메뉴 건너뛰기




Volumn 7, Issue 11, 1998, Pages 2301-2313

Effects of pressure on the structure of metmyoglobin: Molecular dynamics predictions for pressure unfolding through a molten globule intermediate

Author keywords

Molecular dynamics; Molten globule; Myoglobin; Pressure; Unfolding

Indexed keywords

METMYOGLOBIN;

EID: 0031791378     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560071107     Document Type: Article
Times cited : (21)

References (50)
  • 2
    • 0026703657 scopus 로고
    • Haute pression et biologie: Une dé-marche d'avenir
    • Balny C, Heremans K, Masson P. 1992. Haute pression et biologie: Une dé-marche d'avenir. Biofutur 112:37-40.
    • (1992) Biofutur , vol.112 , pp. 37-40
    • Balny, C.1    Heremans, K.2    Masson, P.3
  • 3
    • 0023176681 scopus 로고
    • Determinants of a protein folding: Unique features of the globin amino acid sequences
    • Bashford D, Chotia C, Lesk AM. 1987. Determinants of a protein folding: Unique features of the globin amino acid sequences. J Mol Biol 196:199-216.
    • (1987) J Mol Biol , vol.196 , pp. 199-216
    • Bashford, D.1    Chotia, C.2    Lesk, A.M.3
  • 4
    • 0030031755 scopus 로고    scopus 로고
    • Pressure-induced perturbation of ans-apomyoglobin complex: Frequency-domain fluorescence studies on native and acidic compact states
    • Bismuto E, Irace G, Sirangelo I, Gratton E. 1996a. Pressure-induced perturbation of ans-apomyoglobin complex: Frequency-domain fluorescence studies on native and acidic compact states. Protein Sci 5:121-126.
    • (1996) Protein Sci , vol.5 , pp. 121-126
    • Bismuto, E.1    Irace, G.2    Sirangelo, I.3    Gratton, E.4
  • 5
    • 0030048876 scopus 로고    scopus 로고
    • Pressure-induced perturbation of apomyoglobin structure: Fluorescence studies on native and acidic compact forms
    • Bismuto E, Sirangelo I, Irace G, Gratton E. 1996b. Pressure-induced perturbation of apomyoglobin structure: Fluorescence studies on native and acidic compact forms. Biochemistry 35:1173-1178.
    • (1996) Biochemistry , vol.35 , pp. 1173-1178
    • Bismuto, E.1    Sirangelo, I.2    Irace, G.3    Gratton, E.4
  • 6
    • 33646923521 scopus 로고
    • Thermodynamics of electrolytes. Dielectric properties of water and Debye-Huckel parameters to 350°C and 1kbar
    • Bradley DJ, Pitzer KS. 1979. Thermodynamics of electrolytes. Dielectric properties of water and Debye-Huckel parameters to 350°C and 1kbar. J Phys Chem 83:1599-1603.
    • (1979) J Phys Chem , vol.83 , pp. 1599-1603
    • Bradley, D.J.1    Pitzer, K.S.2
  • 7
    • 0028264083 scopus 로고
    • Kinetic-study on myoglobin refolding monitored by 5 optical probe stopped-flow methods
    • Chiba K, Ikai A, Kawamurakonishi Y, Kihara H. 1994. Kinetic-study on myoglobin refolding monitored by 5 optical probe stopped-flow methods. Proteins 19:110-119.
    • (1994) Proteins , vol.19 , pp. 110-119
    • Chiba, K.1    Ikai, A.2    Kawamurakonishi, Y.3    Kihara, H.4
  • 8
    • 0019874678 scopus 로고
    • Effect of hydrostatic pressure on lyzozyme and chymotripsinogen detected by fluorescence polarization
    • Chryssomallis GS, Torgerson PM, Drickamer HG, Weber G. 1981. Effect of hydrostatic pressure on lyzozyme and chymotripsinogen detected by fluorescence polarization. Biochemistry 20:3955-3959.
    • (1981) Biochemistry , vol.20 , pp. 3955-3959
    • Chryssomallis, G.S.1    Torgerson, P.M.2    Drickamer, H.G.3    Weber, G.4
  • 9
    • 0028180075 scopus 로고
    • High-pressure effects on β-lactoglobulin interactions with ligands studied by fluorescence
    • Dufour E, Hoa GHB, Haertle T. 1994. High-pressure effects on β-lactoglobulin interactions with ligands studied by fluorescence. Biochim Biophys Acta 1206:166-172.
    • (1994) Biochim Biophys Acta , vol.1206 , pp. 166-172
    • Dufour, E.1    Hoa, G.H.B.2    Haertle, T.3
  • 10
    • 0030575785 scopus 로고    scopus 로고
    • Is apomyoglobin a molten globule? Structural characterization by NMR
    • Eliezer D, Wright PE. 1996. Is apomyoglobin a molten globule? Structural characterization by NMR. J Mol Biol 263:531-538.
    • (1996) J Mol Biol , vol.263 , pp. 531-538
    • Eliezer, D.1    Wright, P.E.2
  • 11
    • 0039377478 scopus 로고    scopus 로고
    • A formulation for the static permittivity of water and steam at temperatures from 238 K to 873 K at pressures up to 1200 MPa, including derivatives and Debye-Huckel coefficients
    • Fernandez DP, Goodwin ARH, Lemmon EW, Sengers JMHL, Williams RC. 1997. A formulation for the static permittivity of water and steam at temperatures from 238 K to 873 K at pressures up to 1200 MPa, including derivatives and Debye-Huckel coefficients. J Phys Chem Ref Data 26:1125-1166.
    • (1997) J Phys Chem Ref Data , vol.26 , pp. 1125-1166
    • Fernandez, D.P.1    Goodwin, A.R.H.2    Lemmon, E.W.3    Sengers, J.M.H.L.4    Williams, R.C.5
  • 13
    • 0028329347 scopus 로고
    • Thermodynamic puzzle of apomyoglobin unfolding
    • Griko YV, Privalov PL. 1994. Thermodynamic puzzle of apomyoglobin unfolding. J Mol Biol 235:1318-1325.
    • (1994) J Mol Biol , vol.235 , pp. 1318-1325
    • Griko, Y.V.1    Privalov, P.L.2
  • 14
    • 0028220701 scopus 로고
    • Proteins under pressure: The influence of high hydrostatic-pressure on structure, function and assembly of proteins and protein complexes
    • Gross M, Jaenicke R. 1994. Proteins under pressure: The influence of high hydrostatic-pressure on structure, function and assembly of proteins and protein complexes. Eur J Biochem 221:617-630.
    • (1994) Eur J Biochem , vol.221 , pp. 617-630
    • Gross, M.1    Jaenicke, R.2
  • 15
    • 0029011910 scopus 로고
    • Molecular-dynamics simulations of isolated helices of myoglobin
    • Hirst JD, Brooks CL. 1995. Molecular-dynamics simulations of isolated helices of myoglobin. Biochemistry 34:7614-7621.
    • (1995) Biochemistry , vol.34 , pp. 7614-7621
    • Hirst, J.D.1    Brooks, C.L.2
  • 16
    • 0025186451 scopus 로고
    • Structural characterization of a partly folded apomyoglobin intermediate
    • Hughson FM, Wright PE, Baldwin RL. 1990. Structural characterization of a partly folded apomyoglobin intermediate. Science 249:1544-1548.
    • (1990) Science , vol.249 , pp. 1544-1548
    • Hughson, F.M.1    Wright, P.E.2    Baldwin, R.L.3
  • 17
    • 0032539604 scopus 로고    scopus 로고
    • The pressure dependence of hydrophobic interactions is consistent with the observed pressure denaturation of proteins
    • Hummer G, Garde S, Garcia A, Paulaitis ME, Pratt LR. 1998. The pressure dependence of hydrophobic interactions is consistent with the observed pressure denaturation of proteins. Proc Natl Acad Sci USA 95:1552-1555.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 1552-1555
    • Hummer, G.1    Garde, S.2    Garcia, A.3    Paulaitis, M.E.4    Pratt, L.R.5
  • 18
    • 0028926875 scopus 로고
    • Computational approaches to study protein unfolding: Hen egg white lyzozyme as a case study
    • Hunenberger PE, Mark AE, van Gunsteren WF. 1995. Computational approaches to study protein unfolding: Hen egg white lyzozyme as a case study. Proteins 21:196-213.
    • (1995) Proteins , vol.21 , pp. 196-213
    • Hunenberger, P.E.1    Mark, A.E.2    Van Gunsteren, W.F.3
  • 19
    • 0026320508 scopus 로고
    • Protein stability and molecular adaptation to extreme conditions
    • Jaenicke R. 1991. Protein stability and molecular adaptation to extreme conditions. Eur J Biochem 202:715-728.
    • (1991) Eur J Biochem , vol.202 , pp. 715-728
    • Jaenicke, R.1
  • 20
    • 0027749370 scopus 로고
    • Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin
    • Jennings PA, Wright PE. 1993. Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin. Science 262:892-896.
    • (1993) Science , vol.262 , pp. 892-896
    • Jennings, P.A.1    Wright, P.E.2
  • 21
    • 0028226052 scopus 로고
    • High-pressure NMR-spectroscopy of proteins and membranes
    • Jonas J. Jonas A. 1994. High-pressure NMR-spectroscopy of proteins and membranes. Annu Rev Biophys Biomol Struct 23:287-318.
    • (1994) Annu Rev Biophys Biomol Struct , vol.23 , pp. 287-318
    • Jonas, J.1    Jonas, A.2
  • 22
    • 0028843842 scopus 로고
    • Alignment of 700 globin sequences: Extent of amino acid substitution and its correlation with variation in volume
    • Kapp OH. Moens L, Vanfleteren J, Trotman CNA, Suzuki T, Vinogradov SN. 1995. Alignment of 700 globin sequences: Extent of amino acid substitution and its correlation with variation in volume. Protein Sci 4:2179-2190.
    • (1995) Protein Sci , vol.4 , pp. 2179-2190
    • Kapp, O.H.1    Moens, L.2    Vanfleteren, J.3    Trotman, C.N.A.4    Suzuki, T.5    Vinogradov, S.N.6
  • 23
    • 36849150819 scopus 로고
    • Thermodynamics of unfolding
    • Kauzmann W. 1987. Thermodynamics of unfolding. Nature 325:763-764.
    • (1987) Nature , vol.325 , pp. 763-764
    • Kauzmann, W.1
  • 24
    • 0026785575 scopus 로고
    • Molecular dynamics simulation of solvated protein at high pressure
    • Kitchen DB, Reed LH, Levy RM. 1992. Molecular dynamics simulation of solvated protein at high pressure. Biochemistry 31:10083-10093.
    • (1992) Biochemistry , vol.31 , pp. 10083-10093
    • Kitchen, D.B.1    Reed, L.H.2    Levy, R.M.3
  • 25
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski RA, MacArthur MW, Moss DS, Thornton JM, 1993. PROCHECK: A program to check the stereochemical quality of protein structures. J Appl Cryst 26:283-291.
    • (1993) J Appl Cryst , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 26
    • 0017054059 scopus 로고
    • Plurality of pressure-denatured forms in chymotrypsinogen and lysozyme
    • Li T, Hook JW, Drickamer HG, Weber G. 1976. Plurality of pressure-denatured forms in chymotrypsinogen and lysozyme. Biochemistry 15:5571-5580.
    • (1976) Biochemistry , vol.15 , pp. 5571-5580
    • Li, T.1    Hook, J.W.2    Drickamer, H.G.3    Weber, G.4
  • 29
    • 9144240095 scopus 로고
    • DREIDING: A generic force field for molecular simulations
    • Mayo SL, Olafson BD, Goddard WA III. 1990. DREIDING: A generic force field for molecular simulations. J Phys Chem 94:8897-8909.
    • (1990) J Phys Chem , vol.94 , pp. 8897-8909
    • Mayo, S.L.1    Olafson, B.D.2    Goddard III, W.A.3
  • 30
    • 0000411306 scopus 로고    scopus 로고
    • Constant-pressure molecular dynamics techniques applied to complex molecular systems and solvated proteins
    • Paci E, Marchi M. 1996. Constant-pressure molecular dynamics techniques applied to complex molecular systems and solvated proteins. J Phys Chem 100:4314-4322.
    • (1996) J Phys Chem , vol.100 , pp. 4314-4322
    • Paci, E.1    Marchi, M.2
  • 31
    • 0031097214 scopus 로고    scopus 로고
    • Monte Carlo study of the effect of pressure on hydrophobic association
    • Payne VA, Matubayasi N, Murphy LR, Levy RM, 1997. Monte Carlo study of the effect of pressure on hydrophobic association. J Phys Chem B 101:2054-2060.
    • (1997) J Phys Chem B , vol.101 , pp. 2054-2060
    • Payne, V.A.1    Matubayasi, N.2    Murphy, L.R.3    Levy, R.M.4
  • 32
    • 0028058671 scopus 로고
    • High-pressure NMR study of the dissociation of ARC repressor
    • Peng XD, Jonas J, Silva JL. 1994. High-pressure NMR study of the dissociation of ARC repressor. Biochemistry 33:8223-8329.
    • (1994) Biochemistry , vol.33 , pp. 8223-8329
    • Peng, X.D.1    Jonas, J.2    Silva, J.L.3
  • 33
    • 33748481964 scopus 로고
    • Charge equilibration for molecular dynamics simulations
    • Rappé AK, Goddard WA III. 1991. Charge equilibration for molecular dynamics simulations. J Phys Chem 95:3358-3363.
    • (1991) J Phys Chem , vol.95 , pp. 3358-3363
    • Rappé, A.K.1    Goddard III, W.A.2
  • 35
    • 0028796090 scopus 로고
    • Raman-spectroscopic observation of a conformational change at the heme protein linkage in myoglobin at high-pressure
    • Schulte A, Buchter S, Galkin O, Williams C. 1995. Raman-spectroscopic observation of a conformational change at the heme protein linkage in myoglobin at high-pressure. J Am Chem Soc 117:10149-10150.
    • (1995) J Am Chem Soc , vol.117 , pp. 10149-10150
    • Schulte, A.1    Buchter, S.2    Galkin, O.3    Williams, C.4
  • 37
    • 0029869615 scopus 로고    scopus 로고
    • The use of hydrostatic pressure as a tool to study viruses an other macromolecular assemblages
    • Silva JL, Foguel D, Dapoian AT, Preverige PE. 1996. The use of hydrostatic pressure as a tool to study viruses an other macromolecular assemblages. Curr Opp Struct Biol 6:166-175.
    • (1996) Curr Opp Struct Biol , vol.6 , pp. 166-175
    • Silva, J.L.1    Foguel, D.2    Dapoian, A.T.3    Preverige, P.E.4
  • 38
    • 0023055734 scopus 로고
    • Pressure dissociation and conformational drift of the β dimer of tryptophan synthase
    • Silva JL, Miles EW. Weber G. 1986. Pressure dissociation and conformational drift of the β dimer of tryptophan synthase. Biochemistry 23:5780-5786.
    • (1986) Biochemistry , vol.23 , pp. 5780-5786
    • Silva, J.L.1    Miles, E.W.2    Weber, G.3
  • 39
    • 0027762355 scopus 로고
    • Pressure stability of proteins
    • Silva JL, Weber G. 1993. Pressure stability of proteins. Annu Rev Phys Chem 44:89-113.
    • (1993) Annu Rev Phys Chem , vol.44 , pp. 89-113
    • Silva, J.L.1    Weber, G.2
  • 40
    • 0029833446 scopus 로고    scopus 로고
    • Charge screening and the dielectric-constant of proteins: Insights from molecular-dynamics
    • Simonson T. Brooks CL. 1996. Charge screening and the dielectric-constant of proteins: Insights from molecular-dynamics. J Am Chem Soc 118:8452-8458.
    • (1996) J Am Chem Soc , vol.118 , pp. 8452-8458
    • Simonson, T.1    Brooks, C.L.2
  • 41
    • 33751158897 scopus 로고
    • Modeling solvent in biomolecular systems
    • Smith PE, Pettitt BM. 1994. Modeling solvent in biomolecular systems. J Phys Chem 95:9700-9711.
    • (1994) J Phys Chem , vol.95 , pp. 9700-9711
    • Smith, P.E.1    Pettitt, B.M.2
  • 42
    • 0026237127 scopus 로고
    • Unfolding of an alpha-helix in water
    • Soman KV, Karimi A, Case DA. 1991. Unfolding of an alpha-helix in water. Biopolymers 31:1351-1361.
    • (1991) Biopolymers , vol.31 , pp. 1351-1361
    • Soman, K.V.1    Karimi, A.2    Case, D.A.3
  • 43
    • 0017364269 scopus 로고
    • Structure of myoglobin refined at 2.0 Å resolution: Crystallographic refinement of metmyoglobin from sperm whale
    • Takano T. 1977. Structure of myoglobin refined at 2.0 Å resolution: Crystallographic refinement of metmyoglobin from sperm whale. J Mol Biol 110:537-568.
    • (1977) J Mol Biol , vol.110 , pp. 537-568
    • Takano, T.1
  • 44
    • 0023784241 scopus 로고
    • A structure of sperm whale myoglobin at nitrogen gas-pressure of 145 atmospheres
    • Tilton RF, Petsko GA. 1988. A structure of sperm whale myoglobin at nitrogen gas-pressure of 145 atmospheres. Biochemistry 27:6574-6582.
    • (1988) Biochemistry , vol.27 , pp. 6574-6582
    • Tilton, R.F.1    Petsko, G.A.2
  • 45
    • 0027316216 scopus 로고
    • Molecular dynamics simulations of unfolding of apomyoglobin in water
    • Tirado-Rives J, Jorgensen WL. 1993. Molecular dynamics simulations of unfolding of apomyoglobin in water. Biochemistry 32:4175-4184.
    • (1993) Biochemistry , vol.32 , pp. 4175-4184
    • Tirado-Rives, J.1    Jorgensen, W.L.2
  • 46
    • 0000109395 scopus 로고
    • Thermodynamics of the association and the pressure dissociation of oligomeric proteins
    • Weber G. 1993. Thermodynamics of the association and the pressure dissociation of oligomeric proteins. J Phys Chem 97:7108-7115.
    • (1993) J Phys Chem , vol.97 , pp. 7108-7115
    • Weber, G.1
  • 47
    • 0020712468 scopus 로고
    • The effect of high-pressure upon proteins and other biomolecules
    • Weber G, Drickamer HG. 1983. The effect of high-pressure upon proteins and other biomolecules. Q Rev Biophvs 16:89-112.
    • (1983) Q Rev Biophvs , vol.16 , pp. 89-112
    • Weber, G.1    Drickamer, H.G.2
  • 49
    • 0028829187 scopus 로고
    • Microbiology to 10,500 meters in the deep-sea
    • Yayanos AA. 1995. Microbiology to 10,500 meters in the deep-sea. Annu Rev Microbiol 49:777-805.
    • (1995) Annu Rev Microbiol , vol.49 , pp. 777-805
    • Yayanos, A.A.1
  • 50
    • 0015820466 scopus 로고
    • Pressure denaturation of metmyoglobin
    • Zipp A, Kauzmann W. 1973. Pressure denaturation of metmyoglobin. Biochemistry 12:4217-4227.
    • (1973) Biochemistry , vol.12 , pp. 4217-4227
    • Zipp, A.1    Kauzmann, W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.