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Volumn 1834, Issue 9, 2013, Pages 1910-1922

Volumetric properties underlying ligand binding in a monomeric hemoglobin: A high-pressure NMR study

Author keywords

Coevolution; Functional cavity; High pressure NMR; Local disorder; Protein compressibility; Truncated hemoglobin

Indexed keywords

CYANIDE; HEMOGLOBIN; HISTIDINE; MONOMER; TRUNCATED HEMOGLOBIN;

EID: 84884638449     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2013.04.016     Document Type: Article
Times cited : (12)

References (78)
  • 1
  • 2
    • 0014030651 scopus 로고
    • An X-ray study of azide methaemoglobin
    • M.F. Perutz, F.S. Mathews, An X-ray study of azide methaemoglobin, J. Mol. Biol. 21 (1966) 199-202.
    • (1966) J. Mol. Biol. , vol.21 , pp. 199-202
    • Perutz, M.F.1    Mathews, F.S.2
  • 3
    • 77953655511 scopus 로고    scopus 로고
    • Straight-chain alkyl isocyanides open the distal histidine gate in crystal structures of myoglobin
    • R.D. Smith, G.C. Blouin, K.A. Johnson, G.N. Phillips Jr., J.S. Olson, Straight-chain alkyl isocyanides open the distal histidine gate in crystal structures of myoglobin, Biochemistry 49 (2010) 4977-4986.
    • (2010) Biochemistry , vol.49 , pp. 4977-4986
    • Smith, R.D.1    Blouin, G.C.2    Johnson, K.A.3    Phillips Jr., G.N.4    Olson, J.S.5
  • 6
    • 84877806490 scopus 로고    scopus 로고
    • Hemoglobin, a nitric-oxide dioxygenase
    • (Article ID 683729)
    • P.R. Gardner, Hemoglobin, a nitric-oxide dioxygenase, Scientifica 2012 (2012), (Article ID 683729).
    • (2012) Scientifica , vol.2012
    • Gardner, P.R.1
  • 7
    • 0037018935 scopus 로고    scopus 로고
    • Truncated hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002: Evidence for hexacoordination and covalent adduct formation in the ferric recombinant protein
    • DOI 10.1021/bi025609m
    • N.L Scott, C.J. Falzone, D.A. Vuletich, J. Zhao, D.A. Bryant, J.T.J. Lecomte, The hemoglobin of the cyanobacterium Synechococcus sp. PCC 7002: evidence for hexacoordination and covalent adduct formation in the ferric recombinant protein, Biochemistry 41 (2002) 6902-6910. (Pubitemid 34575661)
    • (2002) Biochemistry , vol.41 , Issue.22 , pp. 6902-6910
    • Scott, N.L.1    Falzone, C.J.2    Vuletich, D.A.3    Zhao, J.4    Bryant, D.A.5    Lecomte, J.T.J.6
  • 9
    • 0034213366 scopus 로고    scopus 로고
    • A novel two-over-two alpha-helical sandwich fold is characteristic of the truncated hemoglobin family
    • A Pesce, M. Couture, S. Dewilde, M. Guertin, K. Yamauchi, P. Ascenzi, L. Moens, M. Bolognesi, A novel two-over-two α-helical sandwich fold is characteristic of the truncated hemoglobin family, EMBO J. 19 (2000) 2424-2434. (Pubitemid 30323532)
    • (2000) EMBO Journal , vol.19 , Issue.11 , pp. 2424-2434
    • Pesce, A.1    Couture, M.2    Dewilde, S.3    Guertin, M.4    Yamauchi, K.5    Ascenzi, P.6    Moens, L.7    Bolognesi, M.8
  • 10
    • 3843100441 scopus 로고    scopus 로고
    • Crystallographic analysis of Synechocystis cyanoglobin reveals the structural changes accompanying ligand binding in a hexacoordinate hemoglobin
    • DOI 10.1016/j.jmb.2004.05.070, PII S0022283604006515
    • J.T. Trent III, S. Kundu, JA Hoy, M.S. Hargrove, Crystallographic analysis of synechocystis cyanoglobin reveals the structural changes accompanying ligand binding in a hexacoordinate hemoglobin, J. Mol. Biol. 341 (2004) 1097-1108. (Pubitemid 39037366)
    • (2004) Journal of Molecular Biology , vol.341 , Issue.4 , pp. 1097-1108
    • Trent III, J.T.1    Kundu, S.2    Hoy, J.A.3    Hargrove, M.S.4
  • 11
    • 0037059826 scopus 로고    scopus 로고
    • Truncated hemoglobins: A new family of hemoglobins widely distributed in bacteria, unicellular eukaryotes, and plants
    • DOI 10.1074/jbc.R100058200
    • J.B. Wittenberg, M. Bolognesi, B.A. Wittenberg, M. Guertin, Truncated hemoglobins: a new family of hemoglobins widely distributed in bacteria, unicellular eukaryotes, and plants, J. Biol. Chem 277 (2002) 871-874. (Pubitemid 34968827)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.2 , pp. 871-874
    • Wittenberg, J.B.1    Bolognesi, M.2    Wittenberg, B.A.3    Guertin, M.4
  • 13
    • 0000725483 scopus 로고
    • Thermodynamic fluctuations in protein molecules
    • A. Cooper, Thermodynamic fluctuations in protein molecules, Proc. Natl. Acad. Sci. U. S. A. 73 (1976) 2740-2741.
    • (1976) Proc. Natl. Acad. Sci. U. S. A. , vol.73 , pp. 2740-2741
    • Cooper, A.1
  • 14
    • 33751584771 scopus 로고    scopus 로고
    • Structural and dynamic repercussions of heme binding and heme-protein cross-linking in Synechococcus sp. PCC 7002 hemoglobin
    • DOI 10.1021/bi061532g
    • DA Vuletich, C.J. Falzone, J.T.J. Lecomte, Structural and dynamic repercussions of heme binding and heme-protein cross-linking in Synechococcus sp. PCC 7002 hemoglobin, Biochemistry 45 (2006) 14075-14084. (Pubitemid 44846196)
    • (2006) Biochemistry , vol.45 , Issue.47 , pp. 14075-14084
    • Vuletich, D.A.1    Falzone, C.J.2    Lecomte, J.T.J.3
  • 15
    • 70449523232 scopus 로고    scopus 로고
    • 13C resonance assignments of the 2/2 hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002 in the ferric bis-histidine state
    • 13C resonance assignments of the 2/2 hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002 in the ferric bis-histidine state, Biomol. NMR Assign. 3 (2009) 211-214
    • (2009) Biomol. NMR Assign. , vol.3 , pp. 211-214
    • Pond, M.P.1    Vuletich, D.A.2    Falzone, C.J.3    Majumdar, A.4    Lecomte, J.T.J.5
  • 16
    • 84864274190 scopus 로고    scopus 로고
    • Influence of heme post-translational modification and distal ligation on the backbone dynamics of a monomeric hemoglobin
    • M.P. Pond, A. Majumdar, J.T.J. Lecomte, Influence of heme post-translational modification and distal ligation on the backbone dynamics of a monomeric hemoglobin, Biochemistry 51 (2012) 5733-5747.
    • (2012) Biochemistry , vol.51 , pp. 5733-5747
    • Pond, M.P.1    Majumdar, A.2    Lecomte, J.T.J.3
  • 17
    • 0025655698 scopus 로고
    • Selective excitation techniques for water suppression in one- and two-dimensional NMR spectroscopy
    • V. Sklenář, Selective excitation techniques for water suppression in one- and two-dimensional NMR spectroscopy, Basic Life Sci. 56 (1990) 63-84.
    • (1990) Basic Life Sci. , vol.56 , pp. 63-84
    • Sklenář, V.1
  • 18
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • M. Piotto, V. Saudek, V. Sklenář, Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions, J. Biomol. NMR 2 (1992) 661-665.
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenář, V.3
  • 19
    • 0042119144 scopus 로고
    • PARIS, a program for automatic recognition and integration of 2D NMR signals
    • V. Stoven, A. Mikou, D. Piveteau, E. Guittet, J.-Y. Lallemand, PARIS, a program for automatic recognition and integration of 2D NMR signals, J. Magn. Reson. 82 (1989) 163-168.
    • (1989) J. Magn. Reson. , vol.82 , pp. 163-168
    • Stoven, V.1    Mikou, A.2    Piveteau, D.3    Guittet, E.4    Lallemand, J.-Y.5
  • 20
  • 21
    • 0029881450 scopus 로고    scopus 로고
    • The solution structure of HIV-1 Nef reveals an unexpected fold and permits delineation of the binding surface for the SH3 domain of Hck tyrosine protein kinase
    • DOI 10.1038/nsb0496-340
    • S. Grzesiek, A. Bax, G.M. Clore, AM. Gronenborn, J.S. Hu, J. Kaufman, I. Palmer, S.J. Stahl, P.T. Wingfield, The solution structure of HIV-1 Nef reveals an unexpected fold and permits delineation of the binding surface for the SH3 domain of Hck tyrosine protein kinase, Nat Struct Biol. 3 (1996) 340-345. (Pubitemid 26112632)
    • (1996) Nature Structural Biology , vol.3 , Issue.4 , pp. 340-345
    • Grzesiek, S.1    Bax, A.2    Clore, G.M.3    Gronenborn, A.M.4    Hu, J.-S.5    Kaufman, J.6    Palmer, I.7    Stahl, S.J.8    Wingfield, P.T.9
  • 22
    • 0032477750 scopus 로고    scopus 로고
    • Effect of pressure on individual hydrogen bonds in proteins. Basic pancreatic trypsin inhibitor
    • DOI 10.1021/bi972288j
    • H. Li, H. Yamada, K. Akasaka, Effect of pressure on individual hydrogen bonds in proteins. Basic pancreatic trypsin inhibitor, Biochemistry 37 (1998) 1167-1173. (Pubitemid 28135700)
    • (1998) Biochemistry , vol.37 , Issue.5 , pp. 1167-1173
    • Li, H.1    Yamada, H.2    Akasaka, K.3
  • 23
    • 0034711091 scopus 로고    scopus 로고
    • High pressure NMR reveals active-site hinge motion of folate-bound Escherichia coli dihydrofolate reductase
    • R. Kitahara, S. Sareth, H. Yamada, E. Ohmae, K. Gekko, K. Akasaka, High pressure NMR reveals active-site hinge motion of folate-bound Escherichia coli dihydrofolate reductase, Biochemistry 39 (2000) 12789-12795.
    • (2000) Biochemistry , vol.39 , pp. 12789-12795
    • Kitahara, R.1    Sareth, S.2    Yamada, H.3    Ohmae, E.4    Gekko, K.5    Akasaka, K.6
  • 25
    • 14644424521 scopus 로고    scopus 로고
    • NMR snapshots of a fluctuating protein structure: Ubiquitin at 30 bar-3 kbar
    • DOI 10.1016/j.jmb.2005.01.052
    • R. Kitahara, S. Yokoyama, K. Akasaka, NMR snapshots of a fluctuating protein structure: ubiquitin at 30 bar-3 kbar, J. Mol. Biol. 347 (2005) 277-285. (Pubitemid 40312458)
    • (2005) Journal of Molecular Biology , vol.347 , Issue.2 , pp. 277-285
    • Kitahara, R.1    Yokoyama, S.2    Akasaka, K.3
  • 26
    • 0344406172 scopus 로고    scopus 로고
    • Pressure-dependent changes in the solution structure of hen egg-white lysozyme
    • DOI 10.1016/S0022-2836(03)00209-2
    • M. Refaee, T. Tezuka, K. Akasaka, M.P. Williamson, Pressure-dependent changes in the solution structure of hen egg-white lysozyme, J. Mol. Biol. 327 (2003) 857-865. (Pubitemid 36315924)
    • (2003) Journal of Molecular Biology , vol.327 , Issue.4 , pp. 857-865
    • Refaee, M.1    Tezuka, T.2    Akasaka, K.3    Williamson, M.P.4
  • 27
    • 0035979363 scopus 로고    scopus 로고
    • 15N NMR
    • DOI 10.1021/bi010312u
    • 15N NMR, Biochemistry 40 (2001) 8665-8671. (Pubitemid 32709497)
    • (2001) Biochemistry , vol.40 , Issue.30 , pp. 8665-8671
    • Akasaka, K.1    Li, H.2
  • 28
    • 0035793220 scopus 로고    scopus 로고
    • High pressure NMR reveals a variety of fluctuating conformers in beta-lactoglobulin
    • DOI 10.1006/jmbi.2000.4350
    • K. Kuwata, H. Li, H. Yamada, CA Batt, Y. Goto, K. Akasaka, High pressure NMR reveals a variety of fluctuating conformers in β-lactoglobulin, J. Mol. Biol. 305 (2001) 1073-1083. (Pubitemid 33027744)
    • (2001) Journal of Molecular Biology , vol.305 , Issue.5 , pp. 1073-1083
    • Kuwata, K.1    Li, H.2    Yamada, H.3    Batt, C.A.4    Goto, Y.5    Akasaka, K.6
  • 29
    • 79955975933 scopus 로고    scopus 로고
    • Cavity hydration as a gateway to unfolding: An NMR study of hen lysozyme at high pressure and low temperature
    • Y.O. Kamatari, L.J. Smith, CM. Dobson, K. Akasaka, Cavity hydration as a gateway to unfolding: an NMR study of hen lysozyme at high pressure and low temperature, Biophys. Chem. 156 (2011) 24-30.
    • (2011) Biophys. Chem. , vol.156 , pp. 24-30
    • Kamatari, Y.O.1    Smith, L.J.2    Dobson, C.M.3    Akasaka, K.4
  • 31
    • 84862541571 scopus 로고    scopus 로고
    • Electron self-exchange and self-amplified posttranslational modification in the hemoglobins from Synechocystis sp. PCC 6803 and Synechococcus sp. PCC 7002
    • M.R. Preimesberger, M.P. Pond, A. Majumdar, J.T.J. Lecomte, Electron self-exchange and self-amplified posttranslational modification in the hemoglobins from Synechocystis sp. PCC 6803 and Synechococcus sp. PCC 7002, J. Biol. Inorg. Chem. 17 (2012) 599-609.
    • (2012) J. Biol. Inorg. Chem. , vol.17 , pp. 599-609
    • Preimesberger, M.R.1    Pond, M.P.2    Majumdar, A.3    Lecomte, J.T.J.4
  • 32
    • 0001165867 scopus 로고    scopus 로고
    • Nuclear magnetic resonance of hemoproteins
    • K.M. Smith, K. Kadish, R. Guilard (eds.) Academic Press, Burlington, MA
    • G.N. La Mar, J.D. Satterlee, J.S. de Ropp, Nuclear magnetic resonance of hemoproteins, in: K.M. Smith, K. Kadish, R. Guilard (Eds.), The Porphyrin Handbook, vol. 5, Academic Press, Burlington, MA, 2000, pp. 185-298.
    • (2000) The Porphyrin Handbook , vol.5 , pp. 185-298
    • La Mar, G.N.1    Satterlee, J.D.2    De Ropp, J.S.3
  • 33
    • 46949110729 scopus 로고    scopus 로고
    • Numbat: An interactive software tool for fitting Δχ-tensors to molecular coordinates using pseudocontact shifts
    • C Schmitz, M.J. Stanton-Cook, X.C. Su, G. Otting, T. Huber, Numbat: an interactive software tool for fitting Δχ-tensors to molecular coordinates using pseudocontact shifts, J. Biomol. NMR 41 (2008) 179-189.
    • (2008) J. Biomol. NMR , vol.41 , pp. 179-189
    • Schmitz, C.1    Stanton-Cook, M.J.2    Su, X.C.3    Otting, G.4    Huber, T.5
  • 35
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • J.D. Thompson, D.G. Higgins, T.J. Gibson, CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice, Nucleic Acids Res. 22 (1994) 4673-4680. (Pubitemid 24354800)
    • (1994) Nucleic Acids Research , vol.22 , Issue.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 36
    • 0025008168 scopus 로고
    • Sequence logos: A new way to display consensus sequences
    • T.D. Schneider, R.M. Stephens, Sequence logos: a new way to display consensus sequences, Nucleic Acids Res. 18 (1990) 6097-6100.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 6097-6100
    • Schneider, T.D.1    Stephens, R.M.2
  • 37
    • 30344446662 scopus 로고    scopus 로고
    • LogoBar: Bar graph visualization of protein logos with gaps
    • DOI 10.1093/bioinformatics/bti761
    • A. Perez-Bercoff, J. Koch, T.R. Burglin, LogoBar: bar graph visualization of protein logos with gaps, Bioinformatics 22 (2006) 112-114. (Pubitemid 43057016)
    • (2006) Bioinformatics , vol.22 , Issue.1 , pp. 112-114
    • Perez-Bercoff, A.1    Koch, J.2    Burglin, T.R.3
  • 38
    • 77954257799 scopus 로고    scopus 로고
    • ConSurf 2010: Calculating evolutionary conservation in sequence and structure of proteins and nucleic acids
    • H. Ashkenazy, E. Erez, E. Martz, T. Pupko, N. Ben-Tal, ConSurf 2010: calculating evolutionary conservation in sequence and structure of proteins and nucleic acids, Nucleic Acids Res. 38 (2010) W529-W533.
    • (2010) Nucleic Acids Res. , vol.38
    • Ashkenazy, H.1    Erez, E.2    Martz, E.3    Pupko, T.4    Ben-Tal, N.5
  • 39
    • 0004280469 scopus 로고
    • Interscience Publishers, New York
    • R.B. Ash, Information Theory, Interscience Publishers, New York, 1965.
    • (1965) Information Theory
    • Ash, R.B.1
  • 41
    • 0037433701 scopus 로고    scopus 로고
    • Using multiple interdependency to separate functional from phylogenetic correlations in protein alignments
    • DOI 10.1093/bioinformatics/btg072
    • E.R. Tillier, T.W. Lui, Using multiple interdependency to separate functional from phylogenetic correlations in protein alignments, Bioinformatics 19 (2003) 750-755. (Pubitemid 36511899)
    • (2003) Bioinformatics , vol.19 , Issue.6 , pp. 750-755
    • Tillier, E.R.M.1    Lui, T.W.H.2
  • 43
    • 0347358202 scopus 로고    scopus 로고
    • Theories of chemical shift anisotropies in proteins and nucleic acids
    • PII S0079656598000132
    • D. Sitkoff, D.A. Case, Theories of chemical shift anisotropies in proteins and nucleic acids, Prog. Nucl. Mag. Res. Sp. 32 (1998) 165-190. (Pubitemid 128459717)
    • (1998) Progress in Nuclear Magnetic Resonance Spectroscopy , vol.32 , Issue.2 , pp. 165-190
    • Sitkoff, D.1    Case, D.A.2
  • 44
    • 57649229060 scopus 로고    scopus 로고
    • HOLLOW: Generating accurate representations of channel and interior surfaces in molecular structures
    • B.K. Ho, F. Gruswitz, HOLLOW: generating accurate representations of channel and interior surfaces in molecular structures, BMC Struct. Biol. 8 (2008) 49.
    • (2008) BMC Struct. Biol. , vol.8 , pp. 49
    • Ho, B.K.1    Gruswitz, F.2
  • 45
    • 33747818007 scopus 로고    scopus 로고
    • CASTp: Computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues
    • DOI 10.1093/nar/gkl282
    • J. Dundas, Z. Ouyang, J. Tseng, A. Binkowski, Y. Turpaz, J. Liang, CASTp: computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues, Nucleic Acids Res. 34 (2006) W116-W118. (Pubitemid 44529746)
    • (2006) Nucleic Acids Research , vol.34 , Issue.WEB. SERV. ISS.
    • Dundas, J.1    Ouyang, Z.2    Tseng, J.3    Binkowski, A.4    Turpaz, Y.5    Liang, J.6
  • 46
    • 0020712468 scopus 로고
    • The effect of high pressure upon proteins and other biomolecules
    • G. Weber, H.G. Drickamer, The effect of high pressure upon proteins and other biomolecules, Q. Rev. Biophys. 16 (1983) 89-112.
    • (1983) Q. Rev. Biophys. , vol.16 , pp. 89-112
    • Weber, G.1    Drickamer, H.G.2
  • 47
    • 33749512406 scopus 로고    scopus 로고
    • High-pressure studies on protein aggregates and amyloid fibrils
    • DOI 10.1016/S0076-6879(06)13013-X, PII S007668790613013X, Amyloid, Prions, and Other Protein Aggregates, Part C
    • Y.S. Kim, T.W. Randolph, M.B. Seefeldt, J.F. Carpenter, High-pressure studies on protein aggregates and amyloid fibrils, Methods Enzymol. 413 (2006) 237-253. (Pubitemid 44528694)
    • (2006) Methods in Enzymology , vol.413 , pp. 237-253
    • Kim, Y.1    Randolph, T.W.2    Seefeldt, M.B.3    Carpenter, J.F.4
  • 49
    • 16344381007 scopus 로고    scopus 로고
    • Pressure denaturation of staphylococcal nuclease studied by neutron small-angle scattering and molecular simulation
    • DOI 10.1529/biophysj.104.050526
    • A. Paliwal, D. Asthagiri, D.P. Bossev, M.E. Paulaitis, Pressure denaturation of staphylococcal nuclease studied by neutron small-angle scattering and molecular simulation, Biophys. J. 87 (2004) 3479-3492. (Pubitemid 40468601)
    • (2004) Biophysical Journal , vol.87 , Issue.5 , pp. 3479-3492
    • Paliwal, A.1    Asthagiri, D.2    Bossev, D.P.3    Paulaitis, M.E.4
  • 52
    • 0026610880 scopus 로고
    • 1H NMR assignments for the amino-terminal domain of the phage 434 repressor in the urea-unfolded form
    • 1H NMR assignments for the amino-terminal domain of the phage 434 repressor in the urea-unfolded form, Proc. Natl. Acad. Sci. U. S. A. 89 (1992) 4397-4401.
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 4397-4401
    • Neri, D.1    Wider, G.2    Wüthrich, K.3
  • 54
    • 33645981275 scopus 로고    scopus 로고
    • Conformational fluctuations of proteins revealed by variable pressure NMR
    • H. Li, K. Akasaka, Conformational fluctuations of proteins revealed by variable pressure NMR, Biochim. Biophys. Acta 1764 (2006) 331-345.
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 331-345
    • Li, H.1    Akasaka, K.2
  • 58
    • 4744359951 scopus 로고    scopus 로고
    • Cyanide binding to hexacoordinate cyanobacterial hemoglobins: Hydrogen-bonding network and heme pocket rearrangement in ferric H117A Synechocystis hemoglobin
    • DOI 10.1021/bi048726l
    • B.C. Vu, H.J. Nothnagel, D.A. Vuletich, C.J. Falzone, J.T.J. Lecomte, Cyanide binding to hexacoordinate cyanobacterial hemoglobins: hydrogen-bonding network and heme pocket rearrangement in ferric H117A Synechocystis hemoglobin, Biochemistry 43 (2004) 12622-12633. (Pubitemid 39314724)
    • (2004) Biochemistry , vol.43 , Issue.39 , pp. 12622-12633
    • Vu, B.C.1    Nothnagel, H.J.2    Vuletich, D.A.3    Falzone, C.J.4    Lecomte, J.T.J.5
  • 60
    • 0037219686 scopus 로고    scopus 로고
    • Evolutionarily conserved networks of residues mediate allosteric communication in proteins
    • DOI 10.1038/nsb881
    • G.M. Suel, S.W. Lockless, M.A. Wall, R. Ranganathan, Evolutionarily conserved networks of residues mediate allosteric communication in proteins, Nat. Struct. Biol. 10 (2003) 59-69. (Pubitemid 36034178)
    • (2003) Nature Structural Biology , vol.10 , Issue.1 , pp. 59-69
    • Suel, G.M.1    Lockless, S.W.2    Wall, M.A.3    Ranganathan, R.4
  • 61
    • 70349656526 scopus 로고    scopus 로고
    • A combinatorial approach to detect coevolved amino acid networks in protein families of variable divergence
    • J. Baussand, A. Carbone, A combinatorial approach to detect coevolved amino acid networks in protein families of variable divergence, PLoS Comput. Biol. 5 (2009) e1000488.
    • (2009) PLoS Comput. Biol. , vol.5
    • Baussand, J.1    Carbone, A.2
  • 62
    • 0019221870 scopus 로고
    • High-pressure proton nuclear magnetic resonance studies of hemoproteins. Pressure-induced structural change in heme environments of myoglobin, hemoglobin, and horseradish peroxidase
    • I. Morishima, S. Ogawa, H. Yamada, High-pressure proton nuclear magnetic resonance studies of hemoproteins. Pressure-induced structural change in heme environments of myoglobin, hemoglobin, and horseradish peroxidase, Biochemistry 19 (1980) 1569-1575. (Pubitemid 10088208)
    • (1980) Biochemistry , vol.19 , Issue.8 , pp. 1569-1575
    • Morishima, I.1    Ogawa, S.2    Yamada, H.3
  • 63
    • 0037307125 scopus 로고    scopus 로고
    • 1H NMR study of pressure-induced structural changes in the heme environments of metcyanomyoglobins
    • DOI 10.1110/ps.4620103
    • 1H NMR study of pressure-induced structural changes in the heme environments of metcyanomyoglobins, Protein Sci. 12 (2003) 207-217. (Pubitemid 36120333)
    • (2003) Protein Science , vol.12 , Issue.2 , pp. 207-217
    • Kitahara, R.1    Kato, M.2    Taniguchi, Y.3
  • 64
    • 0036291143 scopus 로고    scopus 로고
    • High pressure NMR reveals that apomyoglobin is an equilibrium mixture from the native to the unfolded
    • DOI 10.1016/S0022-2836(02)00449-7
    • R. Kitahara, H. Yamada, K. Akasaka, P.E. Wright, High pressure NMR reveals that apomyoglobin is an equilibrium mixture from the native to the unfolded, J. Mol. Biol. 320 (2002) 311-319. (Pubitemid 34722221)
    • (2002) Journal of Molecular Biology , vol.320 , Issue.2 , pp. 311-319
    • Kitahara, R.1    Yamada, H.2    Akasaka, K.3    Wright, P.E.4
  • 65
    • 33646341657 scopus 로고    scopus 로고
    • A phylogenetic and structural analysis of truncated hemoglobins
    • D.A. Vuletich, J.T.J. Lecomte, A phylogenetic and structural analysis of truncated hemoglobins, J. Mol. Evol. 62 (2006) 196-210.
    • (2006) J. Mol. E , vol.62 , pp. 196-210
    • Vuletich, D.A.1    Lecomte, J.T.J.2
  • 66
    • 34447530237 scopus 로고    scopus 로고
    • Protein fold and structure in the truncated (2/2) globin family
    • DOI 10.1016/j.gene.2007.02.045, PII S0378111907001990
    • M. Nardini, A. Pesce, M. Milani, M. Bolognesi, Protein fold and structure in the truncated (2/2) globin family, Gene 398 (2007) 2-11. (Pubitemid 47068885)
    • (2007) Gene , vol.398 , Issue.1-2 SPEC. ISSUE , pp. 2-11
    • Nardini, M.1    Pesce, A.2    Milani, M.3    Bolognesi, M.4
  • 68
    • 69849099148 scopus 로고    scopus 로고
    • High pressure reveals structural determinants for globin hexacoordination: Neuroglobin and myoglobin cases
    • L. Capece, M.A. Marti, A. Bidon-Chanal, A. Nadra, F.J. Luque, D.A. Estrin, High pressure reveals structural determinants for globin hexacoordination: neuroglobin and myoglobin cases, Proteins 75 (2009) 885-894.
    • (2009) Proteins , vol.75 , pp. 885-894
    • Capece, L.1    Marti, M.A.2    Bidon-Chanal, A.3    Nadra, A.4    Luque, F.J.5    Estrin, D.A.6
  • 69
    • 47049091787 scopus 로고    scopus 로고
    • Identification of ligand-binding pathways in truncated hemoglobins using locally enhanced sampling molecular dynamics
    • S.D. Golden, K.W. Olsen, Identification of ligand-binding pathways in truncated hemoglobins using locally enhanced sampling molecular dynamics, Methods Enzymol. 437 (2008) 459-475.
    • (2008) Methods Enzymol. , vol.437 , pp. 459-475
    • Golden, S.D.1    Olsen, K.W.2
  • 70
    • 84872875981 scopus 로고    scopus 로고
    • Oxygen migration pathways in NO-bound truncated hemoglobin
    • P.A. Cazade, M. Meuwly, Oxygen migration pathways in NO-bound truncated hemoglobin, Chemphyschem 13 (2012) 4276-4286.
    • (2012) Chemphyschem , vol.13 , pp. 4276-4286
    • Cazade, P.A.1    Meuwly, M.2
  • 72
    • 84055190273 scopus 로고    scopus 로고
    • Structure and dynamics of Mycobacterium tuberculosis truncated hemoglobin N: Insights from NMR spectroscopy and molecular dynamics simulations
    • P.Y. Savard, R. Daigle, S. Morin, A. Sebilo, F. Meindre, P. Lagüe, M. Guertin, S.M. Gagné, Structure and dynamics of Mycobacterium tuberculosis truncated hemoglobin N: insights from NMR spectroscopy and molecular dynamics simulations, Biochemistry 50 (2011) 11121-11130.
    • (2011) Biochemistry , vol.50 , pp. 11121-11130
    • Savard, P.Y.1    Daigle, R.2    Morin, S.3    Sebilo, A.4    Meindre, F.5    Lagüe, P.6    Guertin, M.7    Gagné, S.M.8
  • 73
    • 79957986258 scopus 로고    scopus 로고
    • Frontier residues lining globin internal cavities present specific mechanical properties
    • A. Bocahut, S. Bernad, P. Sebban, S. Sacquin-Mora, Frontier residues lining globin internal cavities present specific mechanical properties, J. Am. Chem. Soc. 133 (2011) 8753-8761.
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 8753-8761
    • Bocahut, A.1    Bernad, S.2    Sebban, P.3    Sacquin-Mora, S.4
  • 75
    • 77649105245 scopus 로고    scopus 로고
    • Dynamic correlation between pressure-induced protein structural transition and water penetration
    • T. Imai, Y. Sugita, Dynamic correlation between pressure-induced protein structural transition and water penetration, J. Phys. Chem. B 114 (2010) 2281-2286.
    • (2010) J. Phys. Chem. B , vol.114 , pp. 2281-2286
    • Imai, T.1    Sugita, Y.2
  • 76
    • 85021467943 scopus 로고
    • Structure and function of haemoglobin. II. Some relations between polypeptide chain configuration and amino acid sequence
    • M.F. Perutz, J.C. Kendrew, H.C. Watson, Structure and function of haemoglobin. II. Some relations between polypeptide chain configuration and amino acid sequence, J. Mol. Biol. 13 (1965) 669-678.
    • (1965) J. Mol. Biol. , vol.13 , pp. 669-678
    • Perutz, M.F.1    Kendrew, J.C.2    Watson, H.C.3
  • 77
    • 2142738304 scopus 로고    scopus 로고
    • WebLogo: A sequence logo generator
    • DOI 10.1101/gr.849004
    • G.E. Crooks, G. Hon, J.M. Chandonia, S.E. Brenner, WebLogo: a sequence logo generator, Genome Res. 14 (2004) 1188-1190. (Pubitemid 38811555)
    • (2004) Genome Research , vol.14 , Issue.6 , pp. 1188-1190
    • Crooks, G.E.1    Hon, G.2    Chandonia, J.-M.3    Brenner, S.E.4
  • 78
    • 23144448512 scopus 로고    scopus 로고
    • ConSurf 2005: The projection of evolutionary conservation scores of residues on protein structures
    • DOI 10.1093/nar/gki370
    • M. Landau, I. Mayrose, Y. Rosenberg, F. Glaser, E. Martz, T. Pupko, N. Ben-Tal, ConSurf 2005: the projection of evolutionary conservation scores of residues on protein structures, Nucleic Acids Res. 33 (2005) W299-W302. (Pubitemid 44529930)
    • (2005) Nucleic Acids Research , vol.33 , Issue.WEB. SERV. ISS.
    • Landau, M.1    Mayrose, I.2    Rosenberg, Y.3    Glaser, F.4    Martz, E.5    Pupko, T.6    Ben-Tal, N.7


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