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Volumn 1814, Issue 12, 2011, Pages 1919-1929

Structural characterization of recombinant human myoglobin isoforms by 1H and 129Xe NMR and molecular dynamics simulations

Author keywords

129Xe NMR; 1H NMR; Molecular dynamics; Myoglobin; Xenon; Xenon cavity

Indexed keywords

HEME; ISOPROTEIN; MYOGLOBIN; XENON;

EID: 81755184330     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2011.06.014     Document Type: Article
Times cited : (2)

References (76)
  • 2
    • 0029894282 scopus 로고    scopus 로고
    • Kinetic pathways and barriers for ligand binding to myoglobin
    • DOI 10.1074/jbc.271.30.17593
    • J.S. Olson, and G.N. Phillips Kinetic pathways and barriers for ligand binding to myoglobin J. Biol. Chem. 271 1996 17593 17596 (Pubitemid 26250722)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.30 , pp. 17593-17596
    • Olson, J.S.1    Phillips Jr., G.N.2
  • 3
    • 0024316850 scopus 로고
    • Hemoproteins, ligands, and quanta
    • Q.H. Gibson Hemoproteins, ligands, and quanta J. Biol. Chem. 264 1989 20155 20158 (Pubitemid 20009185)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.34 , pp. 20155-20158
    • Gibson, Q.H.1
  • 5
    • 20444500960 scopus 로고    scopus 로고
    • Oxygen supply and nitric oxide scavenging by myoglobin contribute to exercise endurance and cardiac function
    • DOI 10.1096/fj.04-2886fje
    • M.W. Merx, A. Gödecke, U. Flögel, and J. Schrader Oxygen supply and nitric oxide scavenging by myoglobin contribute to exercise endurance and cardiac function FASEB J. 19 2005 1015 1017 (Pubitemid 40827736)
    • (2005) FASEB Journal , vol.19 , Issue.8 , pp. 1015-1017
    • Merx, M.W.1    Godecke, A.2    Flogel, U.3    Schrader, J.4
  • 6
    • 17644400982 scopus 로고    scopus 로고
    • Nitric oxide, cytochrome c oxidase and myoglobin: Competition and reaction pathways
    • DOI 10.1016/j.febslet.2005.03.067
    • A. Giuffre, E. Forte, M. Brunori, and P. Sarti Nitric oxide, cytochrome c oxidase and myoglobin: competition and reaction pathways FEBS Lett. 579 2005 2528 2532 (Pubitemid 40569532)
    • (2005) FEBS Letters , vol.579 , Issue.11 , pp. 2528-2532
    • Giuffre, A.1    Forte, E.2    Brunori, M.3    Sarti, P.4
  • 11
    • 0014688806 scopus 로고
    • Abnormal human myoglobin: 53 (D4) glutamic acid-lysine
    • F.E. Boulton, R.G. Huntsman, P.A. Lorkin, and H. Lehmann Abnormal human myoglobin: 53 (D4) glutamic acid-lysine Nature 223 1969 832 833
    • (1969) Nature , vol.223 , pp. 832-833
    • Boulton, F.E.1    Huntsman, R.G.2    Lorkin, P.A.3    Lehmann, H.4
  • 12
    • 0015237094 scopus 로고
    • The third variant of human myoglobin showing an unusual amino acid substitution 138(H16) arginine-tryptophan
    • F.E. Boulton, R.G. Huntsman, A. Romero Herrera, P.A. Lorkin, and H. Lehmann The third variant of human myoglobin showing an unusual amino acid substitution 138(H16) arginine-tryptophan Biochim. Biophys. Acta 229 1971 716 719
    • (1971) Biochim. Biophys. Acta , vol.229 , pp. 716-719
    • Boulton, F.E.1    Huntsman, R.G.2    Romero Herrera, A.3    Lorkin, P.A.4    Lehmann, H.5
  • 14
    • 0000898256 scopus 로고
    • Myoglobin content and enzymatic activity of muscle and altitude adaptation
    • B. Reynafarje Myoglobin content and enzymatic activity of muscle and altitude adaptation J. Appl. Physiol. 17 1962 301 305
    • (1962) J. Appl. Physiol. , vol.17 , pp. 301-305
    • Reynafarje, B.1
  • 16
    • 2342567729 scopus 로고    scopus 로고
    • Second generation Tibetan lowlanders acclimatize to high altitude more quickly than Caucasians
    • DOI 10.1113/jphysiol.2003.059188
    • C. Marconi, M. Marzorati, B. Grassi, B. Basnyat, A. Colombini, B. Kayser, and P. Cerretelli Second generation Tibetan lowlanders acclimatize to high altitude more quickly than Caucasians J. Physiol. 556 2004 661 671 (Pubitemid 38579014)
    • (2004) Journal of Physiology , vol.556 , Issue.2 , pp. 661-671
    • Marconi, C.1    Marzorati, M.2    Grassi, B.3    Basnyat, B.4    Colombini, A.5    Kayser, B.6    Cerretelli, P.7
  • 17
    • 29244487094 scopus 로고    scopus 로고
    • Economy of locomotion in high-altitude Tibetan migrants exposed to normoxia
    • DOI 10.1113/jphysiol.2005.094979
    • C. Marconi, M. Marzorati, D. Sciuto, A. Ferri, and P. Cerretelli Economy of locomotion in high-altitude Tibetan migrants exposed to normoxia J. Physiol. 569 2005 667 675 (Pubitemid 41830130)
    • (2005) Journal of Physiology , vol.569 , Issue.2 , pp. 667-675
    • Maconi, C.1    Marzorati, M.2    Sciuto, D.3    Ferri, A.4    Cerretelli, P.5
  • 18
    • 70349196513 scopus 로고    scopus 로고
    • Muscle bioenergetics and metabolic control at altitude
    • P. Cerretelli, M. Marzorati, and C. Marconi Muscle bioenergetics and metabolic control at altitude High Alt. Med. Biol. 10 2009 165 174
    • (2009) High Alt. Med. Biol. , vol.10 , pp. 165-174
    • Cerretelli, P.1    Marzorati, M.2    Marconi, C.3
  • 21
    • 0001215890 scopus 로고    scopus 로고
    • Nuclear magnetic resonance of paramagnetic metalloproteins
    • I. Bertini, P. Turano, and A.J. Vila Nuclear magnetic resonance of paramagnetic metalloproteins Chem. Rev. 83 1998 2833 2932
    • (1998) Chem. Rev. , vol.83 , pp. 2833-2932
    • Bertini, I.1    Turano, P.2    Vila, A.J.3
  • 22
    • 0021766921 scopus 로고
    • Cavities in proteins: Structure of metmyoglobin-xenon complex solved to 1.9 Å
    • R.F. Tilton Jr., I.D. Kuntz Jr., and G.A. Petsko Cavities in proteins: structure of metmyoglobin-xenon complex solved to 1.9 Å Biochemistry 23 1984 2849 2857
    • (1984) Biochemistry , vol.23 , pp. 2849-2857
    • Tilton, Jr.R.F.1    Kuntz, Jr.I.D.2    Petsko, G.A.3
  • 23
    • 0013842370 scopus 로고
    • Binding of xenon to sperm whale myoglobin
    • B.P. Schoenborn, H.C. Watson, and J.C. Kendrew Binding of xenon to sperm whale myoglobin Nature 207 1965 28 30
    • (1965) Nature , vol.207 , pp. 28-30
    • Schoenborn, B.P.1    Watson, H.C.2    Kendrew, J.C.3
  • 25
    • 0034662996 scopus 로고    scopus 로고
    • Evidence of non-specific surface interactions between laser-polarized xenon and myoglobin in solution
    • S.M. Rubin, M.M. Spence, B.M. Goodson, D.E. Wemmer, and A. Pines Evidence of non-specific surface interactions between laser-polarized xenon and myoglobin in solution Proc. Natl. Acad. Sci. 97 2000 3472 9475
    • (2000) Proc. Natl. Acad. Sci. , vol.97 , pp. 3472-9475
    • Rubin, S.M.1    Spence, M.M.2    Goodson, B.M.3    Wemmer, D.E.4    Pines, A.5
  • 30
    • 0020285568 scopus 로고
    • Nuclear magnetic resonance studies of xenon-129 with myoglobin and hemoglobin
    • R.F. Tilton Jr., and I.D. Kuntz Jr. Nuclear magnetic resonance studies of xenon-129 with myoglobin and haemoglobin Biochemistry 21 1982 6850 6857 (Pubitemid 13119621)
    • (1982) Biochemistry , vol.21 , Issue.26 , pp. 6850-6857
    • Tilton Jr., R.F.1    Kuntz Jr., I.D.2
  • 31
    • 37049082163 scopus 로고
    • The nuclear magnetic resonance of Xe-129 trapped in clarthrates and some other solids
    • J.A. Ripmeester, C.I. Ratcliffe, and J.S. Tse The nuclear magnetic resonance of Xe-129 trapped in clarthrates and some other solids J. Chem. Soc. Faraday Trans. 84 1988 3731 3745
    • (1988) J. Chem. Soc. Faraday Trans. , vol.84 , pp. 3731-3745
    • Ripmeester, J.A.1    Ratcliffe, C.I.2    Tse, J.S.3
  • 33
    • 0034680315 scopus 로고    scopus 로고
    • Flexibility and ligand exchange in a buried cavity mutant of T4 lysozyme studied by multinuclear NMR
    • F.A.A. Mulder, B. Hon, D. Ranjith Muhandiram, F.W. Dahlquist, and L.E. Kay Flexibility and ligand exchange in a buried cavity mutant of T4 lysozyme studied by multinuclear NMR Biochemistry 39 2000 12614 12622
    • (2000) Biochemistry , vol.39 , pp. 12614-12622
    • Mulder, F.A.A.1    Hon, B.2    Ranjith Muhandiram, D.3    Dahlquist, F.W.4    Kay, L.E.5
  • 34
    • 0035088036 scopus 로고    scopus 로고
    • Magnetization transfer from laser-polarized xenon to protons located in the hydrophobic cavity of the wheat nonspecific lipid transfer protein
    • DOI 10.1110/ps.47001
    • C. Landon, P. Berthault, F. Vovelle, and H. Desvaux Magnetization transfer from laser-polarized xenon to protons located in the hydrophobic cavity of the wheat non-specific lipid transfer protein Protein Sci. 10 2001 762 770 (Pubitemid 32240502)
    • (2001) Protein Science , vol.10 , Issue.4 , pp. 762-770
    • Landon, C.1    Berthault, P.2    Vovelle, F.3    Desvaux, H.4
  • 35
    • 0014352643 scopus 로고
    • Analysis of the visible spectra of some sperm whale ferrimyoglobin derivatives
    • D.W. Smith, and J.P. Williams Analysis of the visible spectra of some sperm whale ferrimyoglobin derivatives Biochem. J. 110 1968 297 301
    • (1968) Biochem. J. , vol.110 , pp. 297-301
    • Smith, D.W.1    Williams, J.P.2
  • 36
    • 0024372423 scopus 로고
    • Ligand and proton exchange dynamics in recombinant human myoglobin mutants
    • DOI 10.1016/0022-2836(89)90456-7
    • D.G. Lambright, S. Balasubramanian, and S.G. Boxer Ligand and proton exchange dynamics in recombinant human myoglobin mutants J. Mol. Biol. 207 1989 289 299 (Pubitemid 19141257)
    • (1989) Journal of Molecular Biology , vol.207 , Issue.1 , pp. 289-299
    • Lambright, D.G.1    Balasubramanian, S.2    Boxer, S.G.3
  • 37
    • 0343359244 scopus 로고
    • Investigation of exchange processes by two-dimensional NMR spectroscopy
    • J. Jeener, B.H. Meyer, P. Bachman, and R.R. Ernst Investigation of exchange processes by two-dimensional NMR spectroscopy J. Chem. Phys. 71 1979 4546 4553
    • (1979) J. Chem. Phys. , vol.71 , pp. 4546-4553
    • Jeener, J.1    Meyer, B.H.2    Bachman, P.3    Ernst, R.R.4
  • 40
    • 0001434099 scopus 로고
    • Proton nuclear magnetic resonance study of the relaxation behavior and kinetic lability of exchangeable protons in the heme pocket of cyanometmyoglobin
    • J.D. Cutnell, G.N. La Mar, and S.B. Kong Proton nuclear magnetic resonance study of the relaxation behavior and kinetic lability of exchangeable protons in the heme pocket of cyanometmyoglobin J. Am. Chem. Soc. 103 1981 3567 3572
    • (1981) J. Am. Chem. Soc. , vol.103 , pp. 3567-3572
    • Cutnell, J.D.1    La Mar, G.N.2    Kong, S.B.3
  • 42
    • 0010262629 scopus 로고    scopus 로고
    • ORAC: A molecular dynamics program to simulate complex molecular systems with realistic electrostatic interactions
    • P. Procacci, T.A. Darden, E. Paci, and M. Marchi ORAC: a molecular dynamics program to simulate complex molecular systems with realistic electrostatic interactions J. Comput. Chem. 18 1997 1848 1862 (Pubitemid 127560714)
    • (1997) Journal of Computational Chemistry , vol.18 , Issue.15 , pp. 1848-1862
    • Procacci, P.1    Darden, T.A.2    Paci, E.3    Marchi, M.4
  • 45
    • 22244449290 scopus 로고    scopus 로고
    • Coordinates scaling and multiple time step algorithms for simulation of solvated proteins in the NPT ensemble
    • DOI 10.1063/1.477136, PII S0021960698509373
    • M. Marchi, and P. Procacci Coordinates scaling and multiple time step algorithms for simulation of solvated proteins in the NPT ensemble J. Chem. Phys. 109 1998 5194 5202 (Pubitemid 128678690)
    • (1998) Journal of Chemical Physics , vol.109 , Issue.13 , pp. 5194-5202
    • Marchi, M.1    Procacci, P.2
  • 46
    • 0025289622 scopus 로고
    • X-ray crystal structure of a recombinant human myoglobin mutant at 2.8 A resolution
    • DOI 10.1016/S0022-2836(05)80181-0
    • S.R. Hubbard, W.A. Hendrickson, D.G. Lambright, and S.G. Boxer X-ray crystal structure of a recombinant human myoglobin mutant at 2.8 Å resolution J. Mol. Biol. 213 1990 215 218 (Pubitemid 20176530)
    • (1990) Journal of Molecular Biology , vol.213 , Issue.2 , pp. 215-218
    • Hubbard, S.R.1    Hendrickson, W.A.2    Lambright, D.G.3    Boxer, S.G.4
  • 47
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • DOI 10.1006/jmbi.1993.1626
    • A. Šali, and T.L. Blundell Comparative protein modeling by satisfaction of spatial restraints J. Mol. Biol. 234 1993 779 815 (Pubitemid 24007801)
    • (1993) Journal of Molecular Biology , vol.234 , Issue.3 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 48
    • 69049084556 scopus 로고    scopus 로고
    • Breathing motions of a respiratory protein revealed by molecular dynamics simulation
    • M.A. Scorciapino, A. Robertazzi, M. Casu, P. Ruggerone, and M. Ceccarelli Breathing motions of a respiratory protein revealed by molecular dynamics simulation J. Am. Chem. Soc. 131 2009 11825 11832
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 11825-11832
    • Scorciapino, M.A.1    Robertazzi, A.2    Casu, M.3    Ruggerone, P.4    Ceccarelli, M.5
  • 51
    • 3242886771 scopus 로고    scopus 로고
    • PDB2PQR: An automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations
    • T.J. Dolinsky, J.E. Nielsen, J.A. McCammon, and N.A. Baker PDB2PQR: an automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations Nucleic Acids Res. 32 2004 665 667
    • (2004) Nucleic Acids Res. , vol.32 , pp. 665-667
    • Dolinsky, T.J.1    Nielsen, J.E.2    McCammon, J.A.3    Baker, N.A.4
  • 52
    • 34547559704 scopus 로고    scopus 로고
    • PDB2PQR: Expanding and upgrading automated preparation of biomolecular structures for molecular simulations
    • T.J. Dolinsky, P. Czodrowski, H. Li, J.E. Nielsen, J.H. Jensen, G. Klebe, and N.A. Baker PDB2PQR: expanding and upgrading automated preparation of biomolecular structures for molecular simulations Nucleic Acids Res. 35 2007 522 525
    • (2007) Nucleic Acids Res. , vol.35 , pp. 522-525
    • Dolinsky, T.J.1    Czodrowski, P.2    Li, H.3    Nielsen, J.E.4    Jensen, J.H.5    Klebe, G.6    Baker, N.A.7
  • 54
    • 0027995683 scopus 로고
    • Detection, delineation, measurement and display of cavities in macromolecular structures
    • DOI 10.1107/S0907444993011333
    • G.J. Kleywegt, and T.A. Jones Detection, delineation, measurement and display of cavities in macromolecular structures Acta Crystallogr. D Biol. Crystallogr. 50 1994 178 185 (Pubitemid 2054290)
    • (1994) Acta Crystallographica Section D: Biological Crystallography , vol.50 , Issue.2 , pp. 178-185
    • Kleywegt, G.J.1    Alwyn Jones, T.2
  • 55
    • 0025195073 scopus 로고
    • Solution structural characterization of cyanometmyoglobin: Resonance: Assignment of heme cavity residues by two-dimensional NMR
    • S.D. Emerson, and G. La Mar Solution structural characterization of cyanometmyoglobin: resonance: assignment of heme cavity residues by two-dimensional NMR Biochemistry 29 1990 1556 1566
    • (1990) Biochemistry , vol.29 , pp. 1556-1566
    • Emerson, S.D.1    La Mar, G.2
  • 57
    • 0023042853 scopus 로고
    • X-ray structure and refinement of carbon-monoxy (Fe II)-myoglobin at 1.5 A resolution
    • J. Kuriyan, S. Wilz, M. Karplus, and G.A. Petsko X-ray structure and refinement of carbon-monoxy (Fe II)-myoglobin at 1.5 A resolution J. Mol. Biol. 192 1986 133 154
    • (1986) J. Mol. Biol. , vol.192 , pp. 133-154
    • Kuriyan, J.1    Wilz, S.2    Karplus, M.3    Petsko, G.A.4
  • 58
    • 0033550490 scopus 로고    scopus 로고
    • Solution NMR determination of the anisotropy and orientation of the paramagnetic susceptibility tensor as a function of temperature for metmyoglobin cyanide: Implications for the population of excited electronic states
    • DOI 10.1021/ja982555o
    • B.D. Nguyen, Z. Xia, D.C. Yeh, K. Vyas, H. Deaguero, and G. La Mar Solution NMR determination of the anisotropy and orientation of the paramagnetic susceptibility tensor as a function of temperature for metmyoglobin cyanide: implications for the population of excited electronic states J. Am. Chem. Soc. 121 1999 208 217 (Pubitemid 29047139)
    • (1999) Journal of the American Chemical Society , vol.121 , Issue.1 , pp. 208-217
    • Nguyen, B.D.1    Xia, Z.2    Yeh, D.C.3    Vyas, K.4    Deaguero, H.5    La Mar, G.N.6
  • 59
    • 0021759017 scopus 로고
    • 1H NMR resonances of histidine and other aromatic residues in met-, cyano-, oxy-, and (carbon monoxy)myoglobins
    • 1H NMR resonances of histidine and other aromatic residues in met-, cyano-, oxy-, and (carbon monoxy)myoglobins Biochemistry 23 1984 4890 4905
    • (1984) Biochemistry , vol.23 , pp. 4890-4905
    • Carver, J.A.1    Bradbury, J.H.2
  • 61
    • 0001520987 scopus 로고
    • Influence of heme orientation on oxygen affinity in native sperm whale myoglobin
    • D.J. Livingston, N.L. Davis, G.N. La Mar, and W.D. Brown Influence of heme orientation on oxygen affinity in native sperm whale myoglobin J. Am. Chem. Soc. 106 1984 3025 3026
    • (1984) J. Am. Chem. Soc. , vol.106 , pp. 3025-3026
    • Livingston, D.J.1    Davis, N.L.2    La Mar, G.N.3    Brown, W.D.4
  • 62
    • 0023108441 scopus 로고
    • Functional effects of heme orientational disorder in sperm whale myoglobin
    • W.R. Light, R.J. Rohlfs, G. Palmer, and J.S. Olson Functional effects of heme orientational disorder in sperm whale myoglobin J. Biol. Chem. 262 1987 46 52 (Pubitemid 17235629)
    • (1987) Journal of Biological Chemistry , vol.262 , Issue.1 , pp. 46-52
    • Light, W.R.1    Rohlfs, R.J.2    Palmer, G.3    Olson, J.S.4
  • 63
  • 65
    • 0015803280 scopus 로고
    • Evaluation of dipolar nuclear magnetic resonance shifts in low-spin hemin systems: Ferricytochrome c and metmyoglobin cyanide
    • W.D. Horrocks Jr., and E.S. Greenberg Evaluation of dipolar nuclear magnetic resonance shifts in low-spin hemin systems: ferricytochrome c and metmyoglobin cyanide Biochim. Biophys. Acta 322 1973 38 44
    • (1973) Biochim. Biophys. Acta , vol.322 , pp. 38-44
    • Horrocks, Jr.W.D.1    Greenberg, E.S.2
  • 66
    • 0015215165 scopus 로고
    • Proton magnetic resonance study of high- and low-spin hemin derivatives
    • R.J. Kurland, R.G. Little, D.G. Davis, and Ch. Ho Proton magnetic resonance study of high- and low-spin hemin derivatives Biochemistry 10 1971 2237 2246
    • (1971) Biochemistry , vol.10 , pp. 2237-2246
    • Kurland, R.J.1    Little, R.G.2    Davis, D.G.3    Ho, Ch.4
  • 67
    • 0016757472 scopus 로고
    • Nuclear magnetic resonance titration curves of histidine ring protons. Human metmyoglobin and the effects of azide on human, horse, and sperm whale metmyoglobins
    • M.B. Hayes, H. Hagenmaier, and J.S. Cohen Nuclear magnetic resonance titration curves of histidine ring protons. Human metmyoglobin and the effects of azide on human, horse, and sperm whale metmyoglobins J. Biol. Chem. 250 1975 7461 7472
    • (1975) J. Biol. Chem. , vol.250 , pp. 7461-7472
    • Hayes, M.B.1    Hagenmaier, H.2    Cohen, J.S.3
  • 68
    • 0023280145 scopus 로고
    • 1H NMR probe for hydrogen bonding of distal residues to bound ligands in heme proteins: Isotope effect on heme electronic structure of myoglobin
    • DOI 10.1021/ja00257a068
    • J.T.J. Lecomte, and G.N. La Mar Proton NMR probe for hydrogen bonding of distal residues to bound ligands in heme proteins: isotope effect on heme electronic structure of myoglobin J. Am. Chem. Soc. 109 1987 7219 7220 (Pubitemid 17158663)
    • (1987) Journal of the American Chemical Society , vol.109 , Issue.23 , pp. 7219-7220
    • Lecomte, J.T.J.1    La Mar, G.N.2
  • 69
    • 0032168882 scopus 로고    scopus 로고
    • Functional implications of the proximal hydrogen-bonding network in myoglobin: A resonance raman and kinetic study of Leu89, Ser92, His97, and F- helix swap mutants
    • DOI 10.1021/bi980752u
    • E.S. Peterson, J.M. Friedman, E.Y.T. Chien, and S.G. Sligar Functional implications of the proximal hydrogen-bonding network in myoglobin: a resonance Raman and kinetic study of Leu89, Ser92, His97, and F-helix swap mutants Biochemistry 37 1998 12301 12319 (Pubitemid 28411317)
    • (1998) Biochemistry , vol.37 , Issue.35 , pp. 12301-12319
    • Peterson, E.S.1    Friedman, J.M.2    Chien, E.Y.T.3    Sligar, S.G.4
  • 70
    • 0000766204 scopus 로고
    • Monoatomic xenon: Its great interest in chemistry as a probe of intermolecular interactions, and its (easy) study by NMR
    • J. Reisse Monoatomic xenon: its great interest in chemistry as a probe of intermolecular interactions, and its (easy) study by NMR N. J. Chem. 10 1986 665 672
    • (1986) N. J. Chem. , vol.10 , pp. 665-672
    • Reisse, J.1
  • 71
    • 0035743583 scopus 로고    scopus 로고
    • Characterization of the effects of non-specific xenon-protein interactions on 129Xe chemical shifts in aqueous solution: Further development of xenon as a biomolecular probe
    • S.M. Rubin, M.M. Spence, A. Pines, and D.E. Wemmer Characterization of the effects of non-specific xenon-protein interactions on 129Xe chemical shifts in aqueous solution: further development of xenon as a biomolecular probe J. Magn. Reson. 152 2001 79 86
    • (2001) J. Magn. Reson. , vol.152 , pp. 79-86
    • Rubin, S.M.1    Spence, M.M.2    Pines, A.3    Wemmer, D.E.4
  • 74
    • 0017164076 scopus 로고
    • Comparison of the amino acid sequence of pig heart myoglobin with other ungulate myoglobins
    • J. Rousseaux, M. Dautrevaux, and K. Han Comparison of the amino acid sequence of pig heart myoglobin with other ungulate myoglobins Biochim. Biophys. Acta 439 1976 55 62
    • (1976) Biochim. Biophys. Acta , vol.439 , pp. 55-62
    • Rousseaux, J.1    Dautrevaux, M.2    Han, K.3
  • 75
    • 0025289622 scopus 로고
    • X-ray crystal structure of a recombinant human myoglobin mutant at 2.8 A resolution
    • DOI 10.1016/S0022-2836(05)80181-0
    • S.R. Hubbard, W.A. Hendrickson, D.G. Lambright, and S.G. Boxer X-ray crystal structure of a recombinant human myoglobin mutant at 2.8 A resolution J. Mol. Biol. 213 1990 215 218 (Pubitemid 20176530)
    • (1990) Journal of Molecular Biology , vol.213 , Issue.2 , pp. 215-218
    • Hubbard, S.R.1    Hendrickson, W.A.2    Lambright, D.G.3    Boxer, S.G.4


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