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Volumn 390, Issue 5, 2009, Pages 1074-1085

Different Members of a Simple Three-Helix Bundle Protein Family Have Very Different Folding Rate Constants and Fold by Different Mechanisms

Author keywords

chevron; folding mechanism; phi value; protein folding; helix

Indexed keywords

FODRIN; MUTANT PROTEIN; PROTEIN R15; PROTEIN R16; PROTEIN R17; UNCLASSIFIED DRUG;

EID: 67649840692     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.05.010     Document Type: Article
Times cited : (35)

References (44)
  • 2
    • 13844299144 scopus 로고    scopus 로고
    • The family feud: do proteins with similar structures fold via the same pathway?
    • Zarrine-Afsar A., Larson S.M., and Davidson A.R. The family feud: do proteins with similar structures fold via the same pathway?. J. Mol. Biol. 15 (2005) 42-49
    • (2005) J. Mol. Biol. , vol.15 , pp. 42-49
    • Zarrine-Afsar, A.1    Larson, S.M.2    Davidson, A.R.3
  • 4
    • 34547151184 scopus 로고    scopus 로고
    • The helix-turn-helix motif as an ultrafast independently folding domain: the pathway of folding of engrailed homeodomain
    • Religa T.L., Johnson C.M., Vu D.M., Brewer S.H., Dyer R.B., and Fersht A.R. The helix-turn-helix motif as an ultrafast independently folding domain: the pathway of folding of engrailed homeodomain. Proc. Natl Acad. Sci. USA 104 (2007) 9272-9277
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 9272-9277
    • Religa, T.L.1    Johnson, C.M.2    Vu, D.M.3    Brewer, S.H.4    Dyer, R.B.5    Fersht, A.R.6
  • 5
    • 27144532135 scopus 로고    scopus 로고
    • Solution structure of a protein denatured state and folding intermediate
    • Religa T.L., Markson J.S., Mayor U., Freund S.M., and Fersht A.R. Solution structure of a protein denatured state and folding intermediate. Nature 437 (2005) 1053-1056
    • (2005) Nature , vol.437 , pp. 1053-1056
    • Religa, T.L.1    Markson, J.S.2    Mayor, U.3    Freund, S.M.4    Fersht, A.R.5
  • 6
    • 0037456298 scopus 로고    scopus 로고
    • The complete folding pathway of a protein from nanoseconds to microseconds
    • Mayor U., Guydosh N.R., Johnson C.M., Grossmann J.G., Sato S., Jas G.S., et al. The complete folding pathway of a protein from nanoseconds to microseconds. Nature 421 (2003) 863-867
    • (2003) Nature , vol.421 , pp. 863-867
    • Mayor, U.1    Guydosh, N.R.2    Johnson, C.M.3    Grossmann, J.G.4    Sato, S.5    Jas, G.S.6
  • 7
    • 0142185492 scopus 로고    scopus 로고
    • The denatured state of engrailed homeodomain under denaturing and native conditions
    • Mayor U., Grossmann J.G., Foster N.W., Freund S.M., and Fersht A.R. The denatured state of engrailed homeodomain under denaturing and native conditions. J. Mol. Biol. 333 (2003) 977-991
    • (2003) J. Mol. Biol. , vol.333 , pp. 977-991
    • Mayor, U.1    Grossmann, J.G.2    Foster, N.W.3    Freund, S.M.4    Fersht, A.R.5
  • 8
    • 0034610360 scopus 로고    scopus 로고
    • Protein folding and unfolding in microseconds to nanoseconds by experiment and simulation
    • Mayor U., Johnson C.M., Daggett V., and Fersht A.R. Protein folding and unfolding in microseconds to nanoseconds by experiment and simulation. Proc. Natl Acad. Sci. USA 97 (2000) 13518-13522
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 13518-13522
    • Mayor, U.1    Johnson, C.M.2    Daggett, V.3    Fersht, A.R.4
  • 9
    • 20544462511 scopus 로고    scopus 로고
    • Simulation and experiment conspire to reveal cryptic intermediates and a slide from nucleation-condensation to framework mechanism of folding
    • White G.W.N., Gianni S., Grossmann J.G., Jemth P., Fersht A.R., and Daggett V. Simulation and experiment conspire to reveal cryptic intermediates and a slide from nucleation-condensation to framework mechanism of folding. J. Mol. Biol. 350 (2005) 757-775
    • (2005) J. Mol. Biol. , vol.350 , pp. 757-775
    • White, G.W.N.1    Gianni, S.2    Grossmann, J.G.3    Jemth, P.4    Fersht, A.R.5    Daggett, V.6
  • 10
    • 52049104954 scopus 로고    scopus 로고
    • Conservation of transition state structure in fast folding peripheral subunit-binding domains
    • Sharpe T.D., Ferguson N., Johnson C.M., and Fersht A.R. Conservation of transition state structure in fast folding peripheral subunit-binding domains. J. Mol. Biol. 383 (2008) 224-237
    • (2008) J. Mol. Biol. , vol.383 , pp. 224-237
    • Sharpe, T.D.1    Ferguson, N.2    Johnson, C.M.3    Fersht, A.R.4
  • 11
  • 12
    • 14844351260 scopus 로고    scopus 로고
    • Simulation and experiment at high temperatures: ultrafast folding of a thermophilic protein by nucleation-condensation
    • Ferguson N., Day R., Johnson C.M., Allen M.D., Daggett V., and Fersht A.R. Simulation and experiment at high temperatures: ultrafast folding of a thermophilic protein by nucleation-condensation. J. Mol. Biol. 347 (2005) 855-870
    • (2005) J. Mol. Biol. , vol.347 , pp. 855-870
    • Ferguson, N.1    Day, R.2    Johnson, C.M.3    Allen, M.D.4    Daggett, V.5    Fersht, A.R.6
  • 13
    • 33745899026 scopus 로고    scopus 로고
    • The folding pathway of spectrin R17 from experiment and simulation: using experimentally validated MD simulations to characterize states hinted at by experiment
    • Scott K.A., Randles L.G., Moran S.J., Daggett V., and Clarke J. The folding pathway of spectrin R17 from experiment and simulation: using experimentally validated MD simulations to characterize states hinted at by experiment. J. Mol. Biol. 359 (2006) 159-173
    • (2006) J. Mol. Biol. , vol.359 , pp. 159-173
    • Scott, K.A.1    Randles, L.G.2    Moran, S.J.3    Daggett, V.4    Clarke, J.5
  • 14
    • 22444436625 scopus 로고    scopus 로고
    • Spectrin R16: broad energy barrier or sequential transition states?
    • Scott K.A., and Clarke J. Spectrin R16: broad energy barrier or sequential transition states?. Protein Sci. 14 (2005) 1617-1629
    • (2005) Protein Sci. , vol.14 , pp. 1617-1629
    • Scott, K.A.1    Clarke, J.2
  • 15
    • 7044222120 scopus 로고    scopus 로고
    • The folding of spectrin domains II: phi-value analysis of R16
    • Scott K.A., Randles L.G., and Clarke J. The folding of spectrin domains II: phi-value analysis of R16. J. Mol. Biol. 344 (2004) 207-221
    • (2004) J. Mol. Biol. , vol.344 , pp. 207-221
    • Scott, K.A.1    Randles, L.G.2    Clarke, J.3
  • 16
    • 7044226061 scopus 로고    scopus 로고
    • The folding of spectrin domains I: wild-type domains have the same stability but very different kinetic properties
    • Scott K.A., Batey S., Hooton K.A., and Clarke J. The folding of spectrin domains I: wild-type domains have the same stability but very different kinetic properties. J. Mol. Biol. 344 (2004) 195-205
    • (2004) J. Mol. Biol. , vol.344 , pp. 195-205
    • Scott, K.A.1    Batey, S.2    Hooton, K.A.3    Clarke, J.4
  • 17
    • 1242319561 scopus 로고    scopus 로고
    • Stabilities of folding of clustered, two-repeat fragments of spectrin reveal a potential hinge in the human erythroid spectrin tetramer
    • MacDonald R.I., and Cummings J.A. Stabilities of folding of clustered, two-repeat fragments of spectrin reveal a potential hinge in the human erythroid spectrin tetramer. Proc. Natl Acad. Sci. USA 101 (2004) 1502-1507
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 1502-1507
    • MacDonald, R.I.1    Cummings, J.A.2
  • 18
    • 7444232111 scopus 로고    scopus 로고
    • Independent movement, dimerization and stability of tandem repeats of chicken brain alpha-spectrin
    • Kusunoki H., Minasov G., Macdonald R.I., and Mondragon A. Independent movement, dimerization and stability of tandem repeats of chicken brain alpha-spectrin. J. Mol. Biol. 344 (2004) 495-511
    • (2004) J. Mol. Biol. , vol.344 , pp. 495-511
    • Kusunoki, H.1    Minasov, G.2    Macdonald, R.I.3    Mondragon, A.4
  • 19
    • 0035799317 scopus 로고    scopus 로고
    • Free energies of urea and of thermal unfolding show that two tandem repeats of spectrin are thermodynamically more stable than a single repeat
    • Macdonald R.I., and Pozharski E.V. Free energies of urea and of thermal unfolding show that two tandem repeats of spectrin are thermodynamically more stable than a single repeat. Biochemistry 40 (2001) 3974-3984
    • (2001) Biochemistry , vol.40 , pp. 3974-3984
    • Macdonald, R.I.1    Pozharski, E.V.2
  • 20
    • 0031592935 scopus 로고    scopus 로고
    • Solution structure of the spectrin repeat: a left-handed antiparallel triple-helical coiled-coil
    • Pascual J., Pfuhl M., Walther D., Saraste M., and Nilges M. Solution structure of the spectrin repeat: a left-handed antiparallel triple-helical coiled-coil. J. Mol. Biol. 273 (1997) 740-751
    • (1997) J. Mol. Biol. , vol.273 , pp. 740-751
    • Pascual, J.1    Pfuhl, M.2    Walther, D.3    Saraste, M.4    Nilges, M.5
  • 21
    • 0029863942 scopus 로고    scopus 로고
    • The spectrin repeat folds into a three-helix bundle in solution
    • Pascual J., Pfuhl M., Rivas G., Pastore A., and Saraste M. The spectrin repeat folds into a three-helix bundle in solution. FEBS Lett. 383 (1996) 201-207
    • (1996) FEBS Lett. , vol.383 , pp. 201-207
    • Pascual, J.1    Pfuhl, M.2    Rivas, G.3    Pastore, A.4    Saraste, M.5
  • 24
    • 0021272595 scopus 로고
    • Erythrocyte spectrin is comprised of many homologous triple helical segments
    • Speicher D.W., and Marchesi V.T. Erythrocyte spectrin is comprised of many homologous triple helical segments. Nature 311 (1984) 177-180
    • (1984) Nature , vol.311 , pp. 177-180
    • Speicher, D.W.1    Marchesi, V.T.2
  • 25
    • 0033200251 scopus 로고    scopus 로고
    • Folding studies of immunoglobulin-like beta-sandwich proteins suggest that they share a common folding pathway
    • Clarke J., Cota E., Fowler S.B., and Hamill S.J. Folding studies of immunoglobulin-like beta-sandwich proteins suggest that they share a common folding pathway. Struct. Fold. Des. 7 (1999) 1145-1153
    • (1999) Struct. Fold. Des. , vol.7 , pp. 1145-1153
    • Clarke, J.1    Cota, E.2    Fowler, S.B.3    Hamill, S.J.4
  • 26
    • 0036304229 scopus 로고    scopus 로고
    • Titin; a multidomain protein that behaves as the sum of its parts
    • Scott K.A., Steward A., Fowler S.B., and Clarke J. Titin; a multidomain protein that behaves as the sum of its parts. J. Mol. Biol. 315 (2002) 819-829
    • (2002) J. Mol. Biol. , vol.315 , pp. 819-829
    • Scott, K.A.1    Steward, A.2    Fowler, S.B.3    Clarke, J.4
  • 27
    • 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. Contact order, transition state placement and the refolding rates of single domain proteins. J. Mol. Biol. 277 (1998) 985-994
    • (1998) J. Mol. Biol. , vol.277 , pp. 985-994
    • Plaxco, K.W.1    Simons, K.T.2    Baker, D.3
  • 28
    • 35648931551 scopus 로고    scopus 로고
    • On the role of structural class of a protein with two-state folding kinetics in determining correlations between its size, topology, and folding rate
    • Istomin A.Y., Jacobs D.J., and Livesay D.R. On the role of structural class of a protein with two-state folding kinetics in determining correlations between its size, topology, and folding rate. Protein Sci. 16 (2007) 2564-2569
    • (2007) Protein Sci. , vol.16 , pp. 2564-2569
    • Istomin, A.Y.1    Jacobs, D.J.2    Livesay, D.R.3
  • 29
    • 0035967862 scopus 로고    scopus 로고
    • Comparison between long-range interactions and contact order in determining the folding rate of two-state proteins: application of long-range order to folding rate prediction
    • Gromiha M.M., and Selvaraj S. Comparison between long-range interactions and contact order in determining the folding rate of two-state proteins: application of long-range order to folding rate prediction. J. Mol. Biol. 310 (2001) 27-32
    • (2001) J. Mol. Biol. , vol.310 , pp. 27-32
    • Gromiha, M.M.1    Selvaraj, S.2
  • 31
    • 0029041315 scopus 로고
    • Exploring the energy surface of protein folding by structure-reactivity relationships and engineered proteins: observation of Hammond behavior for the gross structure of the transition state and anti-Hammond behavior for structural elements for unfolding/folding of barnase
    • Matthews J.M., and Fersht A.R. Exploring the energy surface of protein folding by structure-reactivity relationships and engineered proteins: observation of Hammond behavior for the gross structure of the transition state and anti-Hammond behavior for structural elements for unfolding/folding of barnase. Biochemistry 34 (1995) 6805-6814
    • (1995) Biochemistry , vol.34 , pp. 6805-6814
    • Matthews, J.M.1    Fersht, A.R.2
  • 32
    • 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) 266-280
    • (1986) Methods Enzymol. , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 33
    • 2542599277 scopus 로고    scopus 로고
    • Phi-value analysis and the nature of protein-folding transition states
    • Fersht A.R., and Sato S. Phi-value analysis and the nature of protein-folding transition states. Proc. Natl Acad. Sci. USA 101 (2004) 7976-7981
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 7976-7981
    • Fersht, A.R.1    Sato, S.2
  • 34
    • 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
    • Munoz V., and 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
    • Munoz, V.1    Serrano, L.2
  • 35
    • 0028873081 scopus 로고
    • Elucidating the folding problem of helical peptides using empirical parameters: II. Helix macrodipole effects and rational modification of the helical content of natural peptides
    • Munoz V., and Serrano L. Elucidating the folding problem of helical peptides using empirical parameters: II. Helix macrodipole effects and rational modification of the helical content of natural peptides. J. Mol. Biol. 245 (1995) 275-296
    • (1995) J. Mol. Biol. , vol.245 , pp. 275-296
    • Munoz, V.1    Serrano, L.2
  • 36
    • 0028834210 scopus 로고
    • Elucidating the folding problem of helical peptides using empirical parameters: III. Temperature and pH dependence
    • Munoz V., and Serrano L. Elucidating the folding problem of helical peptides using empirical parameters: III. Temperature and pH dependence. J. Mol. Biol. 245 (1995) 297-308
    • (1995) J. Mol. Biol. , vol.245 , pp. 297-308
    • Munoz, V.1    Serrano, L.2
  • 37
    • 0032553332 scopus 로고    scopus 로고
    • Elucidating the folding problem of alpha-helices: local motifs, long-range electrostatics, ionic-strength dependence and prediction of NMR parameters
    • Lacroix E., Viguera A.R., and Serrano L. Elucidating the folding problem of alpha-helices: local motifs, long-range electrostatics, ionic-strength dependence and prediction of NMR parameters. J. Mol. Biol. 284 (1998) 173-191
    • (1998) J. Mol. Biol. , vol.284 , pp. 173-191
    • Lacroix, E.1    Viguera, A.R.2    Serrano, L.3
  • 39
    • 0037423705 scopus 로고    scopus 로고
    • Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins
    • Friel C.T., Capaldi A.P., and Radford S.E. Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326 (2003) 293-305
    • (2003) J. Mol. Biol. , vol.326 , pp. 293-305
    • Friel, C.T.1    Capaldi, A.P.2    Radford, S.E.3
  • 41
    • 0030478947 scopus 로고    scopus 로고
    • A small engineered protein lacks structural uniqueness by increasing the side-chain conformational entropy
    • Furukawa K., Oda M., and Nakamura H. A small engineered protein lacks structural uniqueness by increasing the side-chain conformational entropy. Proc. Natl Acad. Sci. USA 93 (1996) 13583-13588
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 13583-13588
    • Furukawa, K.1    Oda, M.2    Nakamura, H.3
  • 42
    • 0032529088 scopus 로고    scopus 로고
    • Solution structure of the DNA-binding domain of human telomeric protein, hTRF1
    • Nishikawa T., Nagadoi A., Yoshimura S., Aimoto S., and Nishimura Y. Solution structure of the DNA-binding domain of human telomeric protein, hTRF1. Structure 6 (1998) 1057-1065
    • (1998) Structure , vol.6 , pp. 1057-1065
    • Nishikawa, T.1    Nagadoi, A.2    Yoshimura, S.3    Aimoto, S.4    Nishimura, Y.5
  • 43
    • 2342449128 scopus 로고    scopus 로고
    • Testing protein-folding simulations by experiment: B domain of protein A
    • Sato S., Religa T.L., Daggett V., and Fersht A.R. Testing protein-folding simulations by experiment: B domain of protein A. Proc. Natl Acad. Sci. USA 101 (2004) 6952-6956
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 6952-6956
    • Sato, S.1    Religa, T.L.2    Daggett, V.3    Fersht, A.R.4
  • 44
    • 0030593468 scopus 로고    scopus 로고
    • Over-production of proteins in Escherichia coli: mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels
    • Miroux B., and Walker J.E. Over-production of proteins in Escherichia coli: mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels. J. Mol. Biol. 260 (1996) 289-298
    • (1996) J. Mol. Biol. , vol.260 , pp. 289-298
    • Miroux, B.1    Walker, J.E.2


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