메뉴 건너뛰기




Volumn 286, Issue 5, 1999, Pages 1597-1608

Rapid folding with and without populated intermediates in the homologous four-helix proteins Im7 and Im9

Author keywords

Four helix bundle; Homologous proteins; Populated intermediates; Protein folding; Rapid kinetics

Indexed keywords

BINDING PROTEIN; SODIUM SULFATE; UREA;

EID: 0033548553     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.2548     Document Type: Article
Times cited : (227)

References (54)
  • 1
    • 0030347877 scopus 로고    scopus 로고
    • On-pathway versus off-pathway folding intermediates
    • Baldwin R. L. On-pathway versus off-pathway folding intermediates. Folding Design. 1:1996;R1-R8.
    • (1996) Folding Design , vol.1
    • Baldwin, R.L.1
  • 3
    • 0032554626 scopus 로고    scopus 로고
    • Protein folding dynamics: Quantitative comparison between theory and experiment
    • Burton R. E., Myers J. K., Oas T. G. Protein folding dynamics: quantitative comparison between theory and experiment. Biochemistry. 37:1998;5337-5343.
    • (1998) Biochemistry , vol.37 , pp. 5337-5343
    • Burton, R.E.1    Myers, J.K.2    Oas, T.G.3
  • 4
    • 0029982778 scopus 로고    scopus 로고
    • The crystal structure of the immunity protein of colicin E7 suggests a possible colicin-interacting surface
    • Chak K. F., Safo M. K., Ku W. Y., Hsieh S. Y., Yuan H. S. The crystal structure of the immunity protein of colicin E7 suggests a possible colicin-interacting surface. Proc. Natl Acad. Sci. USA. 93:1996;6437-6442.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 6437-6442
    • Chak, K.F.1    Safo, M.K.2    Ku, W.Y.3    Hsieh, S.Y.4    Yuan, H.S.5
  • 5
    • 0026545583 scopus 로고
    • Folding kinetics of T4 lysozyme and 9 mutants at 12 °c
    • Chen B. L., Baase W. A., Nicholson H., Schellman J. A. Folding kinetics of T4 lysozyme and 9 mutants at 12 °C. Biochemistry. 31:1992;1464-1476.
    • (1992) Biochemistry , vol.31 , pp. 1464-1476
    • Chen, B.L.1    Baase, W.A.2    Nicholson, H.3    Schellman, J.A.4
  • 6
    • 0031214818 scopus 로고    scopus 로고
    • Folding and stability of a fibronectin type III domain of human tenascin
    • Clarke J., Hamill S. J., Johnson C. M. Folding and stability of a fibronectin type III domain of human tenascin. J. Mol. Biol. 270:1997;771-778.
    • (1997) J. Mol. Biol. , vol.270 , pp. 771-778
    • Clarke, J.1    Hamill, S.J.2    Johnson, C.M.3
  • 7
    • 0028402735 scopus 로고
    • The energetic ups and downs of protein folding
    • Creighton T. E. The energetic ups and downs of protein folding. Nature Struct. Biol. 1:1994;135-138.
    • (1994) Nature Struct. Biol. , vol.1 , pp. 135-138
    • Creighton, T.E.1
  • 8
    • 0029981188 scopus 로고    scopus 로고
    • Structure of the transition-state for folding of a protein derived from experiment and simulation
    • Daggett V., Li A. J., Itzhaki L. S., Otzen D. E., Fersht A. R. Structure of the transition-state for folding of a protein derived from experiment and simulation. J. Mol. Biol. 257:1996;430-440.
    • (1996) J. Mol. Biol. , vol.257 , pp. 430-440
    • Daggett, V.1    Li, A.J.2    Itzhaki, L.S.3    Otzen, D.E.4    Fersht, A.R.5
  • 9
    • 0032127769 scopus 로고    scopus 로고
    • A structural comparison of the colicin immunity proteins Im7 and Im9 gives new insights into the molecular determinants of immunity protein specificity
    • Dennis C. A., Videler H., Pauptit R. A., Wallis R., James R., Moore G. R., Kleanthous C. A structural comparison of the colicin immunity proteins Im7 and Im9 gives new insights into the molecular determinants of immunity protein specificity. Biochem. J. 333:1998;183-191.
    • (1998) Biochem. J. , vol.333 , pp. 183-191
    • Dennis, C.A.1    Videler, H.2    Pauptit, R.A.3    Wallis, R.4    James, R.5    Moore, G.R.6    Kleanthous, C.7
  • 10
    • 0031915141 scopus 로고    scopus 로고
    • A metastable state in folding simulations of a protein model
    • Dinner A. R., Karplus M. A metastable state in folding simulations of a protein model. Nature Struct. Biol. 5:1998;236-241.
    • (1998) Nature Struct. Biol. , vol.5 , pp. 236-241
    • Dinner, A.R.1    Karplus, M.2
  • 11
    • 0028053187 scopus 로고
    • Understanding how proteins fold - The lysozyme story so far
    • Dobson C. M., Evans P. A., Radford S. E. Understanding how proteins fold - the lysozyme story so far. Trends Biochemi. Sci. 19:1994;31-37.
    • (1994) Trends Biochemi. Sci. , vol.19 , pp. 31-37
    • Dobson, C.M.1    Evans, P.A.2    Radford, S.E.3
  • 13
    • 0031444104 scopus 로고    scopus 로고
    • Folding dynamics of the src SH3 domain
    • Grantcharova V. P., Baker D. Folding dynamics of the src SH3 domain. Biochemistry. 36:1997;15685-15692.
    • (1997) Biochemistry , vol.36 , pp. 15685-15692
    • Grantcharova, V.P.1    Baker, D.2
  • 14
    • 0031853167 scopus 로고    scopus 로고
    • Important role of hydrogen bonds in the structurally polarized transition state for folding of the src SH3 domain
    • Grantcharova V. P., Riddle D. S., Santiago J. V., Baker D. Important role of hydrogen bonds in the structurally polarized transition state for folding of the src SH3 domain. Nature Struct. Biol. 5:1998;714-720.
    • (1998) Nature Struct. Biol. , vol.5 , pp. 714-720
    • Grantcharova, V.P.1    Riddle, D.S.2    Santiago, J.V.3    Baker, D.4
  • 15
    • 0032570543 scopus 로고    scopus 로고
    • Folding kinetics of the SH3 domain of PI3-kinase by real-time NMR combined with optical spectroscopy
    • Guijarro J. I., Morton C. J., Plaxco K. W., Campbell I. D., Dobson C. M. Folding kinetics of the SH3 domain of PI3-kinase by real-time NMR combined with optical spectroscopy. J. Mol. Biol. 276:1998;657-667.
    • (1998) J. Mol. Biol. , vol.276 , pp. 657-667
    • Guijarro, J.I.1    Morton, C.J.2    Plaxco, K.W.3    Campbell, I.D.4    Dobson, C.M.5
  • 16
    • 0030967896 scopus 로고    scopus 로고
    • Exploring the folding free energy surface of a three-helix bundle protein
    • Guo Z. Y., Brooks C. L., Boczko E. M. Exploring the folding free energy surface of a three-helix bundle protein. Proc. Natl Acad. Sci. USA. 94:1997;10161-10166.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 10161-10166
    • Guo, Z.Y.1    Brooks, C.L.2    Boczko, E.M.3
  • 17
    • 0031815749 scopus 로고    scopus 로고
    • How do small single-domain proteins fold?
    • Jackson S. E. How do small single-domain proteins fold? Folding Design. 3:1998;R81-R91.
    • (1998) Folding Design , vol.3
    • Jackson, S.E.1
  • 18
    • 0026345750 scopus 로고
    • Folding of chymotrypsin inhibitor-2. 1. Evidence for a 2-state transition
    • Jackson S. E., Fersht A. R. Folding of chymotrypsin inhibitor-2. 1. Evidence for a 2-state transition. Biochemistry. 30:1991a;10428-10435.
    • (1991) Biochemistry , vol.30 , pp. 10428-10435
    • Jackson, S.E.1    Fersht, A.R.2
  • 19
    • 0026342150 scopus 로고
    • Folding of chymotrypsin inhibitor-2. 2. Influence of proline isomerization on the folding kinetics and thermodynamic characterization of the transition-state of folding
    • Jackson S. E., Fersht A. R. Folding of chymotrypsin inhibitor-2. 2. Influence of proline isomerization on the folding kinetics and thermodynamic characterization of the transition-state of folding. Biochemistry. 30:1991b;10436-10443.
    • (1991) Biochemistry , vol.30 , pp. 10436-10443
    • Jackson, S.E.1    Fersht, A.R.2
  • 20
    • 0029949518 scopus 로고    scopus 로고
    • The biology of E colicins: Paradigms and paradoxes
    • James R., Kleanthous C., Moore G. R. The biology of E colicins: paradigms and paradoxes. Microbiol. UK. 142:1996;1569-1580.
    • (1996) Microbiol. UK , vol.142 , pp. 1569-1580
    • James, R.1    Kleanthous, C.2    Moore, G.R.3
  • 21
    • 0029061516 scopus 로고
    • Protein stability as a function of denaturant concentration - The thermal-stability of barnase in the presence of urea
    • Johnson C. M., Fersht A. R. Protein stability as a function of denaturant concentration - the thermal-stability of barnase in the presence of urea. Biochemistry. 34:1995;6795-6804.
    • (1995) Biochemistry , vol.34 , pp. 6795-6804
    • Johnson, C.M.1    Fersht, A.R.2
  • 22
    • 0029868589 scopus 로고    scopus 로고
    • Non-linear free energy relationships in Arc repressor unfolding imply the existence of unstable, native-like folding intermediates
    • Jonsson T., Waldburger C. D., Sauer R. T. Non-linear free energy relationships in Arc repressor unfolding imply the existence of unstable, native-like folding intermediates. Biochemistry. 35:1996;4795-4802.
    • (1996) Biochemistry , vol.35 , pp. 4795-4802
    • Jonsson, T.1    Waldburger, C.D.2    Sauer, R.T.3
  • 23
    • 0028949547 scopus 로고
    • Theoretical-studies of protein folding and unfolding
    • Karplus M., Sali A. Theoretical-studies of protein folding and unfolding. Curr. Opin. Struct. Biol. 5:1995;58-73.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 58-73
    • Karplus, M.1    Sali, A.2
  • 24
    • 0028327236 scopus 로고
    • Protein folding dynamics, the diffusion-collision model, and experimental data
    • Karplus M., Weaver D. L. Protein folding dynamics, the diffusion-collision model, and experimental data. Protein Sci. 3:1994;650-668.
    • (1994) Protein Sci. , vol.3 , pp. 650-668
    • Karplus, M.1    Weaver, D.L.2
  • 25
    • 0027305989 scopus 로고
    • Folding and stability of a tryptophan-containing mutant of ubiquitin
    • Khorasanizadeh S., Peters I. D., Butt T. R., Roder H. Folding and stability of a tryptophan-containing mutant of ubiquitin. Biochemistry. 32:1993;7054-7063.
    • (1993) Biochemistry , vol.32 , pp. 7054-7063
    • Khorasanizadeh, S.1    Peters, I.D.2    Butt, T.R.3    Roder, H.4
  • 26
    • 0030057477 scopus 로고    scopus 로고
    • Evidence for a three-state model of protein folding from kinetic analysis of ubiquitin variants with altered core residues
    • Khorasanizadeh S., Peters I. D., Roder H. Evidence for a three-state model of protein folding from kinetic analysis of ubiquitin variants with altered core residues. Nature Struct. Biol. 3:1996;193-205.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 193-205
    • Khorasanizadeh, S.1    Peters, I.D.2    Roder, H.3
  • 27
    • 0029965111 scopus 로고    scopus 로고
    • Fast and one-step folding of closely and distantly related homologous proteins of a four-helix bundle family
    • Kragelund B. B., Hojrup P., Jensen M. S., Schjerling C. K., Juul E., Knudsen J., Poulsen F. M. Fast and one-step folding of closely and distantly related homologous proteins of a four-helix bundle family. J. Mol. Biol. 256:1996;187-200.
    • (1996) J. Mol. Biol. , vol.256 , pp. 187-200
    • Kragelund, B.B.1    Hojrup, P.2    Jensen, M.S.3    Schjerling, C.K.4    Juul, E.5    Knudsen, J.6    Poulsen, F.M.7
  • 28
    • 0031465967 scopus 로고    scopus 로고
    • "New view" of protein folding reconciled with the old through multiple unfolding simulations
    • Lazaridis T., Karplus M. "New view" of protein folding reconciled with the old through multiple unfolding simulations. Science. 278:1997;1928-1931.
    • (1997) Science , vol.278 , pp. 1928-1931
    • Lazaridis, T.1    Karplus, M.2
  • 29
    • 0031576990 scopus 로고    scopus 로고
    • Fast and slow tracks in lysozyme folding: Insight into the role of domains in the folding process
    • Matagne A., Radford S. E., Dobson C. M. Fast and slow tracks in lysozyme folding: insight into the role of domains in the folding process. J. Mol. Biol. 267:1997;1068-1074.
    • (1997) J. Mol. Biol. , vol.267 , pp. 1068-1074
    • Matagne, A.1    Radford, S.E.2    Dobson, C.M.3
  • 30
    • 0028168139 scopus 로고
    • Extrapolation to water of kinetic and equilibrium data for the unfolding of barnase in urea solutions
    • Matouschek A., Matthews J. M., Johnson C. M., Fersht A. R. Extrapolation to water of kinetic and equilibrium data for the unfolding of barnase in urea solutions. Protein Eng. 7:1994;1089-1095.
    • (1994) Protein Eng. , vol.7 , pp. 1089-1095
    • Matouschek, A.1    Matthews, J.M.2    Johnson, C.M.3    Fersht, A.R.4
  • 31
    • 0030334626 scopus 로고    scopus 로고
    • Universality and diversity of the protein folding scenarios: A comprehensive analysis with the aid of a lattice model
    • Mirny L. A., Abkevich V., Shakhnovich E. I. Universality and diversity of the protein folding scenarios: a comprehensive analysis with the aid of a lattice model. Folding Design. 1:1996;103-116.
    • (1996) Folding Design , vol.1 , pp. 103-116
    • Mirny, L.A.1    Abkevich, V.2    Shakhnovich, E.I.3
  • 32
    • 0031127043 scopus 로고    scopus 로고
    • Development of the multiple sequence approximation within the AGADIR model of alpha-helix formation: Comparison with Zimm-Bragg and Lifson-Roig formalisms
    • Mu ñ V., Serrano L. Development of the multiple sequence approximation within the AGADIR model of alpha-helix formation: comparison with Zimm-Bragg and Lifson-Roig formalisms. Biopolymers. 41:1997;495-509.
    • (1997) Biopolymers , vol.41 , pp. 495-509
    • Mu Ñ., V.1    Serrano, L.2
  • 33
    • 0028820703 scopus 로고
    • Denaturant m-values and heat-capacity changes-relation to changes in accessible surface areas of protein unfolding
    • Myers J. K., Pace C. N., Scholtz J. M. Denaturant m-values and heat-capacity changes-relation to changes in accessible surface areas of protein unfolding. Protein Sci. 4:1995;2138-2148.
    • (1995) Protein Sci. , vol.4 , pp. 2138-2148
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 35
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace C. N. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 131:1986;3286-3299.
    • (1986) Methods Enzymol. , vol.131 , pp. 3286-3299
    • Pace, C.N.1
  • 36
    • 0030664958 scopus 로고    scopus 로고
    • An early intermediate in the folding reaction of the B1 domain of protein G contains a native-like core
    • Park S. H., Oneil K. T., Roder H. An early intermediate in the folding reaction of the B1 domain of protein G contains a native-like core. Biochemistry. 36:1997;14277-14283.
    • (1997) Biochemistry , vol.36 , pp. 14277-14283
    • Park, S.H.1    Oneil, K.T.2    Roder, H.3
  • 38
    • 0031214363 scopus 로고    scopus 로고
    • A comparison of the folding kinetics and thermodynamics of two homologous fibronectin type III modules
    • Plaxco K. W., Spitzfaden C., Campbell I. D., Dobson C. M. A comparison of the folding kinetics and thermodynamics of two homologous fibronectin type III modules. J. Mol. Biol. 270:1997;763-770.
    • (1997) J. Mol. Biol. , vol.270 , pp. 763-770
    • Plaxco, K.W.1    Spitzfaden, C.2    Campbell, I.D.3    Dobson, C.M.4
  • 40
    • 0032502839 scopus 로고    scopus 로고
    • Contact order, transition state placement and the refolding rates of single domain proteins
    • Plaxco K. W., Simons K. T., Baker D. Contact order, transition state placement and the refolding rates of single domain proteins. J. Mol. Biol. 277:1998b;985-994.
    • (1998) J. Mol. Biol. , vol.277 , pp. 985-994
    • Plaxco, K.W.1    Simons, K.T.2    Baker, D.3
  • 41
    • 0031697733 scopus 로고    scopus 로고
    • The burst phase in ribonuclease A, folding and solvent dependence of the unfolded state
    • Qi P. X., Sosnick T. R., Englander S. W. The burst phase in ribonuclease A, folding and solvent dependence of the unfolded state. Nature Struct. Biol. 5:1998;882-884.
    • (1998) Nature Struct. Biol. , vol.5 , pp. 882-884
    • Qi, P.X.1    Sosnick, T.R.2    Englander, S.W.3
  • 42
    • 0026751786 scopus 로고
    • The folding of hen lysozyme involves partially structured intermediates and multiple pathways
    • Radford S. E., Dobson C. M., Evans P. A. The folding of hen lysozyme involves partially structured intermediates and multiple pathways. Nature. 358:1992;302-307.
    • (1992) Nature , vol.358 , pp. 302-307
    • Radford, S.E.1    Dobson, C.M.2    Evans, P.A.3
  • 43
    • 0031937871 scopus 로고    scopus 로고
    • Stability and folding properties of a model beta-sheet protein, Escherichia coli CspA
    • Reid K. L., Rodriguez H. M., Hillier B. J., Gregoret L. M. Stability and folding properties of a model beta-sheet protein, Escherichia coli CspA. Protein Sci. 7:1998;470-479.
    • (1998) Protein Sci. , vol.7 , pp. 470-479
    • Reid, K.L.1    Rodriguez, H.M.2    Hillier, B.J.3    Gregoret, L.M.4
  • 45
    • 0031055942 scopus 로고    scopus 로고
    • Kinetic role of early intermediates in protein folding
    • Roder H., Colón W. Kinetic role of early intermediates in protein folding. Curr. Opin. Struct. Biol. 7:1997;15-28.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 15-28
    • Roder, H.1    Colón, W.2
  • 46
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants
    • Santoro M., Bolen D. W. Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants. Biochemistry. 27:1988;8063-8068.
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.1    Bolen, D.W.2
  • 48
    • 0030750236 scopus 로고    scopus 로고
    • High-energy channeling in protein folding
    • Silow M., Oliveberg M. High-energy channeling in protein folding. Biochemistry. 36:1997a;7633-7637.
    • (1997) Biochemistry , vol.36 , pp. 7633-7637
    • Silow, M.1    Oliveberg, M.2
  • 49
    • 0030958760 scopus 로고    scopus 로고
    • Transient aggregates in protein folding are easily mistaken for folding intermediates
    • Silow M., Oliveberg M. Transient aggregates in protein folding are easily mistaken for folding intermediates. Proc. Natl Acad. Sci. USA. 94:1997b;6084-6086.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 6084-6086
    • Silow, M.1    Oliveberg, M.2
  • 51
    • 0028331876 scopus 로고
    • Thermodynamic and kinetic-analysis of the SH3 domain of spectrin shows a 2-state folding transition
    • Viguera A. R., Martinez J. C., Filimonov V. V., Mateo P. L., Serrano L. Thermodynamic and kinetic-analysis of the SH3 domain of spectrin shows a 2-state folding transition. Biochemistry. 33:1994;2142-2150.
    • (1994) Biochemistry , vol.33 , pp. 2142-2150
    • Viguera, A.R.1    Martinez, J.C.2    Filimonov, V.V.3    Mateo, P.L.4    Serrano, L.5
  • 52
    • 0029760326 scopus 로고    scopus 로고
    • Different folding transition-states may result in the same native structure
    • Viguera A. R., Serrano L., Wilmanns M. Different folding transition-states may result in the same native structure. Nature Struct. Biol. 3:1996;874-880.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 874-880
    • Viguera, A.R.1    Serrano, L.2    Wilmanns, M.3
  • 53
    • 0026724613 scopus 로고
    • In vivo and in vitro characterization of overproduced colicin E9 immunity protein
    • Wallis R., Reilly A., Rowe A., Moore G. R., James R., Kleanthous C. In vivo and in vitro characterization of overproduced colicin E9 immunity protein. Eur. J. Biochem. 207:1992;687-695.
    • (1992) Eur. J. Biochem. , vol.207 , pp. 687-695
    • Wallis, R.1    Reilly, A.2    Rowe, A.3    Moore, G.R.4    James, R.5    Kleanthous, C.6
  • 54
    • 0032512424 scopus 로고    scopus 로고
    • Specificity in protein-protein recognition: Conserved Im9 residues are the major determinats of stability in the colicin E9 DNase-Im9 complex
    • Wallis R., Leung K.-Y., Osborne M., James R., Moore G., Kleanthous C. Specificity in protein-protein recognition: conserved Im9 residues are the major determinats of stability in the colicin E9 DNase-Im9 complex. Biochemistry. 37:1998;476-485.
    • (1998) Biochemistry , vol.37 , pp. 476-485
    • Wallis, R.1    Leung, K.-Y.2    Osborne, M.3    James, R.4    Moore, G.5    Kleanthous, C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.