메뉴 건너뛰기




Volumn 3, Issue 3, 1998, Pages 195-201

Chain-like conformation of heat-denatured ribonuclease A and cytochrome c as evidenced by solution X-ray scattering

Author keywords

Compact denatured state; Heat denaturation; Protein folding; Small angle X ray scattering

Indexed keywords

CYTOCHROME C; DISULFIDE; HEME; RIBONUCLEASE A;

EID: 0031779708     PISSN: 13590278     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1359-0278(98)00027-3     Document Type: Article
Times cited : (31)

References (40)
  • 1
    • 0025019350 scopus 로고
    • Conformational stability of globular proteins
    • Pace, C.N. (1990). Conformational stability of globular proteins. Trends Biochem. Sci. 15, 14-17.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 14-17
    • Pace, C.N.1
  • 2
    • 0028929556 scopus 로고
    • Principles of protein folding - A perspective from simple exact model
    • Dill, K.A., et al., & Chan, H.S. (1995). Principles of protein folding - a perspective from simple exact model. Protein Sei. 4, 561-602.
    • (1995) Protein Sei. , vol.4 , pp. 561-602
    • Dill, K.A.1    Chan, H.S.2
  • 3
    • 0027349239 scopus 로고
    • Hydration and heat stability effects on protein unfolding
    • Oobatake, M. & Ooi, T. (1993). Hydration and heat stability effects on protein unfolding. Prog. Biophys. Mol. Biol. 59, 237-284.
    • (1993) Prog. Biophys. Mol. Biol. , vol.59 , pp. 237-284
    • Oobatake, M.1    Ooi, T.2
  • 5
    • 0000697562 scopus 로고
    • Proteins as random coils. I. Intrinsic viscosities and sedimentation coefficients in concentrated guanidine hydrochloride
    • Tanford, C., Kawahara, K. & Lapanje, S. (1967). Proteins as random coils. I. Intrinsic viscosities and sedimentation coefficients in concentrated guanidine hydrochloride. J. Am. Chem. Soc. 89, 729-736.
    • (1967) J. Am. Chem. Soc. , vol.89 , pp. 729-736
    • Tanford, C.1    Kawahara, K.2    Lapanje, S.3
  • 6
    • 0014199111 scopus 로고
    • Evidence for residual structure in acid- And heat-denatured proteins
    • Aune, K.C., Salahuddin, A., Zarlengo, M.H. & Tanford, C. (1967). Evidence for residual structure in acid- and heat-denatured proteins. J. Biol. Chem. 242, 4486-4489.
    • (1967) J. Biol. Chem. , vol.242 , pp. 4486-4489
    • Aune, K.C.1    Salahuddin, A.2    Zarlengo, M.H.3    Tanford, C.4
  • 7
    • 0017042362 scopus 로고
    • Study of thermal denaturation of lysozyme and other globular proteins by light-scattering spectroscopy
    • Nicoli, D.F. & Benedek, G.B. (1976). Study of thermal denaturation of lysozyme and other globular proteins by light-scattering spectroscopy. B/opolymers 15, 2421-2437.
    • (1976) B/opolymers , vol.15 , pp. 2421-2437
    • Nicoli, D.F.1    Benedek, G.B.2
  • 8
    • 0019944760 scopus 로고
    • Secondary structure in ribonuclease: I. Equilibrium folding transitions seen by amide circular dichroism
    • Labhardt, A.M. (1982). Secondary structure in ribonuclease: I. Equilibrium folding transitions seen by amide circular dichroism. J. Mot. Biol. 157, 331-355.
    • (1982) J. Mot. Biol. , vol.157 , pp. 331-355
    • Labhardt, A.M.1
  • 9
    • 0025999787 scopus 로고
    • Hydrogen exchange in thermally denatured ribonuclease A
    • Robertson, A.D. & Baldwin, R.L (1991). Hydrogen exchange in thermally denatured ribonuclease A. Biochemistry 30, 9907-9914.
    • (1991) Biochemistry , vol.30 , pp. 9907-9914
    • Robertson, A.D.1    Baldwin, R.L.2
  • 10
    • 0026733250 scopus 로고
    • Denatured states of ribonuclease A have compact dimensions and residual secondary structure
    • Sosnick, T.R. & Trewhella, J. (1992). Denatured states of ribonuclease A have compact dimensions and residual secondary structure. Biochemistry 31, 8329-8355.
    • (1992) Biochemistry , vol.31 , pp. 8329-8355
    • Sosnick, T.R.1    Trewhella, J.2
  • 11
    • 0028349385 scopus 로고
    • Thermally denatured ribonuclease A retains secondary structure as shown by FTIR
    • Seshadri, S., Oberg, K.A. & Fink, A.L. (1994). Thermally denatured ribonuclease A retains secondary structure as shown by FTIR. Biochemistry 33, 1351-1355.
    • (1994) Biochemistry , vol.33 , pp. 1351-1355
    • Seshadri, S.1    Oberg, K.A.2    Fink, A.L.3
  • 12
    • 0028925816 scopus 로고
    • Compactness of thermally and chemically denatured ribonuclease A as revealed by volume and compressibility
    • Tamura, Y. & Gekko, K. (1995). Compactness of thermally and chemically denatured ribonuclease A as revealed by volume and compressibility. Biochemistry 34, 1878-1884.
    • (1995) Biochemistry , vol.34 , pp. 1878-1884
    • Tamura, Y.1    Gekko, K.2
  • 13
    • 0027394285 scopus 로고
    • Pulsed H/D-exchange studies of folding intermediates
    • Baldwin, R.L. (1993). Pulsed H/D-exchange studies of folding intermediates. Curr. Opin. Struct. Biol. 3, 84-91.
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 84-91
    • Baldwin, R.L.1
  • 14
    • 0027955639 scopus 로고
    • Small angle X-ray scattering studies of protein folding
    • Lattman, E.E. (1994). Small angle X-ray scattering studies of protein folding. Curr. Opin. Struct. Biol. 4, 87-92.
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 87-92
    • Lattman, E.E.1
  • 15
    • 0030324821 scopus 로고    scopus 로고
    • X-ray solution scattering studies of protein folding
    • Kataoka, M. & Goto, Y. (1996). X-ray solution scattering studies of protein folding. Fold Des. 1, R107-R114.
    • (1996) Fold Des. , vol.1
    • Kataoka, M.1    Goto, Y.2
  • 16
    • 0017701604 scopus 로고
    • Automatic identification of secondary structure in globular proteins
    • Levitt, M. & Greer, J. (1977). Automatic identification of secondary structure in globular proteins. J. Mol. Biol. 114, 181-239.
    • (1977) J. Mol. Biol. , vol.114 , pp. 181-239
    • Levitt, M.1    Greer, J.2
  • 17
    • 0019888571 scopus 로고
    • Conformation change of cytochrome c. II. Ferricytochrome c refinement at 1.8 Å and comparison with the ferrocytochrome structure
    • Takano, T. & Dickerson, R.E. (1981). Conformation change of cytochrome c. II. Ferricytochrome c refinement at 1.8 Å and comparison with the ferrocytochrome structure. J. Mol. Biol. 153, 95-115.
    • (1981) J. Mol. Biol. , vol.153 , pp. 95-115
    • Takano, T.1    Dickerson, R.E.2
  • 18
    • 0027400842 scopus 로고
    • Molten globule of cytochrome c studied by small angle X-ray scattering
    • Kataoka, M., Hagihara, Y., Mihara, K. & Goto, Y. (1993). Molten globule of cytochrome c studied by small angle X-ray scattering. J. Mol. Biol. 229, 591-596.
    • (1993) J. Mol. Biol. , vol.229 , pp. 591-596
    • Kataoka, M.1    Hagihara, Y.2    Mihara, K.3    Goto, Y.4
  • 19
    • 0029040449 scopus 로고
    • Thermodynamic stability of the molten globule states of apomyoglobin
    • Nishii, 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
    • Nishii, I.1    Kataoka, M.2    Goto, Y.3
  • 20
    • 0029032691 scopus 로고
    • Structural characterization of molten globule and native states of apomyoglobin by solution X-ray scattering
    • Kataoka, M., et al., & Goto, Y. (1995). Structural characterization of molten globule and native states 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    Goto, Y.2
  • 21
    • 0031050429 scopus 로고    scopus 로고
    • Structural characterization of the molten globule of α-lactalbumin by solution X-ray scattering
    • Kataoka, M., Kuwajima, K., Tokunaga, F. & Goto, Y. (1997). Structural characterization of the molten globule of α-lactalbumin by solution X-ray scattering. Protein Sci. 6, 422-430.
    • (1997) Protein Sci. , vol.6 , pp. 422-430
    • Kataoka, M.1    Kuwajima, K.2    Tokunaga, F.3    Goto, Y.4
  • 22
    • 0027184188 scopus 로고
    • Cold denaturation-induced conformational changes in phosphoglycerate kinase from yeast
    • Damaschun, G., et al., & Zirwer, D. (1993). Cold denaturation-induced conformational changes in phosphoglycerate kinase from yeast. Biochemistry 32, 7739-7746.
    • (1993) Biochemistry , vol.32 , pp. 7739-7746
    • Damaschun, G.1    Zirwer, D.2
  • 23
    • 0030572626 scopus 로고    scopus 로고
    • A lysozyme folding intermediate revealed by solution X-ray scattering
    • Chen, L., Hodgson, K.O. & Doniach, S..(1996). A lysozyme folding intermediate revealed by solution X-ray scattering. J. Mol. Biol. 261, 658-671.
    • (1996) J. Mol. Biol. , vol.261 , pp. 658-671
    • Chen, L.1    Hodgson, K.O.2    Doniach, S.3
  • 24
    • 0025299563 scopus 로고
    • Influence of the solvent on the conformational-dependent properties of random-coil polypeptides. I. the mean-square of the end-to-end distance and of the dipole moment
    • Rowe, G. & Pineiro, A.L. (1990). Influence of the solvent on the conformational-dependent properties of random-coil polypeptides. I. The mean-square of the end-to-end distance and of the dipole moment. Biophys. Chem. 36, 57-64.
    • (1990) Biophys. Chem. , vol.36 , pp. 57-64
    • Rowe, G.1    Pineiro, A.L.2
  • 25
    • 0028978422 scopus 로고
    • Trifluoroethanol-induced stabilization of the α-helical structure of β-lactoglobulin: Implication for non-hierarchical protein folding
    • Shiraki, K., Nishikawa, K. & Goto, Y. (1995). Trifluoroethanol-induced stabilization of the α-helical structure of β-lactoglobulin: implication for non-hierarchical protein folding. J. Mol. Biol. 245, 180-184.
    • (1995) J. Mol. Biol. , vol.245 , pp. 180-184
    • Shiraki, K.1    Nishikawa, K.2    Goto, Y.3
  • 26
    • 0029893286 scopus 로고    scopus 로고
    • The methanol-induced globular and expanded denatured states of cytochrome c: A study by CD, fluorescence, NMR and small angle X-ray scattering
    • Kamatari, Y.O., Konno, T., Kataoka, M. & Akasaka, K. (1996). The methanol-induced globular and expanded denatured states of cytochrome c: a study by CD, fluorescence, NMR and small angle X-ray scattering. J. Mol. Biol. 259, 512-523.
    • (1996) J. Mol. Biol. , vol.259 , pp. 512-523
    • Kamatari, Y.O.1    Konno, T.2    Kataoka, M.3    Akasaka, K.4
  • 27
    • 0029967685 scopus 로고    scopus 로고
    • 15N NMR relaxation measurements of hen egg white lysozyme denatured in trifluoroethanol
    • 15N NMR relaxation measurements of hen egg white lysozyme denatured in trifluoroethanol. J. Mol. Biol. 257, 669-683.
    • (1996) J. Mol. Biol. , vol.257 , pp. 669-683
    • Buck, M.1    Schwalbe, H.2    Dobson, C.M.3
  • 28
    • 0030828611 scopus 로고    scopus 로고
    • Trifluoroethanol-induced conformational transition of hen eggwhite lysozyme studied by small-angle X-ray scattering
    • Hoshino, M., Hagihara, Y., Hamada, D., Kataoka, M. & Goto, Y. (1997). Trifluoroethanol-induced conformational transition of hen eggwhite lysozyme studied by small-angle X-ray scattering. FEBS Lett. 416, 72-76.
    • (1997) FEBS Lett. , vol.416 , pp. 72-76
    • Hoshino, M.1    Hagihara, Y.2    Hamada, D.3    Kataoka, M.4    Goto, Y.5
  • 29
    • 33845555570 scopus 로고
    • Titration of individual components in a mixture with resolution of difference spectra, pKs and redox transitions
    • Shrager, R.I. & Hendler, R.W. (1982). Titration of individual components in a mixture with resolution of difference spectra, pKs and redox transitions. Anal. Chem. 54, 1147-1152.
    • (1982) Anal. Chem. , vol.54 , pp. 1147-1152
    • Shrager, R.I.1    Hendler, R.W.2
  • 30
    • 0030320442 scopus 로고    scopus 로고
    • The concept of a random coil. Residual structure in peptides and denatured proteins
    • Smith, L.J., Fiebig, K.M., Schwalbe, H. & Dobson, C.M. (1996). The concept of a random coil. Residual structure in peptides and denatured proteins. Fold. Des. 1, R95-R106.
    • (1996) Fold. Des. , vol.1
    • Smith, L.J.1    Fiebig, K.M.2    Schwalbe, H.3    Dobson, C.M.4
  • 31
    • 0029978353 scopus 로고    scopus 로고
    • Analysis of main chain torsion angles in proteins. Prediction of NMR coupling constants for native and denatured conformations
    • Smith, L.J., et al., & Dobson, C.M. (1996). Analysis of main chain torsion angles in proteins. Prediction of NMR coupling constants for native and denatured conformations. J. Mol. Biol. 255, 494-506.
    • (1996) J. Mol. Biol. , vol.255 , pp. 494-506
    • Smith, L.J.1    Dobson, C.M.2
  • 32
    • 0000749460 scopus 로고    scopus 로고
    • Towards a description of the conformation of denatured states of proteins. Comparison of a random coil model with NMR measurements
    • Fiebig, K.M., Schwalbe, H., Buck, M., Smith, L.J. & Dobson, C.M. (1996). Towards a description of the conformation of denatured states of proteins. Comparison of a random coil model with NMR measurements. J. Phys. Chem. 100, 2661-2666.
    • (1996) J. Phys. Chem. , vol.100 , pp. 2661-2666
    • Fiebig, K.M.1    Schwalbe, H.2    Buck, M.3    Smith, L.J.4    Dobson, C.M.5
  • 33
    • 0029961647 scopus 로고    scopus 로고
    • Structural analysis of non-native states of proteins by NMR
    • Shortle, D.R. (1996). Structural analysis of non-native states of proteins by NMR. Curr. Opin. Struct. Biol. 6, 24-30.
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 24-30
    • Shortle, D.R.1
  • 34
    • 0030032461 scopus 로고    scopus 로고
    • The denatured state (the other half of the folding equation) and its role in protein stability
    • Shortle, D.R. (1996). The denatured state (the other half of the folding equation) and its role in protein stability. FASEB J. 10, 27-34.
    • (1996) FASEB J. , vol.10 , pp. 27-34
    • Shortle, D.R.1
  • 35
    • 0006555359 scopus 로고
    • Structural studies of ribonuclease. XI. Kinetics of denaturation
    • Scott, R.A. & Scheraga, H.A. (1963). Structural studies of ribonuclease. XI. Kinetics of denaturation. J. Am. Chem. Soc. 85, 3866-3873.
    • (1963) J. Am. Chem. Soc. , vol.85 , pp. 3866-3873
    • Scott, R.A.1    Scheraga, H.A.2
  • 36
    • 0015526732 scopus 로고
    • Participation of the protein ligands in the folding of cytochrome c
    • Babul, J. & Stellwagen, E. (1972). Participation of the protein ligands in the folding of cytochrome c. Biochemistry 11, 1195-1200.
    • (1972) Biochemistry , vol.11 , pp. 1195-1200
    • Babul, J.1    Stellwagen, E.2
  • 37
    • 0022160183 scopus 로고
    • Aggregation of bovine serum albumin upon cleavage of its disulfide bonds, studied by the time-resolved small-angle X-ray scattering technique with synchrotron radiation
    • Ueki, T., er al., & Muroga, Y. (1985). Aggregation of bovine serum albumin upon cleavage of its disulfide bonds, studied by the time-resolved small-angle X-ray scattering technique with synchrotron radiation. Biophys. Chem. 23, 115-124.
    • (1985) Biophys. Chem. , vol.23 , pp. 115-124
    • Ueki, T.1    Muroga, Y.2
  • 39
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 40
    • 0028057108 scopus 로고
    • Raster3D version 2.0. A program for photorealistic molecular graphics
    • Merritt, E.A. & Murphy, M.E.P. (1994). Raster3D version 2.0. A program for photorealistic molecular graphics. Acta Crystallogr. D 50, 869-873.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.