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Volumn 89, Issue 5, 2005, Pages 3353-3361

Folding of the protein domain hbSBD

Author keywords

[No Author keywords available]

Indexed keywords

2 OXOACID DEHYDROGENASE; UREA;

EID: 27744548865     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.105.065151     Document Type: Article
Times cited : (30)

References (45)
  • 1
    • 0037221599 scopus 로고    scopus 로고
    • Is there a unifying mechanism for protein folding?
    • Daggett, V., and A. R. Fersht. 2003. Is there a unifying mechanism for protein folding? Trends Biochem. Sci. 28:18-25.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 18-25
    • Daggett, V.1    Fersht, A.R.2
  • 2
    • 0031815749 scopus 로고    scopus 로고
    • How do small single domain proteins fold?
    • Jackson, S. E. 1998. How do small single domain proteins fold? Fold. Des. 3:R81-R91.
    • (1998) Fold. Des. , vol.3
    • Jackson, S.E.1
  • 4
    • 0028947257 scopus 로고
    • Funnels, pathways, and the energy landscape of protein folding: A synthesis
    • Bryngelson, J., J. N. Onuchic, N. D. Socci, and P. G. Wolynes. 1995. Funnels, pathways, and the energy landscape of protein folding: a synthesis. Proteins. 21:167-195.
    • (1995) Proteins , vol.21 , pp. 167-195
    • Bryngelson, J.1    Onuchic, J.N.2    Socci, N.D.3    Wolynes, P.G.4
  • 6
    • 3242677702 scopus 로고    scopus 로고
    • A simple thermodynamic test to discriminate between two-state and downhill folding
    • Oliva, F. Y., and V. Munoz. 2004. A simple thermodynamic test to discriminate between two-state and downhill folding. J. Am. Chem. Soc. 126:8596-8597.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 8596-8597
    • Oliva, F.Y.1    Munoz, V.2
  • 8
    • 0002977005 scopus 로고    scopus 로고
    • Maple syrup urine disease (branched-chain ketoaciduria)
    • C. R. Scriver, A. L. Beaudet, W. S. Sly, D. Valle, B. Vogelstein, and B. Childs, editors. McGraw-Hill, New York, NY.
    • Chuang, D. T., and V. E. Shih. 2001. Maple syrup urine disease (branched-chain ketoaciduria). in The Metabolic and Molecular Basis of Inherited Disease. C. R. Scriver, A. L. Beaudet, W. S. Sly, D. Valle, B. Vogelstein, and B. Childs, editors. McGraw-Hill, New York, NY. 1971-2006.
    • (2001) The Metabolic and Molecular Basis of Inherited Disease , pp. 1971-2006
    • Chuang, D.T.1    Shih, V.E.2
  • 9
    • 0033790516 scopus 로고    scopus 로고
    • Swinging arms and swinging domains in multifunctional enzymes: Catalytic machines for multistep reactions
    • Perham, R. N. 2000. Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions. Ann. Rev. Biochem. 69:961-1004.
    • (2000) Ann. Rev. Biochem. , vol.69 , pp. 961-1004
    • Perham, R.N.1
  • 10
    • 85030733403 scopus 로고    scopus 로고
    • Reference deleted in proof
    • Reference deleted in proof.
  • 11
    • 0020972782 scopus 로고
    • Theoretical studies of protein folding
    • Go, N. 1983. Theoretical studies of protein folding. Annu. Rev. Biophys. Bioeng. 12:183-210.
    • (1983) Annu. Rev. Biophys. Bioeng. , vol.12 , pp. 183-210
    • Go, N.1
  • 12
    • 0034685604 scopus 로고    scopus 로고
    • Topological and energetic factors: What determines the structural details of the transition state ensemble and "en-route" intermediates for protein folding? An investigation for small globular proteins
    • Clementi, C., H. Nymeyer, and J. Onuchic. 2000. Topological and energetic factors: what determines the structural details of the transition state ensemble and "en-route" intermediates for protein folding? An investigation for small globular proteins. J. Mol. Biol. 298: 937-953.
    • (2000) J. Mol. Biol. , vol.298 , pp. 937-953
    • Clementi, C.1    Nymeyer, H.2    Onuchic, J.3
  • 13
    • 0032742688 scopus 로고    scopus 로고
    • Go-ing for the prediction of protein folding mechanisms
    • Takada, S. 1999. Go-ing for the prediction of protein folding mechanisms. Proc. Natl. Acad. Sci. USA. 96:11698-11700.
    • (1999) Proc. Natl. Acad. Sci. USA. , vol.96 , pp. 11698-11700
    • Takada, S.1
  • 14
    • 0035850732 scopus 로고    scopus 로고
    • Roles of native topology and chain-length scaling in protein folding: A simulation study with a Go-like model
    • Koga, N., and S. Takaga. 2001. Roles of native topology and chain-length scaling in protein folding: a simulation study with a Go-like model. J. Mol. Biol. 313:171-180.
    • (2001) J. Mol. Biol. , vol.313 , pp. 171-180
    • Koga, N.1    Takaga, S.2
  • 15
    • 33646987405 scopus 로고
    • Optimized Monte-Carlo data analysis
    • Ferrenberg, A. M., and R. H. Swendsen. 1989. Optimized Monte-Carlo data analysis. Phys. Rev. Lett. 63:1195-1198.
    • (1989) Phys. Rev. Lett. , vol.63 , pp. 1195-1198
    • Ferrenberg, A.M.1    Swendsen, R.H.2
  • 16
    • 0001504441 scopus 로고    scopus 로고
    • Cooperativity in protein folding: From lattice models with sidechains to real proteins
    • Klimov, D. K., and D. Thirumalai. 1998. Cooperativity in protein folding: from lattice models with sidechains to real proteins. Fold. Des. 3:127-139.
    • (1998) Fold. Des. , vol.3 , pp. 127-139
    • Klimov, D.K.1    Thirumalai, D.2
  • 17
    • 14644442376 scopus 로고    scopus 로고
    • Finite size effects on calorimetric cooperativity of two-state proteins
    • Li, M. S., D. K. Klimov, and D. Thirumalai. 2005. Finite size effects on calorimetric cooperativity of two-state proteins. Physica A. 350: 38-44.
    • (2005) Physica A , vol.350 , pp. 38-44
    • Li, M.S.1    Klimov, D.K.2    Thirumalai, D.3
  • 18
    • 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
  • 19
    • 0023442217 scopus 로고
    • Protein stability curves
    • Becktel, W. J., and J. A. Schellman. 1987. Protein stability curves. Biopolymers. 26:1859-1877.
    • (1987) Biopolymers , vol.26 , pp. 1859-1877
    • Becktel, W.J.1    Schellman, J.A.2
  • 21
    • 0027318781 scopus 로고
    • Kinetics and thermodynamics of folding in model proteins
    • Camacho, C. J., and D. Thirumalai. 1993. Kinetics and thermodynamics of folding in model proteins. Proc. Natl. Acad. Sci. USA. 90:6369-6372.
    • (1993) Proc. Natl. Acad. Sci. USA. , vol.90 , pp. 6369-6372
    • Camacho, C.J.1    Thirumalai, D.2
  • 23
    • 0000399469 scopus 로고    scopus 로고
    • Viscosity dependence of the folding rates of proteins
    • Klimov, D. K., and D. Thirumalai. 1997. Viscosity dependence of the folding rates of proteins. Phys. Rev. Lett. 79:317-320.
    • (1997) Phys. Rev. Lett. , vol.79 , pp. 317-320
    • Klimov, D.K.1    Thirumalai, D.2
  • 24
    • 0030624384 scopus 로고    scopus 로고
    • Protein folding kinetics: Time scales, pathways and energy landscapes in terms of sequence dependent properties
    • Veitshans, T., D. K. Klimov, and D. Thirumalai. 1997. Protein folding kinetics: time scales, pathways and energy landscapes in terms of sequence dependent properties. Fold. Des. 2:1-22.
    • (1997) Fold. Des. , vol.2 , pp. 1-22
    • Veitshans, T.1    Klimov, D.K.2    Thirumalai, D.3
  • 25
    • 36749110571 scopus 로고
    • Computer simulation method for the calculation of equilibrium constants for the formation of physical clusters and molecules: Application to small water clusters
    • Swope, W. C., H. C. Andersen, P. H. Berens, and K. R. Wilson. 1982. Computer simulation method for the calculation of equilibrium constants for the formation of physical clusters and molecules: application to small water clusters. J. Chem. Phys. 76:637-649.
    • (1982) J. Chem. Phys. , vol.76 , pp. 637-649
    • Swope, W.C.1    Andersen, H.C.2    Berens, P.H.3    Wilson, K.R.4
  • 26
    • 0037163881 scopus 로고    scopus 로고
    • Folding kinetics of the lipoic acid-bearing domain of human mitochondrial branched chain alpha-ketoacid dehydrogenase complex
    • Naik, M., Y.-C. Chang, and T.-H. Huang. 2002. Folding kinetics of the lipoic acid-bearing domain of human mitochondrial branched chain alpha-ketoacid dehydrogenase complex. FEBS Lett. 530:133-138.
    • (2002) FEBS Lett , vol.530 , pp. 133-138
    • Naik, M.1    Chang, Y.-C.2    Huang, T.-H.3
  • 27
    • 4344622456 scopus 로고    scopus 로고
    • Conformational stability and thermodynamic characterization of the lipoic acid bearing domain of human mitochondrial branched chain alpha-ketoacid dehydrogenase
    • Naik, M., and T.-H. Huang. 2004. Conformational stability and thermodynamic characterization of the lipoic acid bearing domain of human mitochondrial branched chain alpha-ketoacid dehydrogenase. Protein Sci. 13:2483-2492.
    • (2004) Protein Sci , vol.13 , pp. 2483-2492
    • Naik, M.1    Huang, T.-H.2
  • 28
    • 0037013207 scopus 로고    scopus 로고
    • Solution structure and dynamics of the lipoic acid-bearing domain of human mitochondrial branched-chain alpha-keto acid dehydrogenase complex
    • Chang, C.-F., H.-T. Chou, J. L. Chuang, D. T. Chuang, and T.-H. Huang. 2002. Solution structure and dynamics of the lipoic acid-bearing domain of human mitochondrial branched-chain alpha-keto acid dehydrogenase complex. J. Biochem. (Tokyo). 277:15865-15873.
    • (2002) J. Biochem. (Tokyo) , vol.277 , pp. 15865-15873
    • Chang, C.-F.1    Chou, H.-T.2    Chuang, J.L.3    Chuang, D.T.4    Huang, T.-H.5
  • 29
    • 4243572706 scopus 로고    scopus 로고
    • Criterion that determines the foldability of proteins
    • Klimov, D. K., and D. Thirumalai. 1996. Criterion that determines the foldability of proteins. Phys. Rev. Lett. 76:4070-4073.
    • (1996) Phys. Rev. Lett. , vol.76 , pp. 4070-4073
    • Klimov, D.K.1    Thirumalai, D.2
  • 30
    • 3943113660 scopus 로고    scopus 로고
    • Using protein folding rates to test protein folding theories
    • Gillepse, B., and K. W. Plaxco. 2004. Using protein folding rates to test protein folding theories. Annu. Rev. Biochem. 73:837-859.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 837-859
    • Gillepse, B.1    Plaxco, K.W.2
  • 31
    • 0347123330 scopus 로고    scopus 로고
    • Thermal denaturation and folding rates of single domain proteins: Size matters
    • Li, M. S., D. K. Klimov, and D. Thirumalai. 2004. Thermal denaturation and folding rates of single domain proteins: size matters. Polym. 45:573-579.
    • (2004) Polym , vol.45 , pp. 573-579
    • Li, M.S.1    Klimov, D.K.2    Thirumalai, D.3
  • 32
    • 42749106226 scopus 로고    scopus 로고
    • Finite size effects on thermal denaturation of globular proteins
    • Li, M. S., D. K. Klimov, and D. Thirumalai. 2004. Finite size effects on thermal denaturation of globular proteins. Phys. Rev. Lett. 93:268107.
    • (2004) Phys. Rev. Lett. , vol.93 , pp. 268107
    • Li, M.S.1    Klimov, D.K.2    Thirumalai, D.3
  • 33
    • 0034310589 scopus 로고    scopus 로고
    • Energetic components of cooperative protein folding
    • Kaya, H., and H. S. Chan. 2000. Energetic components of cooperative protein folding. Phys. Rev. Lett. 85:4823-4826.
    • (2000) Phys. Rev. Lett. , vol.85 , pp. 4823-4826
    • Kaya, H.1    Chan, H.S.2
  • 34
    • 1542319916 scopus 로고    scopus 로고
    • Cooperativity principles in protein folding
    • Chan, H. S., S. Shimizu, and H. Kaya. 2004. Cooperativity principles in protein folding. Methods Enzymol. 380:350-379.
    • (2004) Methods Enzymol , vol.380 , pp. 350-379
    • Chan, H.S.1    Shimizu, S.2    Kaya, H.3
  • 35
    • 0032568599 scopus 로고    scopus 로고
    • Folding funnels and frustration in off-lattice minimalist protein landscapes
    • Nymeyer, H., A. E. Garcia, and J. N. Onuchic. 1998. Folding funnels and frustration in off-lattice minimalist protein landscapes. Proc. Natl. Acad. Sci. USA. 95:5921-5926.
    • (1998) Proc. Natl. Acad. Sci. USA. , vol.95 , pp. 5921-5926
    • Nymeyer, H.1    Garcia, A.E.2    Onuchic, J.N.3
  • 36
    • 1942473645 scopus 로고    scopus 로고
    • Critical nucleation size in the folding of small apparently two-state proteins
    • Bai, Y., Y. Zhou, and H. Zhou. 2004. Critical nucleation size in the folding of small apparently two-state proteins. Protein Sci. 13:1173-1181.
    • (2004) Protein Sci , vol.13 , pp. 1173-1181
    • Bai, Y.1    Zhou, Y.2    Zhou, H.3
  • 37
    • 85030726574 scopus 로고    scopus 로고
    • Reference deleted in proof
    • Reference deleted in proof.
  • 38
    • 27744438232 scopus 로고    scopus 로고
    • Deciphering the timescales and mechanisms of protein folding using minimal off-lattice models
    • Klimov, D. K., and D. Thirumalai. 1999. Deciphering the timescales and mechanisms of protein folding using minimal off-lattice models. Curr. Opin. Struct. Biol. 97:97-107.
    • (1999) Curr. Opin. Struct. Biol. , vol.97 , pp. 97-107
    • Klimov, D.K.1    Thirumalai, D.2
  • 39
    • 3342929355 scopus 로고    scopus 로고
    • Investigating protein folding, misfolding and nonnative states: Experimental and theoretical methods
    • Academic Press, San Diego, CA
    • Greene, L. H. ed. (2004). Investigating Protein Folding, Misfolding and Nonnative States: Experimental and Theoretical Methods. Methods 34. Academic Press, San Diego, CA.
    • (2004) Methods , vol.34
    • Greene, L.H.1
  • 40
    • 16244419001 scopus 로고    scopus 로고
    • Elucidation of the protein folding landscape by NMR
    • Dyson, H. J., and P. E. Wright. 2005. Elucidation of the protein folding landscape by NMR. Methods Enzymol. 394:299-321.
    • (2005) Methods Enzymol , vol.394 , pp. 299-321
    • Dyson, H.J.1    Wright, P.E.2
  • 42
    • 85030734847 scopus 로고    scopus 로고
    • Reference deleted in proof
    • Reference deleted in proof.
  • 43
    • 0035451468 scopus 로고    scopus 로고
    • Multicanonical parallel simulations of proteins with continuous potentials
    • Hayryan, S., C.-K. Hu, S.-Y. Hu, and R. J. Shang. 2001. Multicanonical parallel simulations of proteins with continuous potentials. J. Comput. Chem. 22:1287-1296.
    • (2001) J. Comput. Chem. , vol.22 , pp. 1287-1296
    • Hayryan, S.1    Hu, C.-K.2    Hu, S.-Y.3    Shang, R.J.4
  • 44
    • 14744271380 scopus 로고    scopus 로고
    • A new analytical method for calculating the solvent accessible surface area of macromolecules and its gradients
    • Hayryan, S., C.-K. Hu, J. Skvrivanek, E. Hayryan, and I. Pokomy. 2005. A new analytical method for calculating the solvent accessible surface area of macromolecules and its gradients. J. Comput. Chem. 26:334-343.
    • (2005) J. Comput. Chem. , vol.26 , pp. 334-343
    • Hayryan, S.1    Hu, C.-K.2    Skvrivanek, J.3    Hayryan, E.4    Pokomy, I.5
  • 45


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