Kigawa, N. Dohmae, K. Takio, T. Terada, Y. Ito, and et al. Dual amino acid-selective and site-directed stable-isotope labeling of the human c-Ha-Ras protein by cell-free synthesis Journal of Biomolecular NMR 11 3 1998 295 306
    • (1998) Journal of Biomolecular NMR , vol.11 , Issue.3 , pp. 295-306
    • Yabuki, T.1    Kigawa, T.2    Dohmae, N.3    Takio, K.4    Terada, T.5    Ito, Y.6
  • 138
    • 78751584932 scopus 로고    scopus 로고
    • Neutron scattering experiments for protein dynamics
    • G. Zaccai Neutron scattering experiments for protein dynamics Journal of Non-Crystalline Solids 357 2011 615 621
    • (2011) Journal of Non-Crystalline Solids , vol.357 , pp. 615-621
    • Zaccai, G.1
  • 139
    • 77953371403 scopus 로고    scopus 로고
    • Effect of crowding on the conformation of interwound DNA strands from neutron scattering measurements and Monte Carlo simulations
    • X. Zhu, S.Y. Ng, A.N. Gupta, Y.P. Feng, B. Ho, A. Lapp, and et al. Effect of crowding on the conformation of interwound DNA strands from neutron scattering measurements and Monte Carlo simulations Physical Review E 81 2010 061905
    • (2010) Physical Review E , vol.81 , pp. 061905
    • Zhu, X.1    Ng, S.Y.2    Gupta, A.N.3    Feng, Y.P.4    Ho, B.5    Lapp, A.6


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