메뉴 건너뛰기




Volumn 37, Issue 21, 1998, Pages 7859-7868

Alternative models for describing the acid unfolding of the apomyoglobin folding intermediate

Author keywords

[No Author keywords available]

Indexed keywords

APOMYOGLOBIN; MYOGLOBIN; UNCLASSIFIED DRUG;

EID: 0032568639     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9802061     Document Type: Article
Times cited : (38)

References (48)
  • 2
    • 0026253816 scopus 로고
    • The three states of globular proteins: Acid denaturation
    • Alonso, D. O., Dill, K. A., and Stigter, D. (1991) The three states of globular proteins: acid denaturation, Biopolymers 31, 1631-49.
    • (1991) Biopolymers , vol.31 , pp. 1631-1649
    • Alonso, D.O.1    Dill, K.A.2    Stigter, D.3
  • 3
    • 0027245421 scopus 로고
    • Three-state analysis of sperm whale apomyoglobin folding
    • Barrick, D., and Baldwin, R. L. (1993) Three-state analysis of sperm whale apomyoglobin folding, Biochemistry 32, 3790-6.
    • (1993) Biochemistry , vol.32 , pp. 3790-3796
    • Barrick, D.1    Baldwin, R.L.2
  • 4
    • 0027254057 scopus 로고
    • The molten globule intermediate of apomyoglobin and the process of protein folding
    • Barrick, D., and Baldwin, R. L. (1993) The molten globule intermediate of apomyoglobin and the process of protein folding, Protein Sci. 2, 869-76.
    • (1993) Protein Sci. , vol.2 , pp. 869-876
    • Barrick, D.1    Baldwin, R.L.2
  • 5
    • 0028235775 scopus 로고
    • Molecular mechanisms of acid denaturation. The role of histidine residues in the partial unfolding of apomyoglobin
    • Barrick D., Hughson, F. M., and Baldwin, R. L. (1994) Molecular mechanisms 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
  • 6
    • 0025186451 scopus 로고
    • Structural characterization of a partly folded apomyoglobin intermediate
    • Hughson, F. M., Wright, P. E., and Baldwin, R. L. (1990) Structural characterization of a partly folded apomyoglobin intermediate, Science 249, 1544-8.
    • (1990) Science , vol.249 , pp. 1544-1548
    • Hughson, F.M.1    Wright, P.E.2    Baldwin, R.L.3
  • 7
    • 0025891257 scopus 로고
    • Probing the stability of a partly folded apomyoglobin intermediate by site-directed mutagenesis
    • Hughson F. M., Barrick, D., and Baldwin, R. L. (1991) Probing the stability of a partly folded apomyoglobin intermediate by site-directed mutagenesis, Biochemistry 30, 4113-8.
    • (1991) Biochemistry , vol.30 , pp. 4113-4118
    • Hughson, F.M.1    Barrick, D.2    Baldwin, R.L.3
  • 8
    • 0027749370 scopus 로고
    • Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin
    • Jennings, P. A., and Wright, P. E. (1993) Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin, Science 262, 892-6.
    • (1993) Science , vol.262 , pp. 892-896
    • Jennings, P.A.1    Wright, P.E.2
  • 9
    • 0029032691 scopus 로고
    • Structural characterization of the molten globule and native states of apomyoglobin by solution X-ray scattering
    • Kataoka, M., et al. (1995) Structural characterization of the molten globule and native states of apomyoglobin by solution X-ray scattering, J. Mol. Biol. 249, 215-28.
    • (1995) J. Mol. Biol. , vol.249 , pp. 215-228
    • Kataoka, M.1
  • 10
    • 0028884580 scopus 로고
    • The radius of gyration of an apomyoglobin folding intermediate
    • Eliezer, D., et al. (1995) The radius of gyration of an apomyoglobin folding intermediate, Science 270, 487-8.
    • (1995) Science , vol.270 , pp. 487-488
    • Eliezer, D.1
  • 11
    • 0029904282 scopus 로고    scopus 로고
    • Refolding and unfolding kinetics of the equilibrium folding intermediate of apomyoglobin
    • Jamin, M., and Baldwin, R. L. (1996) Refolding and unfolding kinetics of the equilibrium folding intermediate of apomyoglobin, Nat. Struct. Biol. 3, 613-8.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 613-618
    • Jamin, M.1    Baldwin, R.L.2
  • 12
    • 0031932824 scopus 로고    scopus 로고
    • Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding
    • Eliezer, D., Yao, J., Dyson, H. J., and Wright, P. E. (1998) Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding, Nat. Struct. Biol. 5, 148-55.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 148-155
    • Eliezer, D.1    Yao, J.2    Dyson, H.J.3    Wright, P.E.4
  • 13
    • 0029014386 scopus 로고
    • Structure and stability of a second molten globule intermediate in the apomyoglobin folding pathway
    • Loh, S. N., Kay, M. S., and Baldwin, R. L. (1995) Structure and stability of a second molten globule intermediate in the apomyoglobin folding pathway, Proc. Natl. Acad. Sci. U.S.A. 92, 5446-50.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 5446-5450
    • Loh, S.N.1    Kay, M.S.2    Baldwin, R.L.3
  • 14
    • 0029112554 scopus 로고
    • Intrinsic stability of individual alpha helices modulates structure and stability of the apomyoglobin molten globule form
    • Kiefhaber, T., and Baldwin, R. L. (1995) Intrinsic stability of individual alpha helices modulates structure and stability of the apomyoglobin molten globule form, J. Mol. Biol. 252, 122-32.
    • (1995) J. Mol. Biol. , vol.252 , pp. 122-132
    • Kiefhaber, T.1    Baldwin, R.L.2
  • 15
    • 0027165688 scopus 로고
    • Peptide models of protein folding initiation sites. 1. Secondary structure formation by peptides corresponding to the G- and H-helices of myoglobin
    • Waltho, J. P., Feher, V. A., Merutka, G., Dyson, H. J., and Wright, P. E. (1993) Peptide models of protein folding initiation sites. 1. Secondary structure formation by peptides corresponding to the G- and H-helices of myoglobin, Biochemistry 32, 6337-47.
    • (1993) Biochemistry , vol.32 , pp. 6337-6347
    • Waltho, J.P.1    Feher, V.A.2    Merutka, G.3    Dyson, H.J.4    Wright, P.E.5
  • 16
    • 0029981924 scopus 로고    scopus 로고
    • Packing interactions in the apomyglobin folding intermediate
    • Kay, M. S., and Baldwin, R. L. (1996) Packing interactions in the apomyglobin folding intermediate, Nat. Struct. Biol. 3, 439-45.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 439-445
    • Kay, M.S.1    Baldwin, R.L.2
  • 17
    • 78651189765 scopus 로고
    • On the Nature of Allosteric Transitions: A Plausible Model
    • Monod, J., Wyman, J., and Changeux, J. P. (1965) On the Nature of Allosteric Transitions: A Plausible Model, J. Mol. Biol. 12, 88-118.
    • (1965) J. Mol. Biol. , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.P.3
  • 18
    • 0025855421 scopus 로고
    • Spectroscopic studies of myoglobin at low pH: Heme structure and ligation
    • Sage, J. T., Morikis, D., and Champion, P. M. (1991) Spectroscopic studies of myoglobin at low pH: heme structure and ligation, Biochemistry 30, 1227-37.
    • (1991) Biochemistry , vol.30 , pp. 1227-1237
    • Sage, J.T.1    Morikis, D.2    Champion, P.M.3
  • 19
    • 0024334934 scopus 로고
    • Resonance Raman investigations of site-directed mutants of myoglobin: Effects of distal histidine replacement
    • Morikis, D., Champion, P. M., Springer, B. A., and Sligar, S. G. (1989) Resonance Raman investigations of site-directed mutants of myoglobin: effects of distal histidine replacement, Biochemistry 28, 4791-800.
    • (1989) Biochemistry , vol.28 , pp. 4791-4800
    • Morikis, D.1    Champion, P.M.2    Springer, B.A.3    Sligar, S.G.4
  • 21
    • 77956727554 scopus 로고
    • The Interpretation of Hydrogen Ion Titration Curves of Proteins
    • Tanford C. (1962) The Interpretation of Hydrogen Ion Titration Curves of Proteins, Adv. Protein Chem. 17, 69-165.
    • (1962) Adv. Protein Chem. , vol.17 , pp. 69-165
    • Tanford, C.1
  • 22
    • 0026351184 scopus 로고
    • Role of electrostatic repulsion in the acidic molten globule of cytochrome c
    • Goto Y., and Nishikiori, S. (1991) Role of electrostatic repulsion in the acidic molten globule of cytochrome c, J. Mol. Biol. 222, 679-86.
    • (1991) J. Mol. Biol. , vol.222 , pp. 679-686
    • Goto, Y.1    Nishikiori, S.2
  • 23
    • 0028346251 scopus 로고
    • Comparison of the conformational stability of the molten globule and native states of horse cytochrome c. Effects of acetylation, heat, urea and guanidine hydrochloride
    • Hagihara, Y., Tan, Y., and Goto, Y. (1994) Comparison of the conformational stability of the molten globule and native states of horse cytochrome c. Effects of acetylation, heat, urea and guanidine hydrochloride, J. Mol. Biol. 237, 336-48.
    • (1994) J. Mol. Biol. , vol.237 , pp. 336-348
    • Hagihara, Y.1    Tan, Y.2    Goto, Y.3
  • 24
    • 33947469236 scopus 로고
    • Hydrogen Ion Equilibria of Bovine Serum Albumin
    • Tanford C, Swanson, S. A., and Shore, W. S. (1955) Hydrogen Ion Equilibria of Bovine Serum Albumin, J. Am. Chem. Soc. 77, 6414-21.
    • (1955) J. Am. Chem. Soc. , vol.77 , pp. 6414-6421
    • Tanford, C.1    Swanson, S.A.2    Shore, W.S.3
  • 25
    • 0032549072 scopus 로고    scopus 로고
    • Two Forms of the pH 4 Folding Intermediate of Apomyoglobm
    • Jamin, M., and Baldwin, R. (1998) Two Forms of the pH 4 Folding Intermediate of Apomyoglobm, J. Mol. Biol. 276, 491-504.
    • (1998) J. Mol. Biol. , vol.276 , pp. 491-504
    • Jamin, M.1    Baldwin, R.2
  • 26
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl a-chymotrypsm using different denaturants
    • Santoro, M. M., and Bolen, D. W. (1988) Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl a-chymotrypsm using different denaturants, Biochemistry 27, 8063-8.
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2
  • 27
    • 0029040449 scopus 로고
    • Thermodynamic stability of the molten globule states of apomyoglobm
    • Nishii, I., Kataoka, M., and Goto, Y. (1995) Thermodynamic stability of the molten globule states of apomyoglobm, J. Mol. Biol. 250, 223-38.
    • (1995) J. Mol. Biol. , vol.250 , pp. 223-238
    • Nishii, I.1    Kataoka, M.2    Goto, Y.3
  • 28
    • 0030947929 scopus 로고    scopus 로고
    • Folding propensities of peptide fragments ot myoglobin
    • Reymond, M. T., Merutka, G., Dyson, H. J., and Wright, P. E. (1997) Folding propensities of peptide fragments ot myoglobin, Protein Sci. 6, 706-16.
    • (1997) Protein Sci. , vol.6 , pp. 706-716
    • Reymond, M.T.1    Merutka, G.2    Dyson, H.J.3    Wright, P.E.4
  • 29
    • 0014217191 scopus 로고
    • Intrinsic dissociation constant of aspartyl and glutamyl carboxyl groups
    • Nozaki, Y., and Tanford, C. (1967) Intrinsic dissociation constant of aspartyl and glutamyl carboxyl groups, J. Biol. Chem. 242, 4731-5.
    • (1967) J. Biol. Chem. , vol.242 , pp. 4731-4735
    • Nozaki, Y.1    Tanford, C.2
  • 30
    • 0015247070 scopus 로고
    • Hydrogen ion titration curve of lysozyme in 6 M guanidine hydrochloride
    • Roxby, R., and Tanford, C. (1971) Hydrogen ion titration curve of lysozyme in 6 M guanidine hydrochloride, Biochemistry 10, 3348-52.
    • (1971) Biochemistry , vol.10 , pp. 3348-3352
    • Roxby, R.1    Tanford, C.2
  • 31
    • 0028983182 scopus 로고
    • A values of the denatured state are on average 0.4 unit lower than those of model compounds
    • A values of the denatured state are on average 0.4 unit lower than those of model compounds, Biochemistry 34, 9424-33.
    • (1995) Biochemistry , vol.34 , pp. 9424-9433
    • Oliveberg, M.1    Arcus, V.L.2    Fersht, A.R.3
  • 32
    • 0023462496 scopus 로고
    • High-level expression of sperm whale myoglobin in Escherichia coli
    • Springer, B. A., and Sligar, S. G. (1987) High-level expression of sperm whale myoglobin in Escherichia coli, Proc. Natl. Acad. Sci. U.S.A. 84, 8961-5.
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 8961-8965
    • Springer, B.A.1    Sligar, S.G.2
  • 33
    • 0014109212 scopus 로고
    • Spectroscopic determination of tryptophan and tyrosine in proteins
    • Edelhoch, H. (1967) Spectroscopic determination of tryptophan and tyrosine in proteins, Biochemistry 6, 1948-54.
    • (1967) Biochemistry , vol.6 , pp. 1948-1954
    • Edelhoch, H.1
  • 34
    • 0030694241 scopus 로고    scopus 로고
    • Cooperativity of folding of the apomyoglobin pH 4 intermediate studied by glycine and proline mutations
    • Luo, Y., Kay M. S., and Baldwin, R. L. (1997) Cooperativity of folding of the apomyoglobin pH 4 intermediate studied by glycine and proline mutations, Nat. Struct. Biol. 4, 925-30.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 925-930
    • Luo, Y.1    Kay, M.S.2    Baldwin, R.L.3
  • 35
    • 0026553768 scopus 로고
    • The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability
    • Serrano, L., Kellis, J. T., Jr., Cann, P., Matouschek A., and Fersht, A. R. (1992) The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability, J. Mol. Biol. 224, 783-804.
    • (1992) J. Mol. Biol. , vol.224 , pp. 783-804
    • Serrano, L.1    Kellis J.T., Jr.2    Cann, P.3    Matouschek, A.4    Fersht, A.R.5
  • 36
    • 0022401765 scopus 로고
    • Electrostatic interactions in sperm whale myoglobin. Site specificity, roles in structural elements, and external electrostatic potential distributions
    • Garcia-Moreno, B., Chen, L. X., March, K. L., Gurd, R. S., and Gurd, F. R. (1985) Electrostatic interactions in sperm whale myoglobin. Site specificity, roles in structural elements, and external electrostatic potential distributions, J. Biol. Chem. 260, 14070-82.
    • (1985) J. Biol. Chem. , vol.260 , pp. 14070-14082
    • Garcia-Moreno, B.1    Chen, L.X.2    March, K.L.3    Gurd, R.S.4    Gurd, F.R.5
  • 37
    • 0018793926 scopus 로고
    • Electrostatic stabilization in myoglobin. Interactive free energies between individual sites
    • Friend, S. H., and Gurd, F. R. (1979) Electrostatic stabilization in myoglobin. Interactive free energies between individual sites, Biochemistry 18, 4620-30.
    • (1979) Biochemistry , vol.18 , pp. 4620-4630
    • Friend, S.H.1    Gurd, F.R.2
  • 38
    • 0028361968 scopus 로고
    • Structural origins of pH and ionic strength effects on protein stability. Acid denaturation of sperm whale apomyoglobin
    • Yang, A. S., and Honig, B. (1994) Structural origins of pH and ionic strength effects on protein stability. Acid denaturation of sperm whale apomyoglobin, J. Mol. Biol. 237, 602-14.
    • (1994) J. Mol. Biol. , vol.237 , pp. 602-614
    • Yang, A.S.1    Honig, B.2
  • 39
    • 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., and Lecomte, J. T. (1992) Structural comparison of apomyoglobin and metaquomyoglobin: pH titration of histidines by NMR spectroscopy, Biochemistry 31, 6481-91.
    • (1992) Biochemistry , vol.31 , pp. 6481-6491
    • Cocco, M.J.1    Kao, Y.H.2    Phillips, A.T.3    Lecomte, J.T.4
  • 40
    • 0025195499 scopus 로고
    • Mechanism of acid-induced folding of proteins
    • Goto, Y., Takahashi, N., and Fink, A. L. (1990) Mechanism of acid-induced folding of proteins. Biochemistry 29, 3480-8.
    • (1990) Biochemistry , vol.29 , pp. 3480-3488
    • Goto, Y.1    Takahashi, N.2    Fink, A.L.3
  • 41
    • 0020492960 scopus 로고
    • Anion binding and pH-dependent electrostatic effects in ribonuclease
    • Matthew, J. B., and Richards, F. M. (1982) Anion binding and pH-dependent electrostatic effects in ribonuclease, Biochemistry 21, 4989-99.
    • (1982) Biochemistry , vol.21 , pp. 4989-4999
    • Matthew, J.B.1    Richards, F.M.2
  • 42
    • 0030575785 scopus 로고    scopus 로고
    • Is apomyoglobin a molten globule? Structural characterization by NMR
    • Eliezer, D., and Wright, P. E. (1996) Is apomyoglobin a molten globule? Structural characterization by NMR, J. Mol. Biol. 263, 531-8.
    • (1996) J. Mol. Biol. , vol.263 , pp. 531-538
    • Eliezer, D.1    Wright, P.E.2
  • 43
    • 0020474627 scopus 로고
    • Effect on protein stability of reversing the charge on amino groups, Biochim
    • Hollecker, M., and Creighton, T. E. (1982) Effect on protein stability of reversing the charge on amino groups, Biochim. Biophys. Acta 701, 395-404.
    • (1982) Biophys. Acta , vol.701 , pp. 395-404
    • Hollecker, M.1    Creighton, T.E.2
  • 44
    • 0032498239 scopus 로고    scopus 로고
    • Unfolding of apomyoglobin from Aplysia limacina: The effect of salt and pH on the cooperativity of folding
    • Staniforth, R. A., Bigotti, M. G., Cutruzzola, F., Allocatelli, C. T., and Brunori, M. (1998) Unfolding of apomyoglobin from Aplysia limacina: the effect of salt and pH on the cooperativity of folding, J. Mol. Biol. 275, 133-48.
    • (1998) J. Mol. Biol. , vol.275 , pp. 133-148
    • Staniforth, R.A.1    Bigotti, M.G.2    Cutruzzola, F.3    Allocatelli, C.T.4    Brunori, M.5
  • 45
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. (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.1
  • 47
    • 0000913086 scopus 로고
    • A Fast Algorithm for Rendering Space-Filling Molecule Pictures
    • Bacon, D. J., and Anderson, W. F. (1988) A Fast Algorithm for Rendering Space-Filling Molecule Pictures, J. Mol. Graphics 6, 219-220.
    • (1988) J. Mol. Graphics , vol.6 , pp. 219-220
    • Bacon, D.J.1    Anderson, W.F.2
  • 48
    • 0001022707 scopus 로고    scopus 로고
    • Protonation Behavior of Histidine 24 and Histidine 119 in Forming the pH 4 Folding Intermediate of Apomyoglobin
    • Geierstanger, B., Jamin, M., Volkman, B. F., and Baldwin, R. L. (1998) Protonation Behavior of Histidine 24 and Histidine 119 in Forming the pH 4 Folding Intermediate of Apomyoglobin, Biochemistry 37, 4254-4265.
    • (1998) Biochemistry , vol.37 , pp. 4254-4265
    • Geierstanger, B.1    Jamin, M.2    Volkman, B.F.3    Baldwin, R.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.