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Volumn 1702, Issue 2, 2004, Pages 129-136

Effect of hydrostatic pressure on conformational changes of canine milk lysozyme between the native, molten globule, and unfolded states

Author keywords

Canine milk lysozyme; Folding; Hydration; Hydrostatic pressure; Molten globule; Volume change

Indexed keywords

LACTALBUMIN; LYSOZYME; WATER;

EID: 5444259968     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2004.06.012     Document Type: Article
Times cited : (6)

References (56)
  • 1
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chain
    • C.B. Anfinsen Principles that govern the folding of protein chain Science 181 1973 223 230
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 3
    • 0036782097 scopus 로고    scopus 로고
    • Effects of a helix stabilization on the folding mechanism of alpha-lactalbumin
    • M. Mizuguchi, Y. Kobashigawa, Y. Kumaki, M. Demura, K. Kawano, and K. Nitta Effects of a helix stabilization on the folding mechanism of alpha-lactalbumin Proteins 49 2002 95 103
    • (2002) Proteins , vol.49 , pp. 95-103
    • Mizuguchi, M.1    Kobashigawa, Y.2    Kumaki, Y.3    Demura, M.4    Kawano, K.5    Nitta, K.6
  • 4
    • 0029011017 scopus 로고
    • Volumetric characterizations of the native, molten globule and unfolded states of cytochrome c at acidic pH
    • T.V. Chalikian, V.S. Gindikin, and K.J. Breslauer Volumetric characterizations of the native, molten globule and unfolded states of cytochrome c at acidic pH J. Mol. Biol. 250 1995 291 306
    • (1995) J. Mol. Biol. , vol.250 , pp. 291-306
    • Chalikian, T.V.1    Gindikin, V.S.2    Breslauer, K.J.3
  • 5
    • 0343247668 scopus 로고    scopus 로고
    • The native and the heat induced denatured states of α- Chymotrypsinogen A: Thermodynamic and spectroscopic studies
    • T.V. Chalikian, J. Völker, D. Anafi, and K.J. Breslauer The native and the heat induced denatured states of α-Chymotrypsinogen A: thermodynamic and spectroscopic studies J. Mol. Biol. 274 1997 237 252
    • (1997) J. Mol. Biol. , vol.274 , pp. 237-252
    • Chalikian, T.V.1    Völker, J.2    Anafi, D.3    Breslauer, K.J.4
  • 6
    • 0029070645 scopus 로고
    • Volume changes of the molten globule transitions of horse heart ferricytochrome c: A thermodynamic cycle
    • K. Foygel, S. Spector, S. Chatterjee, and P.C. Kahn Volume changes of the molten globule transitions of horse heart ferricytochrome c: a thermodynamic cycle Protein Sci. 4 1995 1426 1429
    • (1995) Protein Sci. , vol.4 , pp. 1426-1429
    • Foygel, K.1    Spector, S.2    Chatterjee, S.3    Kahn, P.C.4
  • 7
    • 0030010408 scopus 로고    scopus 로고
    • Intermediate states in protein folding
    • P.L. Privalov Intermediate states in protein folding J. Mol. Biol. 258 1996 707 725
    • (1996) J. Mol. Biol. , vol.258 , pp. 707-725
    • Privalov, P.L.1
  • 9
    • 0035711472 scopus 로고    scopus 로고
    • Energetics of three-state unfolding of a protein: Canine milk lysozyme
    • T. Koshiba, Y. Kobashigawa, M. Demura, and K. Nitta Energetics of three-state unfolding of a protein: canine milk lysozyme Protein Eng. 14 2001 967 974
    • (2001) Protein Eng. , vol.14 , pp. 967-974
    • Koshiba, T.1    Kobashigawa, Y.2    Demura, M.3    Nitta, K.4
  • 10
    • 0002940127 scopus 로고
    • The molten globule statue
    • T.E. Creighton Freeman New York
    • O.B. Ptitsyn The molten globule statue T.E. Creighton Protein Folding 1992 Freeman New York 243 300
    • (1992) Protein Folding , pp. 243-300
    • Ptitsyn, O.B.1
  • 11
    • 0023041667 scopus 로고
    • Evidence for identity between the equilibrium unfolding intermediate and a transient folding intermediate: A comparative study of the folding reactions of α-lactalbumin and lysozyme
    • M. Ikeguchi, K. Kuwajima, M. Mitani, and S. Sugai Evidence for identity between the equilibrium unfolding intermediate and a transient folding intermediate: a comparative study of the folding reactions of α-lactalbumin and lysozyme Biochemistry 25 1986 6965 6972
    • (1986) Biochemistry , vol.25 , pp. 6965-6972
    • Ikeguchi, M.1    Kuwajima, K.2    Mitani, M.3    Sugai, S.4
  • 12
    • 0027749370 scopus 로고
    • Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin
    • P.A. Jennings, and P.A. Wright Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin Science 262 1993 892 896
    • (1993) Science , vol.262 , pp. 892-896
    • Jennings, P.A.1    Wright, P.A.2
  • 13
    • 0024417964 scopus 로고
    • The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure
    • K. Kuwajima The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure Proteins 6 1989 87 103
    • (1989) Proteins , vol.6 , pp. 87-103
    • Kuwajima, K.1
  • 14
    • 0030059690 scopus 로고    scopus 로고
    • The molten globule state of α-lactalbumin
    • K. Kuwajima The molten globule state of α-lactalbumin FASEB J. 10 1996 102 109
    • (1996) FASEB J. , vol.10 , pp. 102-109
    • Kuwajima, K.1
  • 16
  • 17
    • 0024362936 scopus 로고
    • The evolution of lysozyme and α-lactalbumin
    • K. Nitta, and S. Sugai The evolution of lysozyme and α-lactalbumin Eur. J. Biochem. 182 1989 111 118
    • (1989) Eur. J. Biochem. , vol.182 , pp. 111-118
    • Nitta, K.1    Sugai, S.2
  • 18
    • 0036357509 scopus 로고    scopus 로고
    • α-Lactalbumin and (calcium-binding) lysozyme
    • K. Nitta α-Lactalbumin and (calcium-binding) lysozyme Methods Mol. Biol. 172 2002 211 224
    • (2002) Methods Mol. Biol. , vol.172 , pp. 211-224
    • Nitta, K.1
  • 19
    • 0022559769 scopus 로고
    • 2+ binding on the structure and stability of bovine α-lactalbumin studied by circular dichroism and nuclear magnetic resonance spectra
    • 2+ binding on the structure and stability of bovine α-lactalbumin studied by circular dichroism and nuclear magnetic resonance spectra Int. J. Pept. Protein Res. 27 1986 18 27
    • (1986) Int. J. Pept. Protein Res. , vol.27 , pp. 18-27
    • Kuwajima, K.1    Harushima, Y.2    Sugai, S.3
  • 20
    • 0033588264 scopus 로고    scopus 로고
    • The volume and compression changes of lysozyme associated with guanidinium chloride and pressure-assisted unfolding
    • K. Sasahara, M. Sakurai, and K. Nitta The volume and compression changes of lysozyme associated with guanidinium chloride and pressure-assisted unfolding J. Mol. Biol. 291 1999 693 701
    • (1999) J. Mol. Biol. , vol.291 , pp. 693-701
    • Sasahara, K.1    Sakurai, M.2    Nitta, K.3
  • 21
    • 0027509031 scopus 로고
    • Comparative study of the stability of the folding intermediates of the calcium-binding lysozymes
    • K. Nitta, H. Tsuge, and H. Iwamoto Comparative study of the stability of the folding intermediates of the calcium-binding lysozymes Int. J. Pept. Protein Res. 41 1993 118 123
    • (1993) Int. J. Pept. Protein Res. , vol.41 , pp. 118-123
    • Nitta, K.1    Tsuge, H.2    Iwamoto, H.3
  • 22
    • 0031789584 scopus 로고    scopus 로고
    • Calcium-binding and structural stability of echidna and canine milk lysozymes
    • M. Kikuchi, K. Kawano, and K. Nitta Calcium-binding and structural stability of echidna and canine milk lysozymes Protein Sci. 7 1998 2150 2155
    • (1998) Protein Sci. , vol.7 , pp. 2150-2155
    • Kikuchi, M.1    Kawano, K.2    Nitta, K.3
  • 23
    • 0033536627 scopus 로고    scopus 로고
    • The molten globule state of a chimera of human α-lactalbumin and equine lysozyme
    • M. Mizuguchi, K. Masaki, and K. Nitta The molten globule state of a chimera of human α-lactalbumin and equine lysozyme J. Mol. Biol. 292 1999 1137 1148
    • (1999) J. Mol. Biol. , vol.292 , pp. 1137-1148
    • Mizuguchi, M.1    Masaki, K.2    Nitta, K.3
  • 24
    • 0034283781 scopus 로고    scopus 로고
    • Hydrogen exchange study of canine milk lysozyme: Stabilization mechanism of the molten globule
    • Y. Kobashigawa, M. Demura, T. Koshiba, Y. Kumaki, K. Kuwajima, and K. Nitta Hydrogen exchange study of canine milk lysozyme: stabilization mechanism of the molten globule Proteins 40 2000 579 589
    • (2000) Proteins , vol.40 , pp. 579-589
    • Kobashigawa, Y.1    Demura, M.2    Koshiba, T.3    Kumaki, Y.4    Kuwajima, K.5    Nitta, K.6
  • 25
    • 0026679847 scopus 로고
    • Absence of the thermal transition in apo-α-lactalbumin in the molten globule state: A study differential scanning microcalorimetry
    • K. Yutani, K. Ogasawara, and K. Kuwajima Absence of the thermal transition in apo-α-lactalbumin in the molten globule state: a study differential scanning microcalorimetry J. Mol. Biol. 228 1992 347 350
    • (1992) J. Mol. Biol. , vol.228 , pp. 347-350
    • Yutani, K.1    Ogasawara, K.2    Kuwajima, K.3
  • 27
    • 0033060057 scopus 로고    scopus 로고
    • Expression of a synthetic gene encoding canine milk lysozyme in Escherichia coli and characterization of the expressed protein
    • T. Koshiba, T. Hayashi, M. Ishido, I. Kumagai, and K. Nitta Expression of a synthetic gene encoding canine milk lysozyme in Escherichia coli and characterization of the expressed protein Protein Eng. 12 1999 429 435
    • (1999) Protein Eng. , vol.12 , pp. 429-435
    • Koshiba, T.1    Hayashi, T.2    Ishido, M.3    Kumagai, I.4    Nitta, K.5
  • 28
    • 0015784343 scopus 로고
    • Equilibrium and kinetics of the unfolding of α-lactalbumin by guanidine hydrochloride
    • S. Sugai, H. Yashiro, and K. Nitta Equilibrium and kinetics of the unfolding of α-lactalbumin by guanidine hydrochloride Biochim. Biophys. Acta 328 1973 35 41
    • (1973) Biochim. Biophys. Acta , vol.328 , pp. 35-41
    • Sugai, S.1    Yashiro, H.2    Nitta, K.3
  • 29
    • 0017596565 scopus 로고
    • Equilibrium and kinetics of the unfolding of α-lactalbumin by guanidine hydrochloride (IV): Dependence of the N-A transition on temperature
    • K. Nitta, N. Kita, K. Kuwajima, and S. Sugai Equilibrium and kinetics of the unfolding of α-lactalbumin by guanidine hydrochloride (IV): dependence of the N-A transition on temperature Biochim. Biophys. Acta 490 1977 200 208
    • (1977) Biochim. Biophys. Acta , vol.490 , pp. 200-208
    • Nitta, K.1    Kita, N.2    Kuwajima, K.3    Sugai, S.4
  • 30
    • 0021430496 scopus 로고
    • Thermodynamics of thermal unfolding of bovine apo-α-lactalbumin
    • Y. Hiraoka, and S. Sugai Thermodynamics of thermal unfolding of bovine apo-α-lactalbumin Int. J. Pept. Protein Res. 23 1984 535 542
    • (1984) Int. J. Pept. Protein Res. , vol.23 , pp. 535-542
    • Hiraoka, Y.1    Sugai, S.2
  • 31
    • 0014952474 scopus 로고
    • Thermodynamics of protein denaturation. Effect of pressure on the denaturation of ribonuclease a
    • J.F. Brants, R.J. Oliveria, and C. Westort Thermodynamics of protein denaturation. Effect of pressure on the denaturation of ribonuclease A Biochemistry 9 1970 1038 1047
    • (1970) Biochemistry , vol.9 , pp. 1038-1047
    • Brants, J.F.1    Oliveria, R.J.2    Westort, C.3
  • 32
    • 0015236387 scopus 로고
    • Reversible pressure and temperature denaturation of chymotrypsinogen
    • S.A. Hawley Reversible pressure and temperature denaturation of chymotrypsinogen Biochemistry 10 1971 2436 2442
    • (1971) Biochemistry , vol.10 , pp. 2436-2442
    • Hawley, S.A.1
  • 33
    • 0015820466 scopus 로고
    • Pressure denaturation of metmyoglobin
    • A. Zipp, and W. Kauzmann Pressure denaturation of metmyoglobin Biochemistry 12 1973 4217 4228
    • (1973) Biochemistry , vol.12 , pp. 4217-4228
    • Zipp, A.1    Kauzmann, W.2
  • 34
    • 0033405499 scopus 로고    scopus 로고
    • Effect of hydrostatic pressure on unfolding of α-lactalbumin: Volumetric equivalence of the molten globule and unfolded state
    • Y. Kobashigawa, M. Sakurai, and K. Nitta Effect of hydrostatic pressure on unfolding of α-lactalbumin: volumetric equivalence of the molten globule and unfolded state Protein Sci. 8 1999 2765 2772
    • (1999) Protein Sci. , vol.8 , pp. 2765-2772
    • Kobashigawa, Y.1    Sakurai, M.2    Nitta, K.3
  • 35
    • 0015438810 scopus 로고
    • The preparation of guanidine hydrochloride
    • Y. Nozaki The preparation of guanidine hydrochloride Methods Enzymol. 26 1972 43 50
    • (1972) Methods Enzymol. , vol.26 , pp. 43-50
    • Nozaki, Y.1
  • 37
    • 0037216486 scopus 로고    scopus 로고
    • Pressure-induced unfolding of the molten globule state of all-Ala α-lactalbumin
    • M.W. Lassalle, H. Li, H. Yamada, K. Akasaka, and C. Redfield Pressure-induced unfolding of the molten globule state of all-Ala α-lactalbumin Protein Sci. 12 2003 66 72
    • (2003) Protein Sci. , vol.12 , pp. 66-72
    • Lassalle, M.W.1    Li, H.2    Yamada, H.3    Akasaka, K.4    Redfield, C.5
  • 38
    • 0344406172 scopus 로고    scopus 로고
    • Pressure-dependent changes in the solution structure of hen egg-white lysozyme
    • M. Rafaee, T. Tezuka, K. Akasaka, and M.P. Williamson Pressure-dependent changes in the solution structure of hen egg-white lysozyme J. Mol. Biol. 327 2003 857 865
    • (2003) J. Mol. Biol. , vol.327 , pp. 857-865
    • Rafaee, M.1    Tezuka, T.2    Akasaka, K.3    Williamson, M.P.4
  • 39
    • 0033580649 scopus 로고    scopus 로고
    • Differences between the pressure- and temperature-induced denaturation and aggregation of β-lactoglobulin A, B, and AB monitored by FT-IR spectroscopy and small-angle X-ray scattering
    • G. Panick, R. Malessa, and R. Winter Differences between the pressure- and temperature-induced denaturation and aggregation of β-lactoglobulin A, B, and AB monitored by FT-IR spectroscopy and small-angle X-ray scattering Biochemistry 38 1999 6512 6519
    • (1999) Biochemistry , vol.38 , pp. 6512-6519
    • Panick, G.1    Malessa, R.2    Winter, R.3
  • 40
    • 0037335714 scopus 로고    scopus 로고
    • Pressure and temperature-induced unfolding and aggregation of recombinant human interferon-c: A Fourier transform infrared spectroscopy study
    • K. Goosens, J. Haelewyn, F. Meersman, M.D. Ley, and K. Heremans Pressure and temperature-induced unfolding and aggregation of recombinant human interferon-c: a Fourier transform infrared spectroscopy study Biochem. J. 370 2003 529 535
    • (2003) Biochem. J. , vol.370 , pp. 529-535
    • Goosens, K.1    Haelewyn, J.2    Meersman, F.3    Ley, M.D.4    Heremans, K.5
  • 41
    • 0037219961 scopus 로고    scopus 로고
    • Fluorescence and FTIR study of pressure-induced structural modifications of horse liver alcohol dehydrogenase (HLADH)
    • M. Trovaslet, S. Dallet-Choisy, F. Meersman, K. Heremans, C. Balny, and M.D. Legoy Fluorescence and FTIR study of pressure-induced structural modifications of horse liver alcohol dehydrogenase (HLADH) Eur. J. Biochem. 270 2003 119 128
    • (2003) Eur. J. Biochem. , vol.270 , pp. 119-128
    • Trovaslet, M.1    Dallet-Choisy, S.2    Meersman, F.3    Heremans, K.4    Balny, C.5    Legoy, M.D.6
  • 42
    • 1642409882 scopus 로고    scopus 로고
    • Effects of chaotropic and kosmotropic cosolvents on the pressure-induced unfolding and denaturation of proteins: An FT-IR study on staphylococcal nuclease
    • H. Herberhold, C.A. Royer, and R. Winter Effects of chaotropic and kosmotropic cosolvents on the pressure-induced unfolding and denaturation of proteins: an FT-IR study on staphylococcal nuclease Biochemistry 43 2004 3336 3345
    • (2004) Biochemistry , vol.43 , pp. 3336-3345
    • Herberhold, H.1    Royer, C.A.2    Winter, R.3
  • 43
    • 0038071510 scopus 로고    scopus 로고
    • The thermodynamic analysis of protein stabilization by sucrose and glycerol against pressure-induced unfolding
    • K. Ruan, C. Xu, T. Li, J. Li, R. Lange, and C. Balny The thermodynamic analysis of protein stabilization by sucrose and glycerol against pressure-induced unfolding Eur. J. Biochem. 270 2003 1654 1661
    • (2003) Eur. J. Biochem. , vol.270 , pp. 1654-1661
    • Ruan, K.1    Xu, C.2    Li, T.3    Li, J.4    Lange, R.5    Balny, C.6
  • 44
    • 0030298077 scopus 로고    scopus 로고
    • On volume changes accompanying conformational transitions of biopolymers
    • T.V. Chalikian, and K.J. Breslauer On volume changes accompanying conformational transitions of biopolymers Biopolymers 39 1996 619 626
    • (1996) Biopolymers , vol.39 , pp. 619-626
    • Chalikian, T.V.1    Breslauer, K.J.2
  • 45
    • 0031790423 scopus 로고    scopus 로고
    • Thermodynamic analysis of biomolecules: A volumetric approach
    • T.V. Chalikian, and K.J. Breslauer Thermodynamic analysis of biomolecules: a volumetric approach Curr. Opin. Struck. Biol. 8 1998 657 664
    • (1998) Curr. Opin. Struck. Biol. , vol.8 , pp. 657-664
    • Chalikian, T.V.1    Breslauer, K.J.2
  • 46
    • 0031789585 scopus 로고    scopus 로고
    • Probing the contribution of internal cavities to the volume change of protein unfolding under pressure
    • K.J. Frye, and C.A. Royer Probing the contribution of internal cavities to the volume change of protein unfolding under pressure Protein Sci. 7 1998 2217 2222
    • (1998) Protein Sci. , vol.7 , pp. 2217-2222
    • Frye, K.J.1    Royer, C.A.2
  • 47
    • 0031554921 scopus 로고    scopus 로고
    • Pressure-induced changes in the folded structure of lysozyme
    • K. Akasaka, T. Tezuka, and H. Yamada Pressure-induced changes in the folded structure of lysozyme J. Mol. Biol. 271 1997 671 678
    • (1997) J. Mol. Biol. , vol.271 , pp. 671-678
    • Akasaka, K.1    Tezuka, T.2    Yamada, H.3
  • 48
    • 0035882536 scopus 로고    scopus 로고
    • Pressure effect on denaturant-induced unfolding of hen egg white lysozyme
    • K. Sasahara, M. Sakurai, and K. Nitta Pressure effect on denaturant-induced unfolding of hen egg white lysozyme Proteins 44 2001 180 187
    • (2001) Proteins , vol.44 , pp. 180-187
    • Sasahara, K.1    Sakurai, M.2    Nitta, K.3
  • 50
    • 0029143128 scopus 로고
    • Thermodynamics of unfolding of ribonuclease a under high pressure. A study by proton NMR
    • T. Yamaguchi, H. Yamada, and K. Akasaka Thermodynamics of unfolding of ribonuclease A under high pressure. A study by proton NMR J. Mol. Biol. 250 1995 689 694
    • (1995) J. Mol. Biol. , vol.250 , pp. 689-694
    • Yamaguchi, T.1    Yamada, H.2    Akasaka, K.3
  • 51
    • 0041846677 scopus 로고    scopus 로고
    • Volume and compressibility changes accompanying thermally-induced native-to-unfolded and molten globule-to-unfolded transitions of cytochrome c: A high pressure study
    • D.N. Dublins, R. Filfil, R.B. Macregor Jr., and T.V. Chalikian Volume and compressibility changes accompanying thermally-induced native-to-unfolded and molten globule-to-unfolded transitions of cytochrome c: a high pressure study Biochemistry 42 2003 8671 8678
    • (2003) Biochemistry , vol.42 , pp. 8671-8678
    • Dublins, D.N.1    Filfil, R.2    Macregor Jr., R.B.3    Chalikian, T.V.4
  • 52
    • 0031837399 scopus 로고    scopus 로고
    • Determination of the volume changes for pressure-induced transitions of apomyoglobin between the native, molten globule, and unfolded states
    • G.J.A. Vidugiris, and C.A. Royer Determination of the volume changes for pressure-induced transitions of apomyoglobin between the native, molten globule, and unfolded states Biophys. J. 75 1998 463 470
    • (1998) Biophys. J. , vol.75 , pp. 463-470
    • Vidugiris, G.J.A.1    Royer, C.A.2
  • 53
    • 0037171140 scopus 로고    scopus 로고
    • Revisiting volume changes in pressure-induced protein unfolding
    • C.A. Royer Revisiting volume changes in pressure-induced protein unfolding Biochim. Biophys. Acta 1595 2002 201 209
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 201-209
    • Royer, C.A.1
  • 54
    • 0022999267 scopus 로고
    • Compressibility-structure relationship of globular proteins
    • K. Gekko, and Y. Hasegawa Compressibility-structure relationship of globular proteins Biochemistry 25 1986 6563 6571
    • (1986) Biochemistry , vol.25 , pp. 6563-6571
    • Gekko, K.1    Hasegawa, Y.2
  • 55
    • 0029765444 scopus 로고    scopus 로고
    • Proline scanning mutagenesis of a molten globule reveals non-cooperative formation of a protein's overall topology
    • B.A. Schulman, and P.S. Kim Proline scanning mutagenesis of a molten globule reveals non-cooperative formation of a protein's overall topology Nat. Struct. Biol. 3 1996 682 687
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 682-687
    • Schulman, B.A.1    Kim, P.S.2
  • 56
    • 0029737544 scopus 로고    scopus 로고
    • Testing the correlation between delta a and delta V of protein unfolding using m value mutants of staphylococcal nuclease
    • K.J. Frye, C.S. Perman, and C.A. Royer Testing the correlation between delta A and delta V of protein unfolding using m value mutants of staphylococcal nuclease Biochemistry 35 1996 10234 10239
    • (1996) Biochemistry , vol.35 , pp. 10234-10239
    • Frye, K.J.1    Perman, C.S.2    Royer, C.A.3


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