메뉴 건너뛰기




Volumn 92, Issue 10, 2007, Pages 3442-3447

Theoretical characterization of carbon monoxide vibrational spectrum in sperm whale myoglobin distal pocket

Author keywords

[No Author keywords available]

Indexed keywords

CARBON MONOXIDE; MYOGLOBIN;

EID: 34247849393     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.106.098442     Document Type: Article
Times cited : (25)

References (58)
  • 1
    • 34247875485 scopus 로고
    • X-ray studies of compounds of biological interest
    • Kendrew, J. C., and M. F. Perutz. 1957. X-ray studies of compounds of biological interest. Annu. Rev. Biochem. 26:327-372.
    • (1957) Annu. Rev. Biochem , vol.26 , pp. 327-372
    • Kendrew, J.C.1    Perutz, M.F.2
  • 3
    • 0021766921 scopus 로고    scopus 로고
    • Tilton, R. F., Jr., I. D. Kuntz, Jr., and G. A. Petsko. 1984. Cavities in proteins: structure of a metmyoglobin-xenon complex solved to 1.9 A. Biochemistry. 23:2849-2857.
    • Tilton, R. F., Jr., I. D. Kuntz, Jr., and G. A. Petsko. 1984. Cavities in proteins: structure of a metmyoglobin-xenon complex solved to 1.9 A. Biochemistry. 23:2849-2857.
  • 4
    • 0025600834 scopus 로고
    • Enhanced sampling in molecular dynamics: Use of the time-dependent Hartree approximation for a simulation of carbon monoxide diffusion through myoglobin
    • Elber, R., and M. Karplus. 1990. Enhanced sampling in molecular dynamics: use of the time-dependent Hartree approximation for a simulation of carbon monoxide diffusion through myoglobin. J. Am. Chem. Soc. 112:9161-9175.
    • (1990) J. Am. Chem. Soc , vol.112 , pp. 9161-9175
    • Elber, R.1    Karplus, M.2
  • 6
    • 0028519126 scopus 로고
    • Photolysis-induced structural changes in single crystals of carbonmonoxy myoglobin at 40 K
    • Teng, T. Y., V. Srajer, and K. Moffat. 1994. Photolysis-induced structural changes in single crystals of carbonmonoxy myoglobin at 40 K. Nat. Struct. Biol. 1:701-705.
    • (1994) Nat. Struct. Biol , vol.1 , pp. 701-705
    • Teng, T.Y.1    Srajer, V.2    Moffat, K.3
  • 8
    • 0030768765 scopus 로고    scopus 로고
    • Ligand migration in sperm whale myoglobin
    • Scott, E. E., and Q. H. Gibson. 1997. Ligand migration in sperm whale myoglobin. Biochemistry. 36:11909-11917.
    • (1997) Biochemistry , vol.36 , pp. 11909-11917
    • Scott, E.E.1    Gibson, Q.H.2
  • 9
    • 0031051369 scopus 로고    scopus 로고
    • A comparison between molecular dynamics and x-ray results for dissociated CO in myoglobin
    • Vitkup, D., G. A. Petsko, and M. Karplus. 1997. A comparison between molecular dynamics and x-ray results for dissociated CO in myoglobin. Nat. Struct. Biol. 4:202-208.
    • (1997) Nat. Struct. Biol , vol.4 , pp. 202-208
    • Vitkup, D.1    Petsko, G.A.2    Karplus, M.3
  • 10
    • 0031880931 scopus 로고    scopus 로고
    • Computer simulations of carbon monoxide photodissociation in myoglobin: Structural interpretation of the B states
    • Meller, J., and R. Elber. 1998. Computer simulations of carbon monoxide photodissociation in myoglobin: structural interpretation of the B states. Biophys. J. 74:789-802.
    • (1998) Biophys. J , vol.74 , pp. 789-802
    • Meller, J.1    Elber, R.2
  • 11
    • 0034519834 scopus 로고    scopus 로고
    • Trapping intermediates in the crystal: Ligand binding to myoglobin
    • Schlichting, I., and K. Chu. 2000. Trapping intermediates in the crystal: ligand binding to myoglobin. Curr. Opin. Struct. Biol. 10:744-752.
    • (2000) Curr. Opin. Struct. Biol , vol.10 , pp. 744-752
    • Schlichting, I.1    Chu, K.2
  • 13
    • 0035923445 scopus 로고    scopus 로고
    • Protein conformational relaxation and ligand migration in myoglobin: A nanosecond to millisecond molecular movie from time-resolved Laue x-ray diffraction
    • Srajer, V., Z. Ren, T. Y. Teng, M. Schmidt, T. Ursby, D. Bourgeois, C. Pradervand, W. Schildkamp, M. Wulff, and K. Moffat. 2001. Protein conformational relaxation and ligand migration in myoglobin: a nanosecond to millisecond molecular movie from time-resolved Laue x-ray diffraction. Biochemistry. 40:13802-13815.
    • (2001) Biochemistry , vol.40 , pp. 13802-13815
    • Srajer, V.1    Ren, Z.2    Teng, T.Y.3    Schmidt, M.4    Ursby, T.5    Bourgeois, D.6    Pradervand, C.7    Schildkamp, W.8    Wulff, M.9    Moffat, K.10
  • 14
    • 0037023751 scopus 로고    scopus 로고
    • Structural dynamics of myoglobin: Ligand migration among protein cavities studied by Fourier transform infrared/temperature derivative spectroscopy
    • Lamb, D. C., K. Nienhaus, A. Arcovito, F. Draghi, A. E. Miele, M. Brunori, and G. U. Nienhaus. 2002. Structural dynamics of myoglobin: ligand migration among protein cavities studied by Fourier transform infrared/temperature derivative spectroscopy. J. Biol. Chem. 277:11636-11644.
    • (2002) J. Biol. Chem , vol.277 , pp. 11636-11644
    • Lamb, D.C.1    Nienhaus, K.2    Arcovito, A.3    Draghi, F.4    Miele, A.E.5    Brunori, M.6    Nienhaus, G.U.7
  • 18
    • 2942655520 scopus 로고    scopus 로고
    • Extended molecular dynamics simulation of the carbon monoxide migration in sperm whale myoglobin
    • Bossa, C., M. Anselmi, D. Roccatano, A. Amadei, B. Vallone, M. Brunori, and A. Di Nola. 2004. Extended molecular dynamics simulation of the carbon monoxide migration in sperm whale myoglobin. Biophys. J. 86:3855-3862.
    • (2004) Biophys. J , vol.86 , pp. 3855-3862
    • Bossa, C.1    Anselmi, M.2    Roccatano, D.3    Amadei, A.4    Vallone, B.5    Brunori, M.6    Di Nola, A.7
  • 19
    • 1642619052 scopus 로고    scopus 로고
    • Structural dynamics of myoglobin: An infrared kinetic study of ligand migration in mutants YQR and YQRF
    • Lamb, D. C., A. Arcovito, K. Nienhaus, O. Minkow, F. Draghi, M. Brunori, and G. U. Nienhaus. 2004. Structural dynamics of myoglobin: an infrared kinetic study of ligand migration in mutants YQR and YQRF. Biophys. Chem. 109:41-58.
    • (2004) Biophys. Chem , vol.109 , pp. 41-58
    • Lamb, D.C.1    Arcovito, A.2    Nienhaus, K.3    Minkow, O.4    Draghi, F.5    Brunori, M.6    Nienhaus, G.U.7
  • 20
    • 23244457434 scopus 로고    scopus 로고
    • Molecular dynamics simulation of sperm whale myoglobin: Effects of mutations and trapped CO on the structure and dynamics of cavities
    • Bossa, C., A. Amadei, I. Daidone, M. Anselmi, B. Vallone, M. Brunori, and A. Di Nola. 2005. Molecular dynamics simulation of sperm whale myoglobin: effects of mutations and trapped CO on the structure and dynamics of cavities. Biophys. J. 89:465-474.
    • (2005) Biophys. J , vol.89 , pp. 465-474
    • Bossa, C.1    Amadei, A.2    Daidone, I.3    Anselmi, M.4    Vallone, B.5    Brunori, M.6    Di Nola, A.7
  • 22
    • 3042690149 scopus 로고    scopus 로고
    • Protein relaxation in the photodissociation of myoglobin-CO complexes
    • Angeloni, L., and A. Feis. 2003. Protein relaxation in the photodissociation of myoglobin-CO complexes. Photochem. Photobiol. Sci. 2:730-740.
    • (2003) Photochem. Photobiol. Sci , vol.2 , pp. 730-740
    • Angeloni, L.1    Feis, A.2
  • 23
    • 0042242570 scopus 로고    scopus 로고
    • Structural dynamics of myoglobin: Spectroscopic and structural characterization of ligand docking sites in myoglobin mutant L29W
    • Nienhaus, K., P. Deng, J. M. Kriegl, and G. U. Nienhaus. 2003. Structural dynamics of myoglobin: spectroscopic and structural characterization of ligand docking sites in myoglobin mutant L29W. Biochemistry. 42:9633-9646.
    • (2003) Biochemistry , vol.42 , pp. 9633-9646
    • Nienhaus, K.1    Deng, P.2    Kriegl, J.M.3    Nienhaus, G.U.4
  • 24
    • 0041742184 scopus 로고    scopus 로고
    • Structural dynamics of myoglobin: Effect of internal cavities on ligand migration and binding
    • Nienhaus, K., P. Deng, J. M. Kriegl, and G. U. Nienhaus. 2003. Structural dynamics of myoglobin: effect of internal cavities on ligand migration and binding. Biochemistry. 42:9647-9658.
    • (2003) Biochemistry , vol.42 , pp. 9647-9658
    • Nienhaus, K.1    Deng, P.2    Kriegl, J.M.3    Nienhaus, G.U.4
  • 25
    • 0028328331 scopus 로고
    • Structural determinants of the stretching frequency of CO bound to myoglobin
    • Li, T., M. L. Quillin, G. N. Phillips, Jr., and J. S. Olson. 1994. Structural determinants of the stretching frequency of CO bound to myoglobin. Biochemistry. 33:1433-1446.
    • (1994) Biochemistry , vol.33 , pp. 1433-1446
    • Li, T.1    Quillin, M.L.2    Phillips Jr., G.N.3    Olson, J.S.4
  • 26
    • 0036040539 scopus 로고    scopus 로고
    • Infrared study of carbon monoxide migration among internal cavities of myoglobin mutant L29W
    • Nienhaus, G. U., and K. Nienhaus. 2002. Infrared study of carbon monoxide migration among internal cavities of myoglobin mutant L29W. J. Biol. Phys. 28:163-172.
    • (2002) J. Biol. Phys , vol.28 , pp. 163-172
    • Nienhaus, G.U.1    Nienhaus, K.2
  • 27
    • 0029647452 scopus 로고
    • Binding of CO to myoglobin from a heme pocket docking site to form nearly linear Fe-CO
    • Lim, M., T. A. Jackson, and P. A. Anfinrud. 1995. Binding of CO to myoglobin from a heme pocket docking site to form nearly linear Fe-CO. Science. 269:962-966.
    • (1995) Science , vol.269 , pp. 962-966
    • Lim, M.1    Jackson, T.A.2    Anfinrud, P.A.3
  • 28
    • 36449006186 scopus 로고
    • Mid-infrared vibrational spectrum of CO after photodissociation from heme: Evidence for a ligand docking site in the heme pocket of hemoglobin and myoglobin
    • Lim, M., T. A. Jackson, and P. A. Anfinrud. 1995. Mid-infrared vibrational spectrum of CO after photodissociation from heme: evidence for a ligand docking site in the heme pocket of hemoglobin and myoglobin. J. Chem. Phys. 102:4355-4366.
    • (1995) J. Chem. Phys , vol.102 , pp. 4355-4366
    • Lim, M.1    Jackson, T.A.2    Anfinrud, P.A.3
  • 29
    • 0031054657 scopus 로고    scopus 로고
    • Ultrafast rotation and trapping of carbon monoxide dissociated from myoglobin
    • Lim, M., T. A. Jackson, and P. A. Anfinrud. 1997. Ultrafast rotation and trapping of carbon monoxide dissociated from myoglobin. Nat. Struct. Biol. 4:209-214.
    • (1997) Nat. Struct. Biol , vol.4 , pp. 209-214
    • Lim, M.1    Jackson, T.A.2    Anfinrud, P.A.3
  • 30
    • 0142242162 scopus 로고    scopus 로고
    • Structural dynamics of myoglobin: Ligand migration and binding in valine 68 mutants
    • Nienhaus, K., P. Deng, J. S. Olson, J. J. Warren, and G. U. Nienhaus. 2003. Structural dynamics of myoglobin: ligand migration and binding in valine 68 mutants. J. Biol. Chem. 278:42532-42544.
    • (2003) J. Biol. Chem , vol.278 , pp. 42532-42544
    • Nienhaus, K.1    Deng, P.2    Olson, J.S.3    Warren, J.J.4    Nienhaus, G.U.5
  • 31
    • 3042599461 scopus 로고    scopus 로고
    • Orientational distribution of CO before and after photolysis of MbCO and HbCO: A determination using time-resolved polarized Mid-IR spectroscopy
    • Lim, M., T. A. Jackson, and P. A. Anfinrud. 2004. Orientational distribution of CO before and after photolysis of MbCO and HbCO: a determination using time-resolved polarized Mid-IR spectroscopy. J. Am. Chem. Soc. 126:7946-7957.
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 7946-7957
    • Lim, M.1    Jackson, T.A.2    Anfinrud, P.A.3
  • 32
    • 17744370742 scopus 로고    scopus 로고
    • Picosecond dynamics of ligand interconversion in the primary docking site of heme proteins
    • Kim, S., and M. Lim. 2005. Picosecond dynamics of ligand interconversion in the primary docking site of heme proteins. J. Am. Chem. Soc. 127:5786-5787.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 5786-5787
    • Kim, S.1    Lim, M.2
  • 33
    • 11844258850 scopus 로고    scopus 로고
    • The origin of stark splitting in the initial photoproduct state of MbCO
    • Nienhaus, K., J. S. Olson, S. Franzen, and G. U. Nienhaus. 2005. The origin of stark splitting in the initial photoproduct state of MbCO. J. Am. Chem. Soc. 127:40-41.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 40-41
    • Nienhaus, K.1    Olson, J.S.2    Franzen, S.3    Nienhaus, G.U.4
  • 34
    • 0344551116 scopus 로고    scopus 로고
    • Theoretical investigation of infrared spectra and pocket dynamics of photodissociated carbonmonoxy myoglobin
    • Nutt, D. R., and M. Meuwly. 2003. Theoretical investigation of infrared spectra and pocket dynamics of photodissociated carbonmonoxy myoglobin. Biophys. J. 85:3612-3623.
    • (2003) Biophys. J , vol.85 , pp. 3612-3623
    • Nutt, D.R.1    Meuwly, M.2
  • 35
    • 1942501689 scopus 로고    scopus 로고
    • CO migration in native and mutant myoglobin: Atomistic simulations for the understanding of protein function
    • Nutt, D. R., and M. Meuwly. 2004. CO migration in native and mutant myoglobin: atomistic simulations for the understanding of protein function. Proc. Natl. Acad. Sci. USA. 101:5998-6002.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 5998-6002
    • Nutt, D.R.1    Meuwly, M.2
  • 36
    • 17444426056 scopus 로고    scopus 로고
    • Theoretical modeling of vibroelectronic quantum states in complex molecular systems: Solvated carbon monoxide, a test case
    • 122: article 124506
    • Amadei, A., F. Marinelli, M. D'Abramo, M. D'Alessandro, M. Anselmi, A. Di Nola, and M. Aschi. 2005. Theoretical modeling of vibroelectronic quantum states in complex molecular systems: solvated carbon monoxide, a test case. J. Chem. Phys. 122: article 124506.
    • (2005) J. Chem. Phys
    • Amadei, A.1    Marinelli, F.2    D'Abramo, M.3    D'Alessandro, M.4    Anselmi, M.5    Di Nola, A.6    Aschi, M.7
  • 37
    • 17444418604 scopus 로고    scopus 로고
    • D'Alessandro, M., F. Marinelli, M. D'Abramo, M. Aschi, A. Di Nola, and A. Amadei. 2005. Ground and excited electronic state thermodynamics of aqueous carbon monoxide: a theoretical study. J. Chem. Phys. 122: article 124507.
    • D'Alessandro, M., F. Marinelli, M. D'Abramo, M. Aschi, A. Di Nola, and A. Amadei. 2005. Ground and excited electronic state thermodynamics of aqueous carbon monoxide: a theoretical study. J. Chem. Phys. 122: article 124507.
  • 38
    • 0001321346 scopus 로고    scopus 로고
    • A first-principles method to model perturbed electronic wavefunctions: The effect of an external homogeneous electric field
    • Aschi, M., R. Spezia, A. Di Nola, and A. Amadei. 2001. A first-principles method to model perturbed electronic wavefunctions: the effect of an external homogeneous electric field. Chem. Phys. Lett. 344:374-380.
    • (2001) Chem. Phys. Lett , vol.344 , pp. 374-380
    • Aschi, M.1    Spezia, R.2    Di Nola, A.3    Amadei, A.4
  • 39
    • 0037073225 scopus 로고    scopus 로고
    • Extension of the perturbed matrix method: Application to a water molecule
    • Spezia, R., M. Aschi, A. Di Nola, and A. Amadei. 2002. Extension of the perturbed matrix method: application to a water molecule. Chem. Phys. Lett. 365:450-456.
    • (2002) Chem. Phys. Lett , vol.365 , pp. 450-456
    • Spezia, R.1    Aschi, M.2    Di Nola, A.3    Amadei, A.4
  • 40
    • 0002690528 scopus 로고
    • Molecular dynamics study of the photodissociation of carbon monoxide from myoglobin: Ligand dynamics in the first 10 ps
    • Straub, J. E., and M. Karplus. 1991. Molecular dynamics study of the photodissociation of carbon monoxide from myoglobin: ligand dynamics in the first 10 ps. Chem. Phys. 158:221-248.
    • (1991) Chem. Phys , vol.158 , pp. 221-248
    • Straub, J.E.1    Karplus, M.2
  • 41
    • 0033574735 scopus 로고    scopus 로고
    • A steric mechanism for inhibition of CO binding to heme proteins
    • Kachalova, G. S., A. N. Popov, and H. D. Bartunik. 1999. A steric mechanism for inhibition of CO binding to heme proteins. Science. 284:473-476.
    • (1999) Science , vol.284 , pp. 473-476
    • Kachalova, G.S.1    Popov, A.N.2    Bartunik, H.D.3
  • 42
    • 14644398597 scopus 로고    scopus 로고
    • Quantum chemical evaluation of protein control over heme ligation: CO/O2 discrimination in myoglobin
    • De Angelis, F., A. A. Jarzecki, R. Car, and T. G. Spiro. 2005. Quantum chemical evaluation of protein control over heme ligation: CO/O2 discrimination in myoglobin. J. Phys. Chem. B. 109:3065-3070.
    • (2005) J. Phys. Chem. B , vol.109 , pp. 3065-3070
    • De Angelis, F.1    Jarzecki, A.A.2    Car, R.3    Spiro, T.G.4
  • 43
    • 0002775934 scopus 로고
    • Interaction models for water in relation to protein hydration
    • Pullman, B, editor. D. Reidel Publishing Company, Dordrecht, The Netherlands
    • Berendsen, H. J. C., J. P. M. Postma, W. F. van Gunsteren, and J. Hermans. 1981. Interaction models for water in relation to protein hydration. In Intermolecular Forces. Pullman, B., editor. D. Reidel Publishing Company, Dordrecht, The Netherlands. 331-342.
    • (1981) Intermolecular Forces , pp. 331-342
    • Berendsen, H.J.C.1    Postma, J.P.M.2    van Gunsteren, W.F.3    Hermans, J.4
  • 44
    • 0029633168 scopus 로고
    • GROMACS: A message-passing parallel molecular dynamics implementation
    • Berendsen, H. J. C., D. van der Spoel, and R. van Drunen. 1995. GROMACS: A message-passing parallel molecular dynamics implementation. Comp. Phys. Comm. 91:43-56.
    • (1995) Comp. Phys. Comm , vol.91 , pp. 43-56
    • Berendsen, H.J.C.1    van der Spoel, D.2    van Drunen, R.3
  • 47
    • 0000388705 scopus 로고    scopus 로고
    • LINCS: A linear constraint solver for molecular simulations
    • Hess, B., H. Bekker, H. J. C. Berendsen, and J. G. E. M. Fraaije. 1997. LINCS: a linear constraint solver for molecular simulations. J. Comput. Chem. 18:1463-1472.
    • (1997) J. Comput. Chem , vol.18 , pp. 1463-1472
    • Hess, B.1    Bekker, H.2    Berendsen, H.J.C.3    Fraaije, J.G.E.M.4
  • 48
    • 0002178685 scopus 로고    scopus 로고
    • Molecular dynamics simulations with constrained rototranslational motions: Theoretical basis and statistical mechanical consistency
    • Amadei, A., G. Chillemi, M. A. Ceruso, A. Grottesi, and A. Di Nola. 2000. Molecular dynamics simulations with constrained rototranslational motions: Theoretical basis and statistical mechanical consistency. J. Chem. Phys. 112:9-23.
    • (2000) J. Chem. Phys , vol.112 , pp. 9-23
    • Amadei, A.1    Chillemi, G.2    Ceruso, M.A.3    Grottesi, A.4    Di Nola, A.5
  • 50
    • 0000189651 scopus 로고
    • Density-functional thermochemistry. III. The role of exact exchange
    • Becke, A. D. 1993. Density-functional thermochemistry. III. The role of exact exchange. J. Chem. Phys. 98:5648-5652.
    • (1993) J. Chem. Phys , vol.98 , pp. 5648-5652
    • Becke, A.D.1
  • 51
    • 0345491105 scopus 로고
    • Development of the Colle-Salvetti correlation-energy formula into a functional of the electron density
    • Lee, C., W. Yang, and R. G. Parr. 1988. Development of the Colle-Salvetti correlation-energy formula into a functional of the electron density. Phys. Rev. B. 37:785-789.
    • (1988) Phys. Rev. B , vol.37 , pp. 785-789
    • Lee, C.1    Yang, W.2    Parr, R.G.3
  • 52
    • 33746614482 scopus 로고
    • Gaussian basis sets for use in correlated molecular calculations. I. The atoms boron through neon and hydrogen
    • Dunning, T. H., Jr. 1989. Gaussian basis sets for use in correlated molecular calculations. I. The atoms boron through neon and hydrogen. J. Chem. Phys. 90:1007-1023.
    • (1989) J. Chem. Phys , vol.90 , pp. 1007-1023
    • Dunning Jr., T.H.1
  • 53
    • 0001206302 scopus 로고
    • The graphical unitary group approach to the electron correlation problem. Methods and preliminary applications
    • Brooks, B. R., and H. F. Schaefer III. 1979. The graphical unitary group approach to the electron correlation problem. Methods and preliminary applications. J. Chem. Phys. 70:5092-5106.
    • (1979) J. Chem. Phys , vol.70 , pp. 5092-5106
    • Brooks, B.R.1    Schaefer III, H.F.2
  • 55
    • 33745010649 scopus 로고    scopus 로고
    • On the importance of configurational sampling in theoretical calculation of electronic properties of complex molecular systems: Acetone in water
    • D'Abramo, M., M. Aschi, A. Di Nola, and A. Amadei. 2006. On the importance of configurational sampling in theoretical calculation of electronic properties of complex molecular systems: Acetone in water. Chem. Phys. Lett. 424:289-294.
    • (2006) Chem. Phys. Lett , vol.424 , pp. 289-294
    • D'Abramo, M.1    Aschi, M.2    Di Nola, A.3    Amadei, A.4
  • 56
    • 18744389484 scopus 로고    scopus 로고
    • Quantum corrections in vibrational and electronic condensed phase spectroscopy: Line shapes and echoes
    • Lawrence, C. P., and J. L. Skinner. 2005. Quantum corrections in vibrational and electronic condensed phase spectroscopy: line shapes and echoes. Proc. Natl. Acad. Sci. USA. 102:6720-6725.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 6720-6725
    • Lawrence, C.P.1    Skinner, J.L.2
  • 58
    • 0030936852 scopus 로고    scopus 로고
    • Molecolar dynamics simulation study of the B-states of solvated carbon monoxymyoglobin
    • Ma, J., S. Huo, and J. E. Straub. 1997. Molecolar dynamics simulation study of the B-states of solvated carbon monoxymyoglobin. J. Am. Chem. Soc. 119:2541-2551.
    • (1997) J. Am. Chem. Soc , vol.119 , pp. 2541-2551
    • Ma, J.1    Huo, S.2    Straub, J.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.