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Volumn 243, Issue 1-2, 1997, Pages 292-298

1H-NMR study of inter-segmental hydrogen bonds in sperm whale and horse apomyoglobins

Author keywords

Apomyoglobin; Internal hydrogen bond; Myoglobin; NMR; Protein folding

Indexed keywords

MYOGLOBIN; APOMYOGLOBIN; APOPROTEIN; ASPARTIC ACID; GUANIDINE; GUANIDINE DERIVATIVE; HEME; HISTIDINE;

EID: 0030614440     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.0292a.x     Document Type: Article
Times cited : (10)

References (42)
  • 2
    • 0000686117 scopus 로고
    • Relative conformations of sperm whale metniyoglobin and apomyoglobin in solution
    • Breslow, E., Sherman, B., Hardman, K. D. & Gurd, F. R. N. (1965) Relative conformations of sperm whale metniyoglobin and apomyoglobin in solution, J. Biol. Chem. 240, 304-309.
    • (1965) J. Biol. Chem. , vol.240 , pp. 304-309
    • Breslow, E.1    Sherman, B.2    Hardman, K.D.3    Gurd, F.R.N.4
  • 3
    • 0000707259 scopus 로고
    • Reversible conformational changes of myoglobin and apomyoglobin
    • Harrison, S. C. & Blout, E. R. (1965) Reversible conformational changes of myoglobin and apomyoglobin, J. Biol. Chem. 240, 299-303.
    • (1965) J. Biol. Chem. , vol.240 , pp. 299-303
    • Harrison, S.C.1    Blout, E.R.2
  • 5
    • 0017364269 scopus 로고
    • Structure of myoglobin refined at 2.0 Å resolution. I. Crystallographic refinement of metmyoglobin from sperm whale
    • Takano, T. (1977) Structure of myoglobin refined at 2.0 Å resolution. I. 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
  • 6
    • 0025882875 scopus 로고
    • Neutron diffraction study of carbonmonoxymyoglobin
    • Cheng, X. & Schoenborn, B. P. (1991) Neutron diffraction study of carbonmonoxymyoglobin, J. Mol. Biol. 220, 381-399.
    • (1991) J. Mol. Biol. , vol.220 , pp. 381-399
    • Cheng, X.1    Schoenborn, B.P.2
  • 7
    • 0023910427 scopus 로고
    • Horse heart metmyoglobin. A 2.8 Å resolution three-dimensional structure determinalion
    • Evans, S. V. & Brayer, G. D. (1988) Horse heart metmyoglobin. A 2.8 Å resolution three-dimensional structure determinalion, J. Biol. Chem. 263, 4263-4268.
    • (1988) J. Biol. Chem. , vol.263 , pp. 4263-4268
    • Evans, S.V.1    Brayer, G.D.2
  • 8
    • 0025296867 scopus 로고
    • High-resolution study of the three-dimensional structure of horse heart metmyoglobin
    • Evans, S. V. & Brayer, G. D. (1990) High-resolution study of the three-dimensional structure of horse heart metmyoglobin, J. Mol. Biol. 213, 885-897.
    • (1990) J. Mol. Biol. , vol.213 , pp. 885-897
    • Evans, S.V.1    Brayer, G.D.2
  • 9
    • 0024338305 scopus 로고
    • Use of site-directed mutagenesis to destabilize native apomyoglobin relative to folding intermediates
    • Hughson, F. M. & Baldwin, R. L. (1989) Use of site-directed mutagenesis to destabilize native apomyoglobin relative to folding intermediates, Biochemistry 28, 4415-4422.
    • (1989) Biochemistry , vol.28 , pp. 4415-4422
    • Hughson, F.M.1    Baldwin, R.L.2
  • 10
    • 0025186451 scopus 로고
    • Structural characterization of a partly folded apomyoglobin intermediate
    • Hughson, F. M., Wright, P. E. & Baldwin, R. L. (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
  • 11
    • 0027749370 scopus 로고
    • Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin
    • Jennings, P. A. & Wright, P. E. (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
  • 12
    • 0027245421 scopus 로고
    • Three-state analysis of sperm whale apomyoglobin folding
    • Barrick, D. & Baldwin, R. L. (1993) Three-state analysis of sperm whale apomyoglobin folding, Biochemistry 32, 3790-3796.
    • (1993) Biochemistry , vol.32 , pp. 3790-3796
    • Barrick, D.1    Baldwin, R.L.2
  • 14
    • 0028061408 scopus 로고
    • Compactness of protein molten globules: Temperature-induced structural changes of the apomyoglobin folding intermediate
    • Gast, K., Damaschum, H., Misselwitz, R., Müller-Forhne, M., Zirwer, D. & Damaschum, G. (1994) Compactness of protein molten globules: temperature-induced structural changes of the apomyoglobin folding intermediate, Eur. Biophys. J. 23, 297-305.
    • (1994) Eur. Biophys. J. , vol.23 , pp. 297-305
    • Gast, K.1    Damaschum, H.2    Misselwitz, R.3    Müller-Forhne, M.4    Zirwer, D.5    Damaschum, G.6
  • 15
    • 0028329347 scopus 로고
    • Thermodynamic puzzle of apomyoglobin unfolding
    • Griko, Y. V. & Privalov, P. L. (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
  • 16
    • 0028235775 scopus 로고
    • Molecular mechanism of acid denaturation. The role of histidine residues in the partial unfolding of apomyoglobin
    • Barrick, D., Hughson, F. M. & Baldwin, R. L. (1994) Molecular mechanism of acid denaturation. The role of histidine residues in the partial unfolding of apomyoglobin, J. Mol. Biol. 237, 588-601.
    • (1994) J. Mol. Biol. , vol.237 , pp. 588-601
    • Barrick, D.1    Hughson, F.M.2    Baldwin, R.L.3
  • 17
    • 0029040449 scopus 로고
    • Thermodynamic stability of the molten globule states of apomyoglobin
    • Nishi, I., Kataoka, M. & Goto, Y. (1995) Thermodynamic stability of the molten globule states of apomyoglobin, J. Mol. Biol. 250, 223-238.
    • (1995) J. Mol. Biol. , vol.250 , pp. 223-238
    • Nishi, I.1    Kataoka, M.2    Goto, Y.3
  • 18
    • 0029112554 scopus 로고
    • Intrinsic stability of individual α helices modulates structure and stability of the apomyoglobin molten globule form
    • Kiefhaber, T. & Baldwin, R. L. (1995) Intrinsic stability of individual α helices modulates structure and stability of the apomyoglobin molten globule form, J. Mol. Biol. 252, 122-132.
    • (1995) J. Mol. Biol. , vol.252 , pp. 122-132
    • Kiefhaber, T.1    Baldwin, R.L.2
  • 19
    • 0029014386 scopus 로고
    • Structure and stability of a second molten globule intermediate in the apomyoglobin folding pathway
    • Loh, S. N., Kay, M. S. & Baldwin, R. L. (1995) Structure and stability of a second molten globule intermediate in the apomyoglobin folding pathway, Proc. Natl Acad. Sci. USA 92, 5446-5450.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 5446-5450
    • Loh, S.N.1    Kay, M.S.2    Baldwin, R.L.3
  • 20
    • 0029032691 scopus 로고
    • Structural characterization of the molten globule and native slates of apomyoglobin by solution X-ray scattering
    • Kataoka, M., Nishi, I., Fujisawa, T., Ueki, T., Tokunaga, F. & Goto, Y. (1995) Structural characterization of the molten globule and native slates of apomyoglobin by solution X-ray scattering, J. Mol. Biol. 249, 215-228.
    • (1995) J. Mol. Biol. , vol.249 , pp. 215-228
    • Kataoka, M.1    Nishi, I.2    Fujisawa, T.3    Ueki, T.4    Tokunaga, F.5    Goto, Y.6
  • 21
    • 0029918121 scopus 로고    scopus 로고
    • Time-resolved fluorescence studies of the molten globule state of apomyoglobin
    • Rischel, C., Thyberg, P., Rigler, R. & Poulsen, F. M. (1996) Time-resolved fluorescence studies of the molten globule state of apomyoglobin, J. Mol. Biol. 257, 877-885.
    • (1996) J. Mol. Biol. , vol.257 , pp. 877-885
    • Rischel, C.1    Thyberg, P.2    Rigler, R.3    Poulsen, F.M.4
  • 22
    • 0030010408 scopus 로고    scopus 로고
    • Intermediate states in protein folding
    • Privalov, P. L. (1996) Intermediate states in protein folding, J. Mol. Biol. 258, 707-725.
    • (1996) J. Mol. Biol. , vol.258 , pp. 707-725
    • Privalov, P.L.1
  • 23
    • 0016670614 scopus 로고
    • Conformation of apomyoglobin in aqueous solutions and denaturing organic solvents
    • Herskovits, T. T. & Solli, N. J. (1975) Conformation of apomyoglobin in aqueous solutions and denaturing organic solvents, Biopolymers 14, 319-334.
    • (1975) Biopolymers , vol.14 , pp. 319-334
    • Herskovits, T.T.1    Solli, N.J.2
  • 24
    • 0014961149 scopus 로고
    • Fluorescence studies of Aplysia and sperm whale apomyoglobins
    • Anderson, S. R., Brunori, M. & Weber, G. (1970) Fluorescence studies of Aplysia and sperm whale apomyoglobins, Biochemistry 9, 4723-4729.
    • (1970) Biochemistry , vol.9 , pp. 4723-4729
    • Anderson, S.R.1    Brunori, M.2    Weber, G.3
  • 25
    • 0026643349 scopus 로고
    • Structural comparison of apomyoglobin and metaquomyoglobin: PH titration of histidines by NMR spectroscopy
    • Cocco, M. J., Kao, Y.-H., Phillips, A. T. & Lecomte, J. T. J. (1992) Structural comparison of apomyoglobin and metaquomyoglobin: pH titration of histidines by NMR spectroscopy, Biochemistry 31, 6481-6491.
    • (1992) Biochemistry , vol.31 , pp. 6481-6491
    • Cocco, M.J.1    Kao, Y.-H.2    Phillips, A.T.3    Lecomte, J.T.J.4
  • 26
    • 0025616115 scopus 로고
    • Characterization of hydrophobic cores in apomyoglobin: A proton NMR spectroscopy study
    • Cocco, M. J. & Lecomte, J. T. J. (1990) Characterization of hydrophobic cores in apomyoglobin: A proton NMR spectroscopy study, Biochemistry 29, 11 067-11 072.
    • (1990) Biochemistry , vol.29 , pp. 11067-11072
    • Cocco, M.J.1    Lecomte, J.T.J.2
  • 27
    • 0030179636 scopus 로고    scopus 로고
    • 1H NMR probes for inter-segmental hydrogen bonds in myoglobins
    • 1H NMR probes for inter-segmental hydrogen bonds in myoglobins, J. Biochem. (Tokyo) 120, 126-132.
    • (1996) J. Biochem. (Tokyo) , vol.120 , pp. 126-132
    • Yamamoto, Y.1
  • 28
    • 49749199032 scopus 로고
    • Cleavage of the haem-protein link by acid methyl ethyl ketone
    • 27a. Teale, F. W. J. (1959) Cleavage of the haem-protein link by acid methyl ethyl ketone, Biochim. Biophys. Acta 35, 543.
    • (1959) Biochim. Biophys. Acta , vol.35 , pp. 543
    • Teale, F.W.J.1
  • 30
    • 0028299603 scopus 로고
    • The native state of apomyoglobin described by proton NMR spectroscopy: Interaction with the paramagnetic probe HyTEMPO and the fluorescence dye ANS
    • Cocco, M. J. & Lecomte, J. T. J. (1994) The native state of apomyoglobin described by proton NMR spectroscopy: interaction with the paramagnetic probe HyTEMPO and the fluorescence dye ANS, Protein Sci. 3, 267-281.
    • (1994) Protein Sci. , vol.3 , pp. 267-281
    • Cocco, M.J.1    Lecomte, J.T.J.2
  • 32
    • 0027219184 scopus 로고
    • Electrostatic calculations of side-chain pKa values in myoglobin and comparison with NMR data for histidines
    • Bashford, D., Case, D. A., Dalvit, C., Tennant, L. & Wright, P. E. (1993) Electrostatic calculations of side-chain pKa values in myoglobin and comparison with NMR data for histidines, Biochemistry 32, 8045-8056.
    • (1993) Biochemistry , vol.32 , pp. 8045-8056
    • Bashford, D.1    Case, D.A.2    Dalvit, C.3    Tennant, L.4    Wright, P.E.5
  • 33
    • 0020493395 scopus 로고
    • Hydrogen exchange and the dynamic structure of protein
    • Woodward, C., Simon, E. & Tuchsen, E. (1982) Hydrogen exchange and the dynamic structure of protein, Mol. Cell. Biochem. 48, 135-160.
    • (1982) Mol. Cell. Biochem. , vol.48 , pp. 135-160
    • Woodward, C.1    Simon, E.2    Tuchsen, E.3
  • 35
    • 0018368695 scopus 로고
    • Hydrogen exchange kinetics and internal motions in proteins and nucleic acids
    • Woodward, C. K. & Hilton, B. D. (1979) Hydrogen exchange kinetics and internal motions in proteins and nucleic acids, Annu. Rev. Biophys. Bioeng. 8, 99-127.
    • (1979) Annu. Rev. Biophys. Bioeng. , vol.8 , pp. 99-127
    • Woodward, C.K.1    Hilton, B.D.2
  • 36
    • 0023660124 scopus 로고
    • 1H nuclear magnetic resonance spectrum of the carbon monoxide complex of sperm whale myoglobin by phase-sensitive two-dimensional techniques
    • 1H nuclear magnetic resonance spectrum of the carbon monoxide complex of sperm whale myoglobin by phase-sensitive two-dimensional techniques, J. Mol. Biol. 194, 313-327.
    • (1987) J. Mol. Biol. , vol.194 , pp. 313-327
    • Dalvit, C.1    Wright, P.E.2
  • 37
    • 0014413956 scopus 로고
    • Spectral studies on the denaturation of myoglobin
    • Schechter, A. N. & Epstein, C. J. (1968) Spectral studies on the denaturation of myoglobin, J. Mol. Biol. 35, 567-589.
    • (1968) J. Mol. Biol. , vol.35 , pp. 567-589
    • Schechter, A.N.1    Epstein, C.J.2
  • 38
    • 0015882223 scopus 로고
    • The equilibrium unfolding parameters of horse and sperm whale myoglobin
    • Puett, D. (1973) The equilibrium unfolding parameters of horse and sperm whale myoglobin, J. Biol. Chem. 248, 4623-4634.
    • (1973) J. Biol. Chem. , vol.248 , pp. 4623-4634
    • Puett, D.1
  • 39
    • 0015743399 scopus 로고
    • A comparison of the conformation: Stabilities of homologous hemoproteins. Myoglobin from several species, human hemoglobin and subunits
    • Puett, D., Friebele, E. & Hammonds, R. G. Jr (1973) A comparison of the conformation: stabilities of homologous hemoproteins. Myoglobin from several species, human hemoglobin and subunits, J. Mol. Biol. 328, 261-277.
    • (1973) J. Mol. Biol. , vol.328 , pp. 261-277
    • Puett, D.1    Friebele, E.2    Hammonds Jr., R.G.3
  • 40
    • 0018798895 scopus 로고
    • Determining globular protein stability: Guanidine hydrochloride denaturation of myoglobin
    • Pace, C. N. & Vanderburg, K. E. (1979) Determining globular protein stability: guanidine hydrochloride denaturation of myoglobin, Biochemistry 18, 288-291.
    • (1979) Biochemistry , vol.18 , pp. 288-291
    • Pace, C.N.1    Vanderburg, K.E.2
  • 41
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace, C. N. (1986) Determination and analysis of urea and guanidine hydrochloride denaturation curves, Methods Enzymol. 131, 266-289.
    • (1986) Methods Enzymol. , vol.131 , pp. 266-289
    • Pace, C.N.1
  • 42
    • 0027323022 scopus 로고
    • Guanidine hydrochloride-induced folding of proteins
    • Hagihara, Y., Amino, S., Fink, A. L. & Goto, Y. (1993) Guanidine hydrochloride-induced folding of proteins, J. Mol. Biol. 231, 180-184.
    • (1993) J. Mol. Biol. , vol.231 , pp. 180-184
    • Hagihara, Y.1    Amino, S.2    Fink, A.L.3    Goto, Y.4


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