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Volumn 1, Issue 2, 1996, Pages 145-156

The development of tertiary interactions during the folding of a large protein

Author keywords

Microdomains; Protein engineering, protein folding; Tertiary interactions; Transition states

Indexed keywords

PHOSPHOGLYCERATE KINASE; PROTEIN; SOLVENT;

EID: 0030347884     PISSN: 13590278     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1359-0278(96)00023-5     Document Type: Article
Times cited : (47)

References (51)
  • 1
    • 0001861319 scopus 로고
    • How proteins fold graciously
    • Debrunner, P., Tsibris, J.C.M. & Miinck, E., eds., University of Illinois Press, Urbana
    • Levinthal, C. (1969). How proteins fold graciously. In Mossbauer Spectroscopy in Biological Systems. (Debrunner, P., Tsibris, J.C.M. & Miinck, E., eds.), pp. 22-24, University of Illinois Press, Urbana.
    • (1969) Mossbauer Spectroscopy in Biological Systems , pp. 22-24
    • Levinthal, C.1
  • 2
    • 0028958601 scopus 로고
    • Characterising transition states in protein folding - An essential step in the puzzle
    • Fersht, A.R. (1995). Characterising transition states in protein folding - an essential step in the puzzle. Curr. Opin. Struct. Biol. 5, 79-84.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 79-84
    • Fersht, A.R.1
  • 3
    • 0025345415 scopus 로고
    • Intermediates in the folding reactions of small proteins
    • Kim, P.S. & Baldwin, R.L. (1990). Intermediates in the folding reactions of small proteins. Annu. Rev. Biochem. 59, 631-666.
    • (1990) Annu. Rev. Biochem. , vol.59 , pp. 631-666
    • Kim, P.S.1    Baldwin, R.L.2
  • 4
    • 0004260243 scopus 로고
    • Creighton, T.E., ed., W.H. Freeman & Co., New York
    • Creighton, T.E. (1992). Protein Folding. (Creighton, T.E., ed.), W.H. Freeman & Co., New York.
    • (1992) Protein Folding
    • Creighton, T.E.1
  • 5
    • 0024391879 scopus 로고
    • How does protein folding get started?
    • Baldwin, R.L. (1989). How does protein folding get started? Trends Biochem. Sci. 14, 291-294.
    • (1989) Trends Biochem. Sci. , vol.14 , pp. 291-294
    • Baldwin, R.L.1
  • 6
    • 0028327236 scopus 로고
    • Protein folding dynamics-the diffusion collision model and experimental data
    • Karplus, M. & Weaver, D.L. (1994). Protein folding dynamics-the diffusion collision model and experimental data. Protein Sci. 3, 650-668.
    • (1994) Protein Sci. , vol.3 , pp. 650-668
    • Karplus, M.1    Weaver, D.L.2
  • 8
    • 0000868733 scopus 로고
    • The protein folding problem
    • Chan, H.S. & Dill, K.A. (1993). The protein folding problem. Physics Today 46, 24-32.
    • (1993) Physics Today , vol.46 , pp. 24-32
    • Chan, H.S.1    Dill, K.A.2
  • 9
    • 0028917296 scopus 로고
    • Structures of folding intermediates
    • Ptitsyn, O.B. (1995). Structures of folding intermediates. Curr. Opin. Struct. Biol. 5, 74-78.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 74-78
    • Ptitsyn, O.B.1
  • 10
    • 0024293204 scopus 로고
    • Conformation of peptide fragments of proteins in aqueous solution-implications for initiation of protein folding
    • Wright, P.E., Dyson, H.J. & Lerner, D.A. (1988). Conformation of peptide fragments of proteins in aqueous solution-implications for initiation of protein folding. Biochemistry 27, 7167-7175.
    • (1988) Biochemistry , vol.27 , pp. 7167-7175
    • Wright, P.E.1    Dyson, H.J.2    Lerner, D.A.3
  • 11
  • 12
    • 0026781019 scopus 로고
    • Early steps in cytochrome c folding probed by time resolved circular dichroism and fluorescence spectroscopy
    • Hove, G.A., Chaffotte, A.F., Roder, H. & Goldberg, M.E. (1992). Early steps in cytochrome c folding probed by time resolved circular dichroism and fluorescence spectroscopy. Biochemistry 31, 6876-6883.
    • (1992) Biochemistry , vol.31 , pp. 6876-6883
    • Hove, G.A.1    Chaffotte, A.F.2    Roder, H.3    Goldberg, M.E.4
  • 13
    • 0026607096 scopus 로고
    • Early hydrogen bonding events in the folding reaction of ubiquitin
    • Briggs, M.S. & Roder, H. (1992). Early hydrogen bonding events in the folding reaction of ubiquitin. Proc. Natl. Acad. Sci. U.S.A. 89, 2017-2021.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 2017-2021
    • Briggs, M.S.1    Roder, H.2
  • 14
    • 0026751786 scopus 로고
    • The folding of hen lysozyme involves partially structured intermediates and multiple pathways
    • Radford, S.E., Dobson, C.M. & Evans, P.A. (1992). The folding of hen lysozyme involves partially structured intermediates and multiple pathways. Nature 358, 302-307.
    • (1992) Nature , vol.358 , pp. 302-307
    • Radford, S.E.1    Dobson, C.M.2    Evans, P.A.3
  • 15
    • 0027523179 scopus 로고
    • Residual helical structure in the C-terminal fragment of cytochrome c
    • Kuroda, Y. (1993). Residual helical structure in the C-terminal fragment of cytochrome c. Biochemistry 32, 1219-1224.
    • (1993) Biochemistry , vol.32 , pp. 1219-1224
    • Kuroda, Y.1
  • 16
    • 0027165688 scopus 로고
    • Peptide models of protein folding initiation sites 1. Secondary structure formation by peptides corresponding to the G-helix and H-helix of Myoglobin
    • Waltho, J.P., Feher, V.A., Marukta, G., Dyson, H.J. & Wright, P.E. (1993). Peptide models of protein folding initiation sites 1. Secondary structure formation by peptides corresponding to the G-helix and H-helix of Myoglobin. Biochemistry 32, 6337-6347.
    • (1993) Biochemistry , vol.32 , pp. 6337-6347
    • Waltho, J.P.1    Feher, V.A.2    Marukta, G.3    Dyson, H.J.4    Wright, P.E.5
  • 17
    • 0027442944 scopus 로고
    • A noncovalent peptide complex as a model for an early folding intermediate of cytochrome c
    • Wu, L.C., Laub, P.B., Elöve, G.A., Carvey, J. & Roder, H. (1993). A noncovalent peptide complex as a model for an early folding intermediate of cytochrome c. Biochemistry 32, 10271-10276.
    • (1993) Biochemistry , vol.32 , pp. 10271-10276
    • Wu, L.C.1    Laub, P.B.2    Elöve, G.A.3    Carvey, J.4    Roder, H.5
  • 18
    • 0025150383 scopus 로고
    • Origins of structure in globular proteins
    • Chan, H.S. & Dill, K.A. (1990). Origins of structure in globular proteins. Proc. Natl. Acad. Sci. U.S.A. 87, 6388-6392.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 6388-6392
    • Chan, H.S.1    Dill, K.A.2
  • 19
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill, K.A. (1990). Dominant forces in protein folding. Biochemistry 29, 7133-7155.
    • (1990) Biochemistry , vol.29 , pp. 7133-7155
    • Dill, K.A.1
  • 20
    • 0024750637 scopus 로고
    • A lattice statistical mechanics model of the conformational and sequence spaces of proteins
    • Lau, K.F. & Dill, K.A. (1989). A lattice statistical mechanics model of the conformational and sequence spaces of proteins. Macromolecules 22, 3989-3997.
    • (1989) Macromolecules , vol.22 , pp. 3989-3997
    • Lau, K.F.1    Dill, K.A.2
  • 21
    • 0025101549 scopus 로고
    • Theory for protein mutability and biogenesis
    • Lau, K.F. & Dill, K.A. (1990). Theory for protein mutability and biogenesis. Proc. Natl. Acad. Sci. U.S.A. 87, 638-642.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 638-642
    • Lau, K.F.1    Dill, K.A.2
  • 22
    • 0024507791 scopus 로고
    • Alternative packing arrangements in the hydrophobic core of λ repressor
    • Lim, W.A. & Sauer, R.T. (1989). Alternative packing arrangements in the hydrophobic core of λ repressor. Nature 339, 31-36.
    • (1989) Nature , vol.339 , pp. 31-36
    • Lim, W.A.1    Sauer, R.T.2
  • 23
    • 0022423920 scopus 로고
    • Theory for the folding and stability of globular proteins
    • Dill, K.A. (1985). Theory for the folding and stability of globular proteins. Biochemistry 24, 1501-1509.
    • (1985) Biochemistry , vol.24 , pp. 1501-1509
    • Dill, K.A.1
  • 24
    • 0026305716 scopus 로고
    • Protein folding-effect of packing density on chain conformation
    • Gregoret, L.M. & Cohen, F.E. (1991). Protein folding-effect of packing density on chain conformation. J. Mol. Biol. 219, 109-122.
    • (1991) J. Mol. Biol. , vol.219 , pp. 109-122
    • Gregoret, L.M.1    Cohen, F.E.2
  • 25
    • 0026511656 scopus 로고
    • The folding of an enzyme. 1. The theory of protein engineering analysis of stability and pathway of protein folding
    • Fersht, A.R., Serrano, L. &. Matouschek, A. (1992). The folding of an enzyme. 1. The theory of protein engineering analysis of stability and pathway of protein folding. J. Mol. Biol. 224, 771-782.
    • (1992) J. Mol. Biol. , vol.224 , pp. 771-782
    • Fersht, A.R.1    Serrano, L.2    Matouschek, A.3
  • 26
    • 0027474760 scopus 로고
    • The structure of a thermally stable 3 - Phosphoglycerate kinase and a comparison with its mesophilic equivalent
    • Davies, G.J., Gamblin, S.J., Littlechild, J.A. & Watson, H.C. (1993). The structure of a thermally stable 3 - phosphoglycerate kinase and a comparison with its mesophilic equivalent. Proteins 15, 283-289.
    • (1993) Proteins , vol.15 , pp. 283-289
    • Davies, G.J.1    Gamblin, S.J.2    Littlechild, J.A.3    Watson, H.C.4
  • 27
    • 0028791393 scopus 로고
    • An integrated kinetic analysis of intermediates and transition states in protein folding reactions
    • Parker, M.J., Spencer, J. & Clarke, A.R. (1995). An integrated kinetic analysis of intermediates and transition states in protein folding reactions. J. Mol. Biol. 253, 771-786.
    • (1995) J. Mol. Biol. , vol.253 , pp. 771-786
    • Parker, M.J.1    Spencer, J.2    Clarke, A.R.3
  • 28
    • 0024298839 scopus 로고
    • Stability mutants of staphylococcal nuclease - Large compensating enthalpy entropy changes for the reversible denaturation reaction
    • Shortle, D., Meeker, A.K. & Freire, E. (1988). Stability mutants of staphylococcal nuclease - large compensating enthalpy entropy changes for the reversible denaturation reaction. Biochemistry 27, 4761-4768.
    • (1988) Biochemistry , vol.27 , pp. 4761-4768
    • Shortle, D.1    Meeker, A.K.2    Freire, E.3
  • 29
    • 0027156648 scopus 로고
    • The energetics and cooperativity of protein folding: A simple experimental analysis based upon solvation of internal residues
    • Staniforth, R.A., et al., & Clarke, A.R. (1993). The energetics and cooperativity of protein folding: a simple experimental analysis based upon solvation of internal residues. Biochemistry 32, 3842-3851.
    • (1993) Biochemistry , vol.32 , pp. 3842-3851
    • Staniforth, R.A.1    Clarke, A.R.2
  • 30
    • 0027171034 scopus 로고
    • Application of physical organic chemistry to engineered mutants of proteins - Hammond postulate behaviour in the transition state of protein folding
    • Matouschek, A. & Fersht, A.R. (1993). Application of physical organic chemistry to engineered mutants of proteins - Hammond postulate behaviour in the transition state of protein folding. Proc. Natl. Acad. Sci. U.S.A. 90, 7814-7818.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 7814-7818
    • Matouschek, A.1    Fersht, A.R.2
  • 31
    • 0027408620 scopus 로고
    • Small effects of amino-acid replacements on the reduced and unfolded state of pancreatic trypsin inhibitor
    • Goldenberg, D.P. & Zhang, J.-X. (1993). Small effects of amino-acid replacements on the reduced and unfolded state of pancreatic trypsin inhibitor. Proteins 15, 322-329.
    • (1993) Proteins , vol.15 , pp. 322-329
    • Goldenberg, D.P.1    Zhang, J.-X.2
  • 32
    • 0028033157 scopus 로고
    • Electrophoretic characterisation of the denatured states of staphylococcal nuclease
    • Creighton, T.E. & Shortle, D. (1994). Electrophoretic characterisation of the denatured states of staphylococcal nuclease. J. Mol. Biol. 242, 670-682.
    • (1994) J. Mol. Biol. , vol.242 , pp. 670-682
    • Creighton, T.E.1    Shortle, D.2
  • 33
    • 0024295240 scopus 로고
    • Contribution of hydrophobia interactions to protein stability
    • Kellis, J.T., Nyberg, K., Sali, D. & Fersht, A.R. (1988). Contribution of hydrophobia interactions to protein stability. Nature 333, 784-786.
    • (1988) Nature , vol.333 , pp. 784-786
    • Kellis, J.T.1    Nyberg, K.2    Sali, D.3    Fersht, A.R.4
  • 34
    • 0024375463 scopus 로고
    • Energetics of complementary side-chain packing in a protein hydrophobic core
    • Kellis, J.T., Nyberg, K. & Fersht, A.R. (1989). Energetics of complementary side-chain packing in a protein hydrophobic core. Biochemistry 28, 4914-4922.
    • (1989) Biochemistry , vol.28 , pp. 4914-4922
    • Kellis, J.T.1    Nyberg, K.2    Fersht, A.R.3
  • 35
    • 0025005525 scopus 로고
    • Contributions of the large hydrophobic amino acids to the stability of staphylococcal nuclease
    • Shortle, D., Stiles, W.E. & Meeker, A.K. (1990). Contributions of the large hydrophobic amino acids to the stability of staphylococcal nuclease. Biochemistry 29, 8033-8041.
    • (1990) Biochemistry , vol.29 , pp. 8033-8041
    • Shortle, D.1    Stiles, W.E.2    Meeker, A.K.3
  • 36
    • 0026567907 scopus 로고
    • Response of a protein structure to cavity creating mutations and its relation to the hydrophobic effect
    • Eriksson, A.E., et al., & Matthews, B.W. (1992). Response of a protein structure to cavity creating mutations and its relation to the hydrophobic effect. Science 255, 178-183.
    • (1992) Science , vol.255 , pp. 178-183
    • Eriksson, A.E.1    Matthews, B.W.2
  • 37
    • 0025360593 scopus 로고
    • Heat capacity of proteins. 1. Partial molar heat capacity of individual amino acid residues in aqueous solution
    • Makhatadze, G.I. & Privalov, P.L. (1990). Heat capacity of proteins. 1. Partial molar heat capacity of individual amino acid residues in aqueous solution. J. Mol. Biol. 213, 375-381.
    • (1990) J. Mol. Biol. , vol.213 , pp. 375-381
    • Makhatadze, G.I.1    Privalov, P.L.2
  • 38
    • 0026672305 scopus 로고
    • NMR determination of residual structure in a urea-denatured protein, the 434 repressor
    • Neri, D., Billeter, M., Wider, G. & Wüthrich, K. (1992). NMR determination of residual structure in a urea-denatured protein, the 434 repressor. Science 257, 1559-1563.
    • (1992) Science , vol.257 , pp. 1559-1563
    • Neri, D.1    Billeter, M.2    Wider, G.3    Wüthrich, K.4
  • 39
    • 0020698476 scopus 로고
    • Dynamics of proteins - Elements and function
    • Karplus, M. & McCammon, J.A. (1983). Dynamics of proteins - elements and function. Annu. Rev. Biochem. 52, 263-300.
    • (1983) Annu. Rev. Biochem. , vol.52 , pp. 263-300
    • Karplus, M.1    McCammon, J.A.2
  • 41
    • 0024802618 scopus 로고
    • Filtering molecular dynamics trajectories to reveal low frequency collective motions - Phospholipase A2
    • Sessions, R.B., Osguthorpe, P.D. & Osguthorpe, D.J. (1989). Filtering molecular dynamics trajectories to reveal low frequency collective motions - phospholipase A2. J. Mol. Biol. 209, 617-633.
    • (1989) J. Mol. Biol. , vol.209 , pp. 617-633
    • Sessions, R.B.1    Osguthorpe, P.D.2    Osguthorpe, D.J.3
  • 42
    • 0024417964 scopus 로고
    • The molten globule state as a clue for understanding of the folding and cooperativity of globular protein structure
    • Kuwajima, K. (1989). The molten globule state as a clue for understanding of the folding and cooperativity of globular protein structure. Proteins 6, 87-103.
    • (1989) Proteins , vol.6 , pp. 87-103
    • Kuwajima, K.1
  • 43
    • 0018588511 scopus 로고
    • Stability of proteins; small globular proteins
    • Privalov, P.L. (1979). Stability of proteins; small globular proteins. Adv. Protein Chem. 33, 167-241.
    • (1979) Adv. Protein Chem. , vol.33 , pp. 167-241
    • Privalov, P.L.1
  • 44
  • 45
    • 0000180763 scopus 로고
    • Temperature dependence of the hydrophobic interaction in protein folding
    • Baldwin, R.L. (1986). Temperature dependence of the hydrophobic interaction in protein folding. Proc. Natl. Acad. Sci. U.S.A. 83, 8069-8072.
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 8069-8072
    • Baldwin, R.L.1
  • 46
    • 0002770218 scopus 로고
    • Theoretical models of protein folding
    • Creighton, T.E., ed., Freeman & Co., New York
    • Karplus, M. & Shakhnovich, E. (1992). Theoretical models of protein folding. In Protein Folding. (Creighton, T.E., ed.), pp 127-195, Freeman & Co., New York.
    • (1992) Protein Folding , pp. 127-195
    • Karplus, M.1    Shakhnovich, E.2
  • 47
    • 0025126043 scopus 로고
    • Strategy for analysing the cooperativity of intramolecular interactions in peptides and proteins
    • Horovitz, A. & Fersht, A.R. (1990). Strategy for analysing the cooperativity of intramolecular interactions in peptides and proteins. J. Mol. Biol. 214, 613-617.
    • (1990) J. Mol. Biol. , vol.214 , pp. 613-617
    • Horovitz, A.1    Fersht, A.R.2
  • 48
    • 0026587310 scopus 로고
    • Cooperative interactions during protein folding
    • Horovitz, A. & Fersht, A.R. (1992). Cooperative interactions during protein folding. J. Mol. Biol. 224, 733-740.
    • (1992) J. Mol. Biol. , vol.224 , pp. 733-740
    • Horovitz, A.1    Fersht, A.R.2
  • 49
    • 0029055313 scopus 로고
    • LINUS a hierarchical procedure to predict the fold of a protein
    • Srinivasan, R. & Rose, G.D. (1995). LINUS a hierarchical procedure to predict the fold of a protein. Proteins 22, 81-99.
    • (1995) Proteins , vol.22 , pp. 81-99
    • Srinivasan, R.1    Rose, G.D.2
  • 50
    • 0014718113 scopus 로고
    • Protein denaturation
    • Tanford, C. (1970). Protein denaturation. Adv. Protein Chem. 24, 1-95.
    • (1970) Adv. Protein Chem. , vol.24 , pp. 1-95
    • Tanford, C.1
  • 51
    • 0016505899 scopus 로고
    • The stability of globular proteins
    • Pace, C.N. (1975). The stability of globular proteins. CRC Crit. Rev. Biochem. 3, 1-43.
    • (1975) CRC Crit. Rev. Biochem. , vol.3 , pp. 1-43
    • Pace, C.N.1


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