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Volumn 90, Issue 6, 2006, Pages 2120-2130

Complex folding kinetics of a multidomain protein

Author keywords

[No Author keywords available]

Indexed keywords

MUTANT PROTEIN; PROTEIN; SPECTRIN;

EID: 33646000631     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.105.072710     Document Type: Article
Times cited : (55)

References (33)
  • 3
    • 0021272595 scopus 로고
    • Erythrocyte spectrin is comprised of many homologous triple helical segments
    • Speicher, D. W., and V. T. Marchesi. 1984. Erythrocyte spectrin is comprised of many homologous triple helical segments. Nature. 311:177-180.
    • (1984) Nature , vol.311 , pp. 177-180
    • Speicher, D.W.1    Marchesi, V.T.2
  • 5
    • 0029863942 scopus 로고    scopus 로고
    • The spectrin repeat folds into a three-helix bundle in solution
    • Pascual, J., M. Pfuhl, G. Rivas, A. Pastore, and M. Saraste. 1996. The spectrin repeat folds into a three-helix bundle in solution. FEBS Lett. 383:201-207.
    • (1996) FEBS Lett. , vol.383 , pp. 201-207
    • Pascual, J.1    Pfuhl, M.2    Rivas, G.3    Pastore, A.4    Saraste, M.5
  • 6
    • 0031592935 scopus 로고    scopus 로고
    • Solution structure of the spectrin repeat: A left-handed antiparallel triple-helical coiled-coil
    • Pascual, J., M. Pfuhl, D. Walther, M. Saraste, and M. Nilges. 1997. Solution structure of the spectrin repeat: a left-handed antiparallel triple-helical coiled-coil. J. Mol. Biol. 273:740-751.
    • (1997) J. Mol. Biol. , vol.273 , pp. 740-751
    • Pascual, J.1    Pfuhl, M.2    Walther, D.3    Saraste, M.4    Nilges, M.5
  • 7
    • 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 E. V. Pozharski. 2001. Free energies of urea and of thermal unfolding show that two tandem repeats of spectrin are thermodynamically more stable than a single repeat. Biochemistry. 40:3974-3984.
    • (2001) Biochemistry , vol.40 , pp. 3974-3984
    • Macdonald, R.I.1    Pozharski, E.V.2
  • 8
    • 0034933167 scopus 로고    scopus 로고
    • Crystal structure of the alpha-actinin rod reveals an extensive torsional twist
    • Ylanne, J., K. Scheffzek, P. Young, and M. Saraste. 2001. Crystal structure of the alpha-actinin rod reveals an extensive torsional twist. Structure 9:597-604.
    • (2001) Structure , vol.9 , pp. 597-604
    • Ylanne, J.1    Scheffzek, K.2    Young, P.3    Saraste, M.4
  • 9
    • 0033588274 scopus 로고    scopus 로고
    • Structures of two repeats of spectrin suggest models of flexibility
    • Grum, V. L., D. Li, R. I. Macdonald, and A. Mondragon. 1999. Structures of two repeats of spectrin suggest models of flexibility. Cell. 98:523-535.
    • (1999) Cell , vol.98 , pp. 523-535
    • Grum, V.L.1    Li, D.2    Macdonald, R.I.3    Mondragon, A.4
  • 10
    • 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 J. A. Cummings. 2004. 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. 101:1502-1507.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 1502-1507
    • MacDonald, R.I.1    Cummings, J.A.2
  • 11
    • 22444436625 scopus 로고    scopus 로고
    • 16: Broad energy barrier or sequential transition states?
    • 16: broad energy barrier or sequential transition states? Protein Sci. 14:1617-1629.
    • (2005) Protein Sci. , vol.14 , pp. 1617-1629
    • Scott, K.A.1    Clarke, J.2
  • 12
    • 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., S. Batey, K. A. Hooton, and J. Clarke. 2004. The folding of spectrin domains I: wild-type domains have the same stability but very different kinetic properties. J. Mol. Biol. 344:195-205.
    • (2004) J. Mol. Biol. , vol.344 , pp. 195-205
    • Scott, K.A.1    Batey, S.2    Hooton, K.A.3    Clarke, J.4
  • 13
    • 20344406783 scopus 로고    scopus 로고
    • Cooperative folding in a multi-domain protein
    • Batey, S., L. G. Randles, A. Steward, and J. Clarke. 2005. Cooperative folding in a multi-domain protein. J. Mol. Biol. 349:1045-1059.
    • (2005) J. Mol. Biol. , vol.349 , pp. 1045-1059
    • Batey, S.1    Randles, L.G.2    Steward, A.3    Clarke, J.4
  • 15
    • 0002203625 scopus 로고    scopus 로고
    • Kinetic models in protein folding
    • R. H. Pain, editor. Oxford University Press, Oxford
    • Bieri, O., and T. Kiefhaber. 2000. Kinetic models in protein folding. In Mechanisms of Protein Folding, 2nd ed. R. H. Pain, editor. Oxford University Press, Oxford. 34-64.
    • (2000) Mechanisms of Protein Folding, 2nd Ed. , pp. 34-64
    • Bieri, O.1    Kiefhaber, T.2
  • 17
    • 0030844281 scopus 로고    scopus 로고
    • Recombination of protein domains facilitated by co-translational folding in eukaryotes
    • Netzer, W. J., and F. U. Hartl. 1997. Recombination of protein domains facilitated by co-translational folding in eukaryotes. Nature. 388:343-349.
    • (1997) Nature , vol.388 , pp. 343-349
    • Netzer, W.J.1    Hartl, F.U.2
  • 19
    • 0033582763 scopus 로고    scopus 로고
    • Single molecule force spectroscopy of spectrin repeats: Low unfolding forces in helix bundles
    • Rief, M., J. Pascual, M. Saraste, and H. E. Gaub. 1999. Single molecule force spectroscopy of spectrin repeats: low unfolding forces in helix bundles. J. Mol. Biol. 286:553-561.
    • (1999) J. Mol. Biol. , vol.286 , pp. 553-561
    • Rief, M.1    Pascual, J.2    Saraste, M.3    Gaub, H.E.4
  • 20
    • 0242353807 scopus 로고    scopus 로고
    • Pathway shifts and thermal softening in temperature-coupled forced unfolding of spectrin domains
    • Law, R., G. Liao, S. Harper, G. Yang, D. W. Speicher, and D. E. Discher. 2003. Pathway shifts and thermal softening in temperature-coupled forced unfolding of spectrin domains. Biophys. J. 85:3286-3293.
    • (2003) Biophys. J. , vol.85 , pp. 3286-3293
    • Law, R.1    Liao, G.2    Harper, S.3    Yang, G.4    Speicher, D.W.5    Discher, D.E.6
  • 21
    • 20544465799 scopus 로고    scopus 로고
    • Mechanical unfolding of TNfn3: The unfolding pathway of a fnIII domain probed by protein engineering, AFM and MD simulation
    • Ng, S. P., R. W. Rounsevell, A. Steward, C. D. Geierhaas, P. M. Williams, E. Paci, and J. Clarke. 2005. Mechanical unfolding of TNfn3: the unfolding pathway of a fnIII domain probed by protein engineering, AFM and MD simulation. J. Mol. Biol. 350:776-789.
    • (2005) J. Mol. Biol. , vol.350 , pp. 776-789
    • Ng, S.P.1    Rounsevell, R.W.2    Steward, A.3    Geierhaas, C.D.4    Williams, P.M.5    Paci, E.6    Clarke, J.7
  • 22
    • 0042744701 scopus 로고    scopus 로고
    • Mechanical unfolding of a titin Ig domain: Structure of transition state revealed by combining atomic force microscopy, protein engineering and molecular dynamics simulations
    • Best, R. B., S. B. Fowler, J. L. Herrera, A. Steward, E. Paci, and J. Clarke. 2003. Mechanical unfolding of a titin Ig domain: structure of transition state revealed by combining atomic force microscopy, protein engineering and molecular dynamics simulations. J. Mol. Biol. 330:867-877.
    • (2003) J. Mol. Biol. , vol.330 , pp. 867-877
    • Best, R.B.1    Fowler, S.B.2    Herrera, J.L.3    Steward, A.4    Paci, E.5    Clarke, J.6
  • 23
    • 0034804341 scopus 로고    scopus 로고
    • Can non-mechanical proteins withstand force? Stretching barnase by atomic force microscopy and molecular dynamics simulation
    • Best, R. B., B. Li, A. Steward, V. Daggett, and J. Clarke. 2001. Can non-mechanical proteins withstand force? Stretching barnase by atomic force microscopy and molecular dynamics simulation. Biophys. J. 81:2344-2356.
    • (2001) Biophys. J. , vol.81 , pp. 2344-2356
    • Best, R.B.1    Li, B.2    Steward, A.3    Daggett, V.4    Clarke, J.5
  • 24
    • 19444372522 scopus 로고    scopus 로고
    • The remarkable mechanical strength of polycystin-1 supports a direct role in mechanotransduction
    • Forman, J. R., S. Qamar, E. Paci, R. N. Sandford, and J. Clarke. 2005. The remarkable mechanical strength of polycystin-1 supports a direct role in mechanotransduction. J. Mol. Biol. 349:861-871.
    • (2005) J. Mol. Biol. , vol.349 , pp. 861-871
    • Forman, J.R.1    Qamar, S.2    Paci, E.3    Sandford, R.N.4    Clarke, J.5
  • 25
    • 0034612284 scopus 로고    scopus 로고
    • Unfolding proteins by external forces and temperature: The importance of topology and energetics
    • Paci, E., and M. Karplus. 2000. Unfolding proteins by external forces and temperature: the importance of topology and energetics. Proc. Natl. Acad. Sci. USA. 97:6521-6526.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6521-6526
    • Paci, E.1    Karplus, M.2
  • 26
    • 0034874601 scopus 로고    scopus 로고
    • Stability and folding rates of domains spanning the large A-band super-repeat of titin
    • Head, J. G., A. Houmeida, P. J. Knight, A. R. Clarke, J. Trinick, and R. L. Brady. 2001. Stability and folding rates of domains spanning the large A-band super-repeat of titin. Biophys. J. 81:1570-1579.
    • (2001) Biophys. J. , vol.81 , pp. 1570-1579
    • Head, J.G.1    Houmeida, A.2    Knight, P.J.3    Clarke, A.R.4    Trinick, J.5    Brady, R.L.6
  • 27
    • 0036304229 scopus 로고    scopus 로고
    • Titin; a multidomain protein that behaves as the sum of its parts
    • Scott, K. A., A. Steward, S. B. Fowler, and J. Clarke. 2002. Titin; a multidomain protein that behaves as the sum of its parts. J. Mol. Biol. 315:819-829.
    • (2002) J. Mol. Biol. , vol.315 , pp. 819-829
    • Scott, K.A.1    Steward, A.2    Fowler, S.B.3    Clarke, J.4
  • 28
    • 17344384932 scopus 로고    scopus 로고
    • Fast folding of the two-domain semliki forest virus capsid protein explains co-translational proteolytic activity
    • Sanchez, I. E., M. Morillas, E. Zobeley, T. Kiefhaber, and R. Glockshuber. 2004. Fast folding of the two-domain semliki forest virus capsid protein explains co-translational proteolytic activity. J. Mol. Biol. 338:159-167.
    • (2004) J. Mol. Biol. , vol.338 , pp. 159-167
    • Sanchez, I.E.1    Morillas, M.2    Zobeley, E.3    Kiefhaber, T.4    Glockshuber, R.5
  • 31
    • 0037954112 scopus 로고    scopus 로고
    • The folding mechanism of a twodomain protein: Folding kinetics and domain docking of the gene-3 protein of phage fd
    • Martin, A., and F. X. Schmid. 2003. The folding mechanism of a twodomain protein: folding kinetics and domain docking of the gene-3 protein of phage fd. J. Mol. Biol. 329:599-610.
    • (2003) J. Mol. Biol. , vol.329 , pp. 599-610
    • Martin, A.1    Schmid, F.X.2
  • 32
    • 0025339471 scopus 로고
    • Folding of an all-beta protein: Independent domain folding in gamma II-crystallin from calf eye lens
    • Rudolph, R., R. Siebendritt, G. Nesslauer, A. K. Sharma, and R. Jaenicke. 1990. Folding of an all-beta protein: independent domain folding in gamma II-crystallin from calf eye lens. Proc. Natl. Acad. Sci. USA. 87:4625-4629.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4625-4629
    • Rudolph, R.1    Siebendritt, R.2    Nesslauer, G.3    Sharma, A.K.4    Jaenicke, R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.