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Volumn 45, Issue 27, 2006, Pages 8393-8401

Extensive misfolding in the refolding reaction of alkaline ferrocytochrome c

Author keywords

[No Author keywords available]

Indexed keywords

ALKALINITY; CARBON MONOXIDE; CELL MEMBRANES; POLYPEPTIDES;

EID: 33745838251     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi060141z     Document Type: Article
Times cited : (4)

References (48)
  • 1
    • 0009586942 scopus 로고    scopus 로고
    • Understanding protein folding via free-energy surfaces from theory and experiment
    • Dinner, A. R., Sali, A., Smith, L. J., Dobson, C. M., and Karplus, M. (2000) Understanding protein folding via free-energy surfaces from theory and experiment, Trends Biochem. Sci. 25, 331-339.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 331-339
    • Dinner, A.R.1    Sali, A.2    Smith, L.J.3    Dobson, C.M.4    Karplus, M.5
  • 2
    • 0032502839 scopus 로고    scopus 로고
    • Contact order, transition state placement and the refolding rates of single domain proteins
    • Plaxco, K. W., Simons, K. T., and Baker, D. (1998) Contact order, transition state placement and the refolding rates of single domain proteins, J. Mol. Biol. 277, 985-994.
    • (1998) J. Mol. Biol. , vol.277 , pp. 985-994
    • Plaxco, K.W.1    Simons, K.T.2    Baker, D.3
  • 3
    • 0034604105 scopus 로고    scopus 로고
    • A surprising simplicity to protein folding
    • Baker, D. A. (2000) A surprising simplicity to protein folding, Nature 405, 39-42.
    • (2000) Nature , vol.405 , pp. 39-42
    • Baker, D.A.1
  • 4
    • 0037215268 scopus 로고    scopus 로고
    • The topomer search model: A simple, quantitative theory of two-state protein folding kinetics
    • Makarov, D. E., and Plaxco, K. W. (2003) The topomer search model: a simple, quantitative theory of two-state protein folding kinetics, Protein Sci. 12, 17-26.
    • (2003) Protein Sci. , vol.12 , pp. 17-26
    • Makarov, D.E.1    Plaxco, K.W.2
  • 5
    • 0029940033 scopus 로고    scopus 로고
    • Molecular collapse: The rate-limiting step in two-state cytochrome c folding
    • Sosnick, T. R., Mayne, L., and Englander, S. W. (1996) Molecular collapse: the rate-limiting step in two-state cytochrome c folding, Proteins 24, 413-426.
    • (1996) Proteins , vol.24 , pp. 413-426
    • Sosnick, T.R.1    Mayne, L.2    Englander, S.W.3
  • 7
    • 14344261397 scopus 로고    scopus 로고
    • Protein folding in classical perspecive: Folding of horse cytochrome c
    • Bhuyan, A. K., Rao, D. K., and Prabhu, N. P. (2005) Protein folding in classical perspecive: folding of horse cytochrome c, Biochemistry 44, 3034-3040.
    • (2005) Biochemistry , vol.44 , pp. 3034-3040
    • Bhuyan, A.K.1    Rao, D.K.2    Prabhu, N.P.3
  • 8
    • 0029740071 scopus 로고    scopus 로고
    • Non-native alpha-helical intermediate in the refolding of beta-lactoglobulin, a predominantly beta-sheet protein
    • Hamada, D., Segawa, S.-I., and Goto, Y. (1996) Non-native alpha-helical intermediate in the refolding of beta-lactoglobulin, a predominantly beta-sheet protein, Nat. Struct. Biol. 3, 868-873.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 868-873
    • Hamada, D.1    Segawa, S.-I.2    Goto, Y.3
  • 9
    • 0342679998 scopus 로고    scopus 로고
    • Transient non-native secondary structures during the refolding of alpha-lactalbumin detected by infrared spectroscopy
    • Troullier, A., Reinstädler, D., Dupont, Y., Naumann, D., and Forge, V. (2000) Transient non-native secondary structures during the refolding of alpha-lactalbumin detected by infrared spectroscopy, Nat. Struct. Biol. 7, 78-86.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 78-86
    • Troullier, A.1    Reinstädler, D.2    Dupont, Y.3    Naumann, D.4    Forge, V.5
  • 10
    • 0036183221 scopus 로고    scopus 로고
    • Im7 folding mechanism: Misfolding on a path to the native state
    • Capaldi, A. P., Kleanthous, C., and Radford, S. E. (2002) Im7 folding mechanism: misfolding on a path to the native state, Nat. Struct. Biol. 9, 209-216.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 209-216
    • Capaldi, A.P.1    Kleanthous, C.2    Radford, S.E.3
  • 11
    • 0842281551 scopus 로고    scopus 로고
    • Principles of protein folding, misfolding and aggregation
    • Dobson, C. M. (2004) Principles of protein folding, misfolding and aggregation, Semin. Cell Dev. Biol. 15, 3-16.
    • (2004) Semin. Cell Dev. Biol. , vol.15 , pp. 3-16
    • Dobson, C.M.1
  • 12
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: From nascent chain to folded proteins
    • Hartl, F. U., and Hayer-Hartl, M. (2002) Molecular chaperones in the cytosol: from nascent chain to folded proteins, Science 295, 1852-1858.
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 13
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething, M.-J., and Sambrook, J. (1992) Protein folding in the cell, Nature 355, 33-45.
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.-J.1    Sambrook, J.2
  • 14
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl α-chymotrypsin 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 α-chymotrypsin using different denaturants, Biochemistry 27, 8063-8068.
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2
  • 15
    • 0014718113 scopus 로고
    • Protein denaturation. C. Theoretical models for the mechanism of denaturation
    • Tanford, C. (1970) Protein denaturation. C. Theoretical models for the mechanism of denaturation, Adv. Protein Chem. 24, 1-95.
    • (1970) Adv. Protein Chem. , vol.24 , pp. 1-95
    • Tanford, C.1
  • 16
  • 17
    • 0032878322 scopus 로고    scopus 로고
    • Formation of short-lived protein aggregates directly from the coil in two-state folding
    • Silow, M., Tan, Y.-J., Fersht, A. R., and Oliveberg, M. (1999) Formation of short-lived protein aggregates directly from the coil in two-state folding, Biochemistry 38, 13006-13012.
    • (1999) Biochemistry , vol.38 , pp. 13006-13012
    • Silow, M.1    Tan, Y.-J.2    Fersht, A.R.3    Oliveberg, M.4
  • 18
    • 0015522926 scopus 로고
    • Electromagnetic properties of hemoproteins. V. Optical and electron paramagnetic resonance characteristics of nitric oxide derivatives of metalloporphyrin-apohemoprotein complexes
    • Yonetani, T., Yamamoto, H., Erman, J. E., Leigh, J. S., and Reed, G. H. (1972) Electromagnetic properties of hemoproteins. V. Optical and electron paramagnetic resonance characteristics of nitric oxide derivatives of metalloporphyrin-apohemoprotein complexes, J. Biol. Chem. 247, 2447-2455.
    • (1972) J. Biol. Chem. , vol.247 , pp. 2447-2455
    • Yonetani, T.1    Yamamoto, H.2    Erman, J.E.3    Leigh, J.S.4    Reed, G.H.5
  • 19
    • 0022555898 scopus 로고
    • Fast-folding and slow folding forms of unfolded proteins
    • Schmid, F. X. (1986) Fast-folding and slow folding forms of unfolded proteins, Methods Enzymol. 131, 70-82.
    • (1986) Methods Enzymol. , vol.131 , pp. 70-82
    • Schmid, F.X.1
  • 20
    • 0030796986 scopus 로고    scopus 로고
    • Three-state model for lysozyme folding: Triangular folding mechanism with an energetically trapped intermediate
    • Wildegger, G., and Kiefhaber, T. (1997) Three-state model for lysozyme folding: triangular folding mechanism with an energetically trapped intermediate, J. Mol. Biol. 270, 294-304.
    • (1997) J. Mol. Biol. , vol.270 , pp. 294-304
    • Wildegger, G.1    Kiefhaber, T.2
  • 21
    • 0013807126 scopus 로고
    • On the conformational stability of globular proteins. The effect of various electrolytes and nonelectrolytes on the thermal ribonuclease transition
    • von Hippel, P. H., and Wong, K.-Y. (1965) On the conformational stability of globular proteins. The effect of various electrolytes and nonelectrolytes on the thermal ribonuclease transition, J. Biol. Chem. 240, 3909-3923.
    • (1965) J. Biol. Chem. , vol.240 , pp. 3909-3923
    • Von Hippel, P.H.1    Wong, K.-Y.2
  • 22
    • 0037159215 scopus 로고    scopus 로고
    • Kinetic barriers to the folding of horse cytochrome c in the reduced state
    • Bhuyan, A. K., and Kumar, R. (2002) Kinetic barriers to the folding of horse cytochrome c in the reduced state, Biochemistry 41, 12821-12834.
    • (2002) Biochemistry , vol.41 , pp. 12821-12834
    • Bhuyan, A.K.1    Kumar, R.2
  • 23
    • 1442277673 scopus 로고    scopus 로고
    • Folding barrier in horse cytochrome c: Support for a classical folding pathway
    • Prabhu, N. P., Kumar, R., and Bhuyan, A. K. (2004) Folding barrier in horse cytochrome c: support for a classical folding pathway, J. Mol. Biol. 337, 195-208.
    • (2004) J. Mol. Biol. , vol.337 , pp. 195-208
    • Prabhu, N.P.1    Kumar, R.2    Bhuyan, A.K.3
  • 24
    • 14344267020 scopus 로고    scopus 로고
    • Two-state folding of horse ferrocytochrome c: Analyses of linear free energy relationship, chevron curvature, and stopped-flow burst relaxation kinetics
    • Kumar, R., and Bhuyan, A. K. (2005) Two-state folding of horse ferrocytochrome c: analyses of linear free energy relationship, chevron curvature, and stopped-flow burst relaxation kinetics, Biochemistry 44, 3024-3033.
    • (2005) Biochemistry , vol.44 , pp. 3024-3033
    • Kumar, R.1    Bhuyan, A.K.2
  • 25
    • 0023758305 scopus 로고
    • NMR evidence for an early intermediate in the folding pathway of ribonuclease A
    • Udgaonkar, J. B., and Baldwin, R. L. (1988) NMR evidence for an early intermediate in the folding pathway of ribonuclease A, Nature 335, 694-699.
    • (1988) Nature , vol.335 , pp. 694-699
    • Udgaonkar, J.B.1    Baldwin, R.L.2
  • 26
    • 0023705432 scopus 로고
    • Structural characterization of folding intermediates in cytochrome c by H-exchange labeling and proton NMR
    • Roder, H., Elove, G. A., and Englander, S. W. (1988) Structural characterization of folding intermediates in cytochrome c by H-exchange labeling and proton NMR, Nature 335, 700-704.
    • (1988) Nature , vol.335 , pp. 700-704
    • Roder, H.1    Elove, G.A.2    Englander, S.W.3
  • 27
    • 0031026007 scopus 로고    scopus 로고
    • How important is the molten globule for correct protein folding
    • Creighton, T. E. (1997) How important is the molten globule for correct protein folding, Trends Biochem. Sci. 22, 6-10.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 6-10
    • Creighton, T.E.1
  • 28
    • 0025698613 scopus 로고
    • Transient folding intermediates characterized by protein engineering
    • Matouschek, A., Kellis, J. T., Jr., Serrano, L., Bycroft, M., and Fersht, A. R. (1990) Transient folding intermediates characterized by protein engineering, Nature 346, 440-445.
    • (1990) Nature , vol.346 , pp. 440-445
    • Matouschek, A.1    Kellis Jr., J.T.2    Serrano, L.3    Bycroft, M.4    Fersht, A.R.5
  • 29
    • 0029015319 scopus 로고
    • The nature of the initial step in the condormational folding of disulfide-intact ribonuclease A
    • Houry, W. A., Rothwarf, D. M., and Scheraga, H. A. (1995) The nature of the initial step in the condormational folding of disulfide-intact ribonuclease A, Nat. Struct. Biol. 2, 495-503.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 495-503
    • Houry, W.A.1    Rothwarf, D.M.2    Scheraga, H.A.3
  • 30
    • 0030057477 scopus 로고    scopus 로고
    • Evidence for a three-state model of protein foding from kinetic analysis of ubiquitin variants with altered core residues
    • Khorasanizadeh, S., Peters, I. D., and Roder, H. (1996) Evidence for a three-state model of protein foding from kinetic analysis of ubiquitin variants with altered core residues, Nat. Struct. Biol. 3, 193-205.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 193-205
    • Khorasanizadeh, S.1    Peters, I.D.2    Roder, H.3
  • 31
    • 0030347877 scopus 로고    scopus 로고
    • On-pathway versus off-pathway folding intermediates
    • Baldwin, R. L. (1996) On-pathway versus off-pathway folding intermediates, Folding Des. 1, R1-R8.
    • (1996) Folding Des. , vol.1
    • Baldwin, R.L.1
  • 32
    • 33645240906 scopus 로고    scopus 로고
    • Prediction of folding rates of small proteins: Empirical relations based on length, secondary structure content, residue type, and stability
    • Prabhu, N. P., and Bhuyan, A. K. (2006) Prediction of folding rates of small proteins: empirical relations based on length, secondary structure content, residue type, and stability, Biochemistry 45, 3805-3812.
    • (2006) Biochemistry , vol.45 , pp. 3805-3812
    • Prabhu, N.P.1    Bhuyan, A.K.2
  • 33
    • 0031043161 scopus 로고    scopus 로고
    • Nucleation mechanism in protein folding
    • Fersht, A. R. (1997) Nucleation mechanism in protein folding, Curr. Opin. Struct. Biol. 7, 3-9.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 3-9
    • Fersht, A.R.1
  • 35
    • 0032147243 scopus 로고    scopus 로고
    • Protein folding mechanisms and the multidimensional folding funnel
    • Socci, N. D., Onuchic, J. N., and Wolynes, P. G. (1998) Protein folding mechanisms and the multidimensional folding funnel, Proteins 32, 136-158.
    • (1998) Proteins , vol.32 , pp. 136-158
    • Socci, N.D.1    Onuchic, J.N.2    Wolynes, P.G.3
  • 36
    • 2342525803 scopus 로고    scopus 로고
    • Latest folding game results: Protein A barely frustrates computationalists
    • Wolynes, P. G. (2004) Latest folding game results: protein A barely frustrates computationalists, Proc. Natl. Acad. Sci. U.S.A. 101, 6837-6838.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 6837-6838
    • Wolynes, P.G.1
  • 38
    • 0027163998 scopus 로고
    • Protein folding and stability: The pathway of folding of barnase
    • Fersht, A. R. (1993) Protein folding and stability: the pathway of folding of barnase, FEBS Lett. 325, 5-16.
    • (1993) FEBS Lett. , vol.325 , pp. 5-16
    • Fersht, A.R.1
  • 39
    • 0032582479 scopus 로고    scopus 로고
    • A pulse-chase-competition experiment to determine if a folding intermediate is on or off-pathway: Application to ribonuclease A
    • Laurents, D. V., Bruix, M., Jamin, M., and Baldwin, R. L. (1998) A pulse-chase-competition experiment to determine if a folding intermediate is on or off-pathway: application to ribonuclease A, J. Mol. Biol. 283, 669-678.
    • (1998) J. Mol. Biol. , vol.283 , pp. 669-678
    • Laurents, D.V.1    Bruix, M.2    Jamin, M.3    Baldwin, R.L.4
  • 40
    • 13044284157 scopus 로고    scopus 로고
    • Kinetic evidence for an on-pathway intermediate in the folding of cytochrome c
    • Bai, Y. (1999) Kinetic evidence for an on-pathway intermediate in the folding of cytochrome c, Proc. Natl. Acad. Sci. U.S.A. 96, 477-480.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 477-480
    • Bai, Y.1
  • 41
    • 0025949415 scopus 로고
    • Reexamination of the folding of BPTI: Predominance of native intermediates
    • Weisman, J. S., and Kim, P. S. (1991) Reexamination of the folding of BPTI: predominance of native intermediates, Science 253, 1386-1393.
    • (1991) Science , vol.253 , pp. 1386-1393
    • Weisman, J.S.1    Kim, P.S.2
  • 42
    • 0026538017 scopus 로고
    • Kinetic coupling between protein folding and prolyl isomerization. II. Folding of ribonuclease A and ribonuclease T1
    • Kiefhaber, T., and Schmid, F. X. (1992) Kinetic coupling between protein folding and prolyl isomerization. II. Folding of ribonuclease A and ribonuclease T1, J. Mol. Biol. 224, 231-240.
    • (1992) J. Mol. Biol. , vol.224 , pp. 231-240
    • Kiefhaber, T.1    Schmid, F.X.2
  • 43
    • 0028352044 scopus 로고
    • Kinetic mechanism of cytochrome c folding: Involvement of the heme and its ligands
    • Elöve, G. A., Bhuyan, A. K., and Roder, H. (1994) Kinetic mechanism of cytochrome c folding: involvement of the heme and its ligands, Biochemistry 33, 6925-6935.
    • (1994) Biochemistry , vol.33 , pp. 6925-6935
    • Elöve, G.A.1    Bhuyan, A.K.2    Roder, H.3
  • 44
    • 0025832142 scopus 로고
    • Effective concentrations of amino acid side chains in an unfolded protein
    • Muthukrishnan, K., and Nail, B. T. (1991) Effective concentrations of amino acid side chains in an unfolded protein, Biochemistry 30, 4706-4710.
    • (1991) Biochemistry , vol.30 , pp. 4706-4710
    • Muthukrishnan, K.1    Nail, B.T.2
  • 45
    • 0035812628 scopus 로고    scopus 로고
    • Folding of horse cytochrome c in the reduced state
    • Bhuyan, A. K., and Udgaonkar, J. B. (2001) Folding of horse cytochrome c in the reduced state, J. Mol. Biol. 312, 1135-1160.
    • (2001) J. Mol. Biol. , vol.312 , pp. 1135-1160
    • Bhuyan, A.K.1    Udgaonkar, J.B.2
  • 47
    • 0029967474 scopus 로고    scopus 로고
    • Side chain packing of the N- and C-terminal helices plays a critical role in the kinetics of cytochrome c folding
    • Colón, W., Elöve, G. A., Wakem, L. P., Sherman, F., and Roder, H. (1996) Side chain packing of the N- and C-terminal helices plays a critical role in the kinetics of cytochrome c folding, Biochemistry 35, 5538-5549.
    • (1996) Biochemistry , vol.35 , pp. 5538-5549
    • Colón, W.1    Elöve, G.A.2    Wakem, L.P.3    Sherman, F.4    Roder, H.5
  • 48
    • 0031022024 scopus 로고    scopus 로고
    • Two-state models of protein folding kinetics
    • Zwanzig, R. W. (1997) Two-state models of protein folding kinetics, Proc. Natl. Acad. Sci. U.S.A. 94, 148-150.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 148-150
    • Zwanzig, R.W.1


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