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Volumn 147, Issue 1, 2000, Pages 1-8

Protein Hydration and Location of Water Molecules in Oxidized Horse Heart Cytochrome c by 1H NMR

Author keywords

Heme proteins; Paramagnetic systems; Protein hydrophilicity; Protein NMR; Proton exchange; Water protein interactions

Indexed keywords

CYTOCHROME C; WATER;

EID: 0034330017     PISSN: 10907807     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmre.2000.2131     Document Type: Article
Times cited : (23)

References (64)
  • 1
    • 0020861687 scopus 로고
    • Water and proteins. II: The location and dynamics of water in protein systems and its relation to their stability properties
    • J. T. Edsall and H. A. McKenzie, Water and proteins. II: The location and dynamics of water in protein systems and its relation to their stability properties, Adv. Biophys. 16, 53-183 (1983).
    • (1983) Adv. Biophys. , vol.16 , pp. 53-183
    • Edsall, J.T.1    McKenzie, H.A.2
  • 2
    • 0030325741 scopus 로고    scopus 로고
    • Protein hydration dynamics in acqueous solution
    • V. P. Denisov and B. Halle, Protein hydration dynamics in acqueous solution, Faraday Discuss. 103, 227-244 (1996).
    • (1996) Faraday Discuss. , vol.103 , pp. 227-244
    • Denisov, V.P.1    Halle, B.2
  • 3
    • 0026326956 scopus 로고
    • Protein hydration in aqueous solution
    • G. Otting, E. Liepinsh, and K. Wüthrich, Protein hydration in aqueous solution, Science 254, 974-980 (1991).
    • (1991) Science , vol.254 , pp. 974-980
    • Otting, G.1    Liepinsh, E.2    Wüthrich, K.3
  • 5
    • 0028220311 scopus 로고
    • The role of conserved internal water molecule and its associated hydrogen bond network in cytochrome c
    • A. M. Berghuis, J. G. Guillemette, G. McLendon, F. Sherman, M. Smith, and G. D. Brayer, The role of conserved internal water molecule and its associated hydrogen bond network in cytochrome c, J. Mol. Biol. 236, 786-799 (1994).
    • (1994) J. Mol. Biol. , vol.236 , pp. 786-799
    • Berghuis, A.M.1    Guillemette, J.G.2    McLendon, G.3    Sherman, F.4    Smith, M.5    Brayer, G.D.6
  • 6
    • 0000764227 scopus 로고
    • NMR detection of hydration water in the intermolecular interface of a protein-DNa complex
    • Y. Q. Qian, G. Otting, and K. Wüthrich, NMR detection of hydration water in the intermolecular interface of a protein-DNA complex, J. Am. Chem. Soc. 115, 1189-1190 (1993).
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 1189-1190
    • Qian, Y.Q.1    Otting, G.2    Wüthrich, K.3
  • 7
    • 0027068111 scopus 로고
    • Buried water in homologous serine proteases
    • U. Sreenivasan and P. H. Axelsen, Buried water in homologous serine proteases, Biochemistry 31, 12785-12791 (1992).
    • (1992) Biochemistry , vol.31 , pp. 12785-12791
    • Sreenivasan, U.1    Axelsen, P.H.2
  • 8
    • 0021782926 scopus 로고
    • The application of neutron crystallography to the study of dynamic and hydration properties of proteins
    • A. A. Kossiakoff, The application of neutron crystallography to the study of dynamic and hydration properties of proteins, Annu. Rev. Biochem. 54, 1195-1227 (1985).
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 1195-1227
    • Kossiakoff, A.A.1
  • 9
    • 0000701443 scopus 로고
    • Computer simulation of the dynamics of hydrated protein crystals and its comparison with X-ray data
    • W. F. van Gunsteren, H. J. C. Berendsen, J. Hermans, W. G. Hol, and J. P. Postma, Computer simulation of the dynamics of hydrated protein crystals and its comparison with X-ray data, Proc. Natl. Acad. Sci. USA 80, 4315-4319 (1983).
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 4315-4319
    • Van Gunsteren, W.F.1    Berendsen, H.J.C.2    Hermans, J.3    Hol, W.G.4    Postma, J.P.5
  • 10
    • 0026556022 scopus 로고
    • On the interpretation of biochemical data by molecular dynamics computer simulation
    • W. F. van Gunsteren and A. E. Mark, On the interpretation of biochemical data by molecular dynamics computer simulation, Eur. J. Biochem. 204, 947-961 (1992).
    • (1992) Eur. J. Biochem. , vol.204 , pp. 947-961
    • Van Gunsteren, W.F.1    Mark, A.E.2
  • 11
    • 0001073393 scopus 로고
    • The dynamics of water-protein interactions. Results from measurements of nuclear magnetic relaxation dispersion
    • S. H. Koenig and R. D. Brown III, The dynamics of water-protein interactions. Results from measurements of nuclear magnetic relaxation dispersion, Prog. NMR Spectrosc. 22, 487-567 (1991).
    • (1991) Prog. NMR Spectrosc. , vol.22 , pp. 487-567
    • Koenig, S.H.1    Brown R.D. III2
  • 12
    • 0028105204 scopus 로고
    • Dynamics of the internal and external hydration of globular proteins
    • V. P. Denisov and B. Halle, Dynamics of the internal and external hydration of globular proteins, J. Am. Chem. Soc. 116, 10324-10325 (1994).
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 10324-10325
    • Denisov, V.P.1    Halle, B.2
  • 13
    • 0030919951 scopus 로고    scopus 로고
    • 1H magnetic relaxation dispersion in protein solutions. a quantitative assessment of internal hydration, proton exchange, and cross-relaxation
    • 1H magnetic relaxation dispersion in protein solutions. A quantitative assessment of internal hydration, proton exchange, and cross-relaxation, J. Am. Chem. Soc. 119, 3122-3134 (1997).
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 3122-3134
    • Venu, K.1    Denisov, V.P.2    Halle, B.3
  • 14
    • 0028871018 scopus 로고
    • Direct observation of calcium-coordinated water in Calbindin D9k by nuclear magnetic relaxation dispersion
    • V. P. Denisov and B. Halle, Direct observation of calcium-coordinated water in Calbindin D9k by nuclear magnetic relaxation dispersion, J. Am. Chem. Soc. 117, 8456-8465 (1995).
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 8456-8465
    • Denisov, V.P.1    Halle, B.2
  • 15
    • 0001335514 scopus 로고    scopus 로고
    • NMR studies on Phtalate Dioxygenase: Evidence for displacement of water on binding substrate
    • I. Bertini, C. Luchinat, G. Mincione, G. Parigi, G. T. Gassner, and D. P. Ballou, NMR studies on Phtalate Dioxygenase: Evidence for displacement of water on binding substrate, JBIC 1, 468-475 (1996).
    • (1996) JBIC , vol.1 , pp. 468-475
    • Bertini, I.1    Luchinat, C.2    Mincione, G.3    Parigi, G.4    Gassner, G.T.5    Ballou, D.P.6
  • 16
    • 0000857486 scopus 로고
    • Studies of protein hydration in aqueous solution by direct NMR observation in individual protein-bound water molecules
    • G. Otting and K. Wüthrich, Studies of protein hydration in aqueous solution by direct NMR observation in individual protein-bound water molecules, J. Am. Chem. Soc. 111, 1871-1875 (1989).
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 1871-1875
    • Otting, G.1    Wüthrich, K.2
  • 17
    • 0000547870 scopus 로고
    • Protein hydration viewed by high-resolution NMR spectroscopy: Implications for magnetic resonance image contrast
    • G. Otting and E. Liepinsh, Protein hydration viewed by high-resolution NMR spectroscopy: Implications for magnetic resonance image contrast, Acc. Chem. Res. 28, 171-177 (1995).
    • (1995) Acc. Chem. Res. , vol.28 , pp. 171-177
    • Otting, G.1    Liepinsh, E.2
  • 18
    • 0003233568 scopus 로고    scopus 로고
    • NMR studies of water bound to biological molecules
    • G. Otting, NMR studies of water bound to biological molecules, Prog. NMR Spectrosc. 31, 259-285 (1997).
    • (1997) Prog. NMR Spectrosc. , vol.31 , pp. 259-285
    • Otting, G.1
  • 19
    • 0027456532 scopus 로고
    • Heteronuclear 3D studies of water bound to an FK506 binding protein/immunosuppressant complex
    • R. X. Xu, R. P. Meadows, and S. W. Fesik, Heteronuclear 3D studies of water bound to an FK506 binding protein/immunosuppressant complex, Biochemistry 32, 2473-2480 (1993).
    • (1993) Biochemistry , vol.32 , pp. 2473-2480
    • Xu, R.X.1    Meadows, R.P.2    Fesik, S.W.3
  • 20
    • 0000961515 scopus 로고    scopus 로고
    • Technical aspects of NMR spectroscopy with biological macromolecules and studies of hydration in solution
    • G. Wider, Technical aspects of NMR spectroscopy with biological macromolecules and studies of hydration in solution, Prog. NMR Spectrosc. 32, 193-275 (1998).
    • (1998) Prog. NMR Spectrosc. , vol.32 , pp. 193-275
    • Wider, G.1
  • 21
    • 0032006812 scopus 로고    scopus 로고
    • Bound water in apo and holo bovine heart fatty-acid-binding protein determined by heteronuclear NMR spectroscopy
    • A. Mesgarzadeh, S. Pfeiffer, I. Engelke, D. Lassen, and H. Rüterjans, Bound water in apo and holo bovine heart fatty-acid-binding protein determined by heteronuclear NMR spectroscopy, Eur. J. Biochem. 251, 781-786 (1998).
    • (1998) Eur. J. Biochem. , vol.251 , pp. 781-786
    • Mesgarzadeh, A.1    Pfeiffer, S.2    Engelke, I.3    Lassen, D.4    Rüterjans, H.5
  • 25
    • 0033069433 scopus 로고    scopus 로고
    • Editing of chemical exchange-relayed NOEs in NMR experiments for the observation of protein-water interactions
    • G. Melacini, R. Kaptein, and R. Boelens, Editing of chemical exchange-relayed NOEs in NMR experiments for the observation of protein-water interactions, J. Magn. Reson. 136, 214-218 (1999).
    • (1999) J. Magn. Reson. , vol.136 , pp. 214-218
    • Melacini, G.1    Kaptein, R.2    Boelens, R.3
  • 29
    • 0025234717 scopus 로고
    • Redox dependent structure change and hyperfine nuclear magnetic resonance shifts in cytochrome c
    • Y. Q. Feng, H. Roder, and S. W. Englander, Redox dependent structure change and hyperfine nuclear magnetic resonance shifts in cytochrome c, Biochemistry 29, 3494-3504 (1990).
    • (1990) Biochemistry , vol.29 , pp. 3494-3504
    • Feng, Y.Q.1    Roder, H.2    Englander, S.W.3
  • 31
    • 0028246555 scopus 로고
    • Solution structure of horse heart ferrocytochrome c determined by high-resolution NMR and restrained simulated annealing
    • P. X. Qi, D. L. Di Stefano, and A. J. Wand, Solution structure of horse heart ferrocytochrome c determined by high-resolution NMR and restrained simulated annealing, Biochemistry 33, 6408-6417 (1994).
    • (1994) Biochemistry , vol.33 , pp. 6408-6417
    • Qi, P.X.1    Di Stefano, D.L.2    Wand, A.J.3
  • 33
  • 34
    • 0025007598 scopus 로고
    • High-resolution three-dimensional structure of horse heart cytochrome c
    • G. W. Bushnell, G. V. Louie, and G. D. Brayer, High-resolution three-dimensional structure of horse heart cytochrome c, J. Mol. Biol. 214, 585-595 (1990).
    • (1990) J. Mol. Biol. , vol.214 , pp. 585-595
    • Bushnell, G.W.1    Louie, G.V.2    Brayer, G.D.3
  • 35
    • 0028847055 scopus 로고
    • Entropic stabilization of cytochrome c upon reduction
    • D. S. Cohen and G. J. Pielak, Entropic stabilization of cytochrome c upon reduction, J. Am. Chem. Soc. 117, 1675-1677 (1995).
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 1675-1677
    • Cohen, D.S.1    Pielak, G.J.2
  • 36
    • 0030881179 scopus 로고    scopus 로고
    • ePHOGSY experiment on a paramagnetic protein: Location of the catalytic water molecule in the heme crevice of the oxidized form of horse heart cytochrome c
    • I. Bertini, C. Dalvit, J. G. Huber, C. Luchinat, and M. Piccioli, ePHOGSY experiment on a paramagnetic protein: Location of the catalytic water molecule in the heme crevice of the oxidized form of horse heart cytochrome c, FEBS Lett. 415, 45-48 (1997).
    • (1997) FEBS Lett. , vol.415 , pp. 45-48
    • Bertini, I.1    Dalvit, C.2    Huber, J.G.3    Luchinat, C.4    Piccioli, M.5
  • 38
    • 0000427691 scopus 로고    scopus 로고
    • Homonuclear 1D and 2D NMR experiments for the observation of solvent-solute interactions
    • C. Dalvit, Homonuclear 1D and 2D NMR experiments for the observation of solvent-solute interactions, J. Magn. Reson. Ser. B 112, 282-288 (1996).
    • (1996) J. Magn. Reson. Ser. B , vol.112 , pp. 282-288
    • Dalvit, C.1
  • 39
    • 0001357001 scopus 로고
    • Sensitivity-improved detection of protein hydration and its extension to the assignment of fast-exchanging resonances
    • C. Dalvit and U. Hommel, Sensitivity-improved detection of protein hydration and its extension to the assignment of fast-exchanging resonances, J. Magn. Reson. Ser. B 109, 334-338 (1995).
    • (1995) J. Magn. Reson. Ser. B , vol.109 , pp. 334-338
    • Dalvit, C.1    Hommel, U.2
  • 40
    • 0000427672 scopus 로고
    • New pulsed field gradient NMR experiments for the detection of bound water in proteins
    • C. Dalvit and U. Hommel, New pulsed field gradient NMR experiments for the detection of bound water in proteins, J. Biomol. NMR 5, 306-310 (1995).
    • (1995) J. Biomol. NMR , vol.5 , pp. 306-310
    • Dalvit, C.1    Hommel, U.2
  • 41
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single quantum NMR spectroscopy of aqueous solutions
    • M. Piotto, V. Saudek, and V. Sklenar, Gradient-tailored excitation for single quantum NMR spectroscopy of aqueous solutions, J. Biomol. NMR 2, 661-666 (1992).
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-666
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 43
    • 0031992911 scopus 로고    scopus 로고
    • Solvent magnetization artifacts in high-field NMR studies of macromolecular hydration
    • A. G. Sobol, G. Wider, H. Iwai, and K. Wüthrich, Solvent magnetization artifacts in high-field NMR studies of macromolecular hydration, J. Am. Chem. Soc. 130, 262-271 (1998).
    • (1998) J. Am. Chem. Soc. , vol.130 , pp. 262-271
    • Sobol, A.G.1    Wider, G.2    Iwai, H.3    Wüthrich, K.4
  • 44
    • 0021114895 scopus 로고
    • Application of phase-sensitive correlated spectroscopy (COSY) for measurements of proton-proton spin-spin coupling constants in proteins
    • D. Marion and K. Wüthrich, Application of phase-sensitive correlated spectroscopy (COSY) for measurements of proton-proton spin-spin coupling constants in proteins, Biochem. Biophys. Res. Commun. 113, 967-974 (1983).
    • (1983) Biochem. Biophys. Res. Commun. , vol.113 , pp. 967-974
    • Marion, D.1    Wüthrich, K.2
  • 45
    • 84915716471 scopus 로고
    • Elucidation of cross relaxation in liquids by two-dimensional NMR spectroscopy
    • S. Macura and R. R. Ernst, Elucidation of cross relaxation in liquids by two-dimensional NMR spectroscopy, Mol. Phys. 41, 95-95 (1980).
    • (1980) Mol. Phys. , vol.41 , pp. 95-95
    • Macura, S.1    Ernst, R.R.2
  • 46
    • 0030797606 scopus 로고    scopus 로고
    • Application of phase-modulated CLEAN chemical Exchange Spectroscopy (CLEANEX-PM) to detect water-protein proton exchange and intermolecular NOEs
    • T. L. Hwang, S. Mori, A. J. Shaka, and P. C. M. van Zijl, Application of phase-modulated CLEAN chemical Exchange Spectroscopy (CLEANEX-PM) to detect water-protein proton exchange and intermolecular NOEs, J. Am. Chem. Soc. 119, 6203-6204 (1998).
    • (1998) J. Am. Chem. Soc. , vol.119 , pp. 6203-6204
    • Hwang, T.L.1    Mori, S.2    Shaka, A.J.3    Van Zijl, P.C.M.4
  • 47
    • 0029693096 scopus 로고    scopus 로고
    • Separation of intramolecular NOE and exchange peaks in water exchange spectroscopy using spin echo filters
    • S. Mori, J. Berg, and P. C. M. van Zijl, Separation of intramolecular NOE and exchange peaks in water exchange spectroscopy using spin echo filters, J. Biomol. NMR 7, 77-82 (1996).
    • (1996) J. Biomol. NMR , vol.7 , pp. 77-82
    • Mori, S.1    Berg, J.2    Van Zijl, P.C.M.3
  • 48
    • 0029912597 scopus 로고    scopus 로고
    • Diffusion filters for separation of solvent-protein and protein-protein nuclear Overhauser effects (HYDRA)
    • G. Wider, R. Riek, and K. Wüthrich, Diffusion filters for separation of solvent-protein and protein-protein nuclear Overhauser effects (HYDRA), J. Am. Chem. Soc. 118, 11629-11634 (1996).
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 11629-11634
    • Wider, G.1    Riek, R.2    Wüthrich, K.3
  • 49
    • 0026410969 scopus 로고
    • Relationship between nuclear magnetic resonance chemical shift and protein secondary structure
    • D. S. Wishart, B. D. Sykes, and F. M. Richards, Relationship between nuclear magnetic resonance chemical shift and protein secondary structure, J. Mol. Biol. 222, 311-333 (1991).
    • (1991) J. Mol. Biol. , vol.222 , pp. 311-333
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 50
    • 0029864396 scopus 로고    scopus 로고
    • 15N-labeled proteins by a straightforward water selective NOESY-HSQC experiment
    • 15N-labeled proteins by a straightforward water selective NOESY-HSQC experiment, FEBS Lett. 383, 191-195 (1996).
    • (1996) FEBS Lett. , vol.383 , pp. 191-195
    • Böckmann, A.1    Penin, F.2    Guittet, E.3
  • 51
    • 0029685015 scopus 로고    scopus 로고
    • Water exchange filter with improved sensitivity (WEX II) to study solvent-exchangeable protons. Application to the consensus zinc finger peptide CP-1
    • S. Mori, C. Abeygunawardana, and P. C. M. van Zijl, Water exchange filter with improved sensitivity (WEX II) to study solvent-exchangeable protons. Application to the consensus zinc finger peptide CP-1, J. Magn. Reson. Ser. B 110, 96-101 (1996).
    • (1996) J. Magn. Reson. Ser. B , vol.110 , pp. 96-101
    • Mori, S.1    Abeygunawardana, C.2    Van Zijl, P.C.M.3
  • 54
    • 0031989849 scopus 로고    scopus 로고
    • Accurate quantification of water-amide proton exchange rates using the Phase-Modulated CLEAN chemical Exchange (CLEANEX-PM) approach with a Fast-HSQC (FHSQC) detection scheme
    • T. L. Hwang, P. C. M. van Zijl, and S. Mori, Accurate quantification of water-amide proton exchange rates using the Phase-Modulated CLEAN chemical Exchange (CLEANEX-PM) approach with a Fast-HSQC (FHSQC) detection scheme, J. Biomol. NMR 11, 221-226 (1998).
    • (1998) J. Biomol. NMR , vol.11 , pp. 221-226
    • Hwang, T.L.1    Van Zijl, P.C.M.2    Mori, S.3
  • 55
    • 0030691160 scopus 로고    scopus 로고
    • A molecular dynamics study in explicit water of the reduced and oxidized forms of yeast iso-1-cytochrome c. Solvation and dynamic properties of the two oxidation states
    • L. Banci, G. Gori Savellini, and P. Turano, A molecular dynamics study in explicit water of the reduced and oxidized forms of yeast iso-1-cytochrome c. Solvation and dynamic properties of the two oxidation states, Eur. J. Biochem. 249, 716-723 (1997).
    • (1997) Eur. J. Biochem. , vol.249 , pp. 716-723
    • Banci, L.1    Gori Savellini, G.2    Turano, P.3
  • 56
    • 0026608669 scopus 로고
    • Oxidation state-dependent conformational changes in cytochrome c
    • A. M. Berghuis and G. D. Brayer, Oxidation state-dependent conformational changes in cytochrome c, J. Mol. Biol. 223, 959-976 (1992).
    • (1992) J. Mol. Biol. , vol.223 , pp. 959-976
    • Berghuis, A.M.1    Brayer, G.D.2
  • 58
    • 0019888623 scopus 로고
    • Conformation change of cytochrome c: I. Ferrocytochrome c structure refined at 1.5 Å resolution
    • T. Takano and R. E. Dickerson, Conformation change of cytochrome c: I. Ferrocytochrome c structure refined at 1.5 Å resolution, J. Mol. Biol. 153, 79-94 (1981).
    • (1981) J. Mol. Biol. , vol.153 , pp. 79-94
    • Takano, T.1    Dickerson, R.E.2
  • 59
    • 0019888571 scopus 로고
    • Conformation change in cytochrome c: II. Ferricytochrome c refinement at 1.8 Å and comparison with ferrocytochrome c structure
    • T. Takano and R. E. Dickerson, Conformation change in cytochrome c: II. Ferricytochrome c refinement at 1.8 Å and comparison with ferrocytochrome c structure, J. Mol. Biol. 153, 95-155 (1981).
    • (1981) J. Mol. Biol. , vol.153 , pp. 95-155
    • Takano, T.1    Dickerson, R.E.2
  • 60
    • 0025146477 scopus 로고
    • High-resolution refinement of yeast iso-1-cytochrome c and comparison with other eukaryotic cytochromes
    • G. V. Louie and G. D. Brayer, High-resolution refinement of yeast iso-1-cytochrome c and comparison with other eukaryotic cytochromes, J. Mol. Biol. 214, 527-555 (1990).
    • (1990) J. Mol. Biol. , vol.214 , pp. 527-555
    • Louie, G.V.1    Brayer, G.D.2
  • 61
    • 0029081424 scopus 로고
    • Residence times of the buried water molecules in bovine pacreatic trypsin inhibitor and its G36S mutant
    • V. P. Denisov, B. Halle, J. Peters, and H. D. Horlein, Residence times of the buried water molecules in bovine pacreatic trypsin inhibitor and its G36S mutant, Biochemistry 34, 9046-9051 (1995).
    • (1995) Biochemistry , vol.34 , pp. 9046-9051
    • Denisov, V.P.1    Halle, B.2    Peters, J.3    Horlein, H.D.4
  • 62
    • 0029994817 scopus 로고    scopus 로고
    • Using buried water molecules to explore the energy landscape of proteins
    • V. P. Denisov, J. Peters, H. D. Horlein, and B. Halle, Using buried water molecules to explore the energy landscape of proteins, Nature Struct. Biol. 3, 505-509 (1996).
    • (1996) Nature Struct. Biol. , vol.3 , pp. 505-509
    • Denisov, V.P.1    Peters, J.2    Horlein, H.D.3    Halle, B.4
  • 63
    • 0000837519 scopus 로고    scopus 로고
    • Structural studies of eukariotic cytochromes c
    • R. A. Scott and A. G. Mauk, Eds., University Science Books, Sausalito, CA
    • G. D. Brayer and M. E. P. Murphy, Structural studies of eukariotic cytochromes c, in "Cytochrome c. A Multidisciplinary Approach" (R. A. Scott and A. G. Mauk, Eds.), pp. 103-166, University Science Books, Sausalito, CA (1996).
    • (1996) Cytochrome c. A Multidisciplinary Approach , pp. 103-166
    • Brayer, G.D.1    Murphy, M.E.P.2
  • 64
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structure
    • R. Koradi, M. Billeter, and K. Wüthrich, MOLMOL: A program for display and analysis of macromolecular structure, J. Mol. Graphics 14, 51-55 (1996).
    • (1996) J. Mol. Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3


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