메뉴 건너뛰기




Volumn 105, Issue 7, 2008, Pages 2397-2402

Cooperative folding kinetics of BBL protein and peripheral subunit-binding domain homologues

Author keywords

Global downhill folding; Protein folding mechanism; Protein thermodynamics; Relaxation kinetics of protein

Indexed keywords

BBL PROTEIN; PERIPHERAL SUBUNIT BINDING DOMAIN PROTEIN; PROTEIN; UNCLASSIFIED DRUG; ESCHERICHIA COLI PROTEIN;

EID: 40649105020     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0708480105     Document Type: Article
Times cited : (26)

References (40)
  • 1
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen CB (1973) Principles that govern the folding of protein chains. Science 181:223-230.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 2
    • 0028929556 scopus 로고
    • Principles of protein folding - A perspective from simple exact models
    • Dill KA, et al. (1995) Principles of protein folding - A perspective from simple exact models. Protein Sci 4:561-602.
    • (1995) Protein Sci , vol.4 , pp. 561-602
    • Dill, K.A.1
  • 3
    • 0037686252 scopus 로고    scopus 로고
    • The present view of the mechanism of protein folding
    • Daggett V, Fersht AR (2003) The present view of the mechanism of protein folding. Nat Rev Mol Cell Biol 4:497-502.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 497-502
    • Daggett, V.1    Fersht, A.R.2
  • 4
    • 33646931471 scopus 로고    scopus 로고
    • Protein folding thermodynamics and dynamics: Where physics, chemistry, and biology meet
    • Shakhnovich EI (2006) Protein folding thermodynamics and dynamics: Where physics, chemistry, and biology meet. Chem Rev 106:1559-1588.
    • (2006) Chem Rev , vol.106 , pp. 1559-1588
    • Shakhnovich, E.I.1
  • 5
    • 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
  • 6
    • 0023449962 scopus 로고
    • Spin glasses and the statistical mechanics of protein folding
    • Bryngelson JD, Wolynes PG (1987) Spin glasses and the statistical mechanics of protein folding. Proc Natl Acad Sci USA 84:7524-7528.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 7524-7528
    • Bryngelson, J.D.1    Wolynes, P.G.2
  • 7
    • 0028947257 scopus 로고
    • Funnels, pathways, and the energy landscape of protein folding: A synthesis
    • Bryngelson JD, Onuchic JN, Socci ND, Wolynes PG (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.D.1    Onuchic, J.N.2    Socci, N.D.3    Wolynes, P.G.4
  • 8
    • 0024357911 scopus 로고
    • Formation of unique structure in polypeptide chains. Theoretical investigation with the aid of a replica approach
    • Shakhnovich EI, Gutin AM (1989) Formation of unique structure in polypeptide chains. Theoretical investigation with the aid of a replica approach. Biophys Chem 34:187-199.
    • (1989) Biophys Chem , vol.34 , pp. 187-199
    • Shakhnovich, E.I.1    Gutin, A.M.2
  • 9
    • 0026511656 scopus 로고
    • The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding
    • Matouschek A, Serrano L, Fersht AR (1992) The folding of an enzyme. I. 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
    • Matouschek, A.1    Serrano, L.2    Fersht, A.R.3
  • 10
    • 0029155772 scopus 로고
    • Impact of local and non-local interactions on thermodynamics and kinetics of protein folding
    • Abkevich VI, Gutin AM, Shakhnovich EI (1995) Impact of local and non-local interactions on thermodynamics and kinetics of protein folding. J Mol Biol 252:460-471.
    • (1995) J Mol Biol , vol.252 , pp. 460-471
    • Abkevich, V.I.1    Gutin, A.M.2    Shakhnovich, E.I.3
  • 11
    • 0033060613 scopus 로고    scopus 로고
    • Searching for "downhill scenarios" in protein folding
    • Eaton WA (1999) Searching for "downhill scenarios" in protein folding. Proc Natl Acad Sci USA 96:5897-5899.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 5897-5899
    • Eaton, W.A.1
  • 12
    • 0037111966 scopus 로고    scopus 로고
    • Thermodynamics and kinetics of downhill protein folding investigated with a simple statistical mechanical model
    • Muñoz V (2002) Thermodynamics and kinetics of downhill protein folding investigated with a simple statistical mechanical model. Int J Quantum Chem 90:1522-1528.
    • (2002) Int J Quantum Chem , vol.90 , pp. 1522-1528
    • Muñoz, V.1
  • 14
    • 3242677702 scopus 로고    scopus 로고
    • A simple thermodynamic test to discriminate between two-state and downhill folding
    • Oliva FY, Muñoz VA (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    Muñoz, V.A.2
  • 16
    • 25144462746 scopus 로고    scopus 로고
    • Ultra-fast barrier-limited folding in the peripheral subunit-binding domain family
    • Ferguson, N et al. (2005) Ultra-fast barrier-limited folding in the peripheral subunit-binding domain family. J Mol Biol 353:427-446.
    • (2005) J Mol Biol , vol.353 , pp. 427-446
    • Ferguson, N.1
  • 17
    • 0037154277 scopus 로고    scopus 로고
    • Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum
    • Fitz-Gibbon ST, et al. (2002) Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum. Proc Natl Acad Sci USA 99:984-989.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 984-989
    • Fitz-Gibbon, S.T.1
  • 18
    • 18844421130 scopus 로고    scopus 로고
    • Robustness of downhill folding: Guidelines for the analysis of equilibrium folding experiments on small proteins
    • Naganathan AN, Perez-Jimenez R, Sanchez-Ruiz JM, Muñoz V (2005) Robustness of downhill folding: Guidelines for the analysis of equilibrium folding experiments on small proteins. Biochemistry 44:7435-7449.
    • (2005) Biochemistry , vol.44 , pp. 7435-7449
    • Naganathan, A.N.1    Perez-Jimenez, R.2    Sanchez-Ruiz, J.M.3    Muñoz, V.4
  • 19
    • 33746102627 scopus 로고    scopus 로고
    • Atom-by-atom analysis of global downhill protein folding
    • Sadqi M, Fushman D, Muñoz V (2006) Atom-by-atom analysis of global downhill protein folding. Nature 442:317-321.
    • (2006) Nature , vol.442 , pp. 317-321
    • Sadqi, M.1    Fushman, D.2    Muñoz, V.3
  • 21
    • 33847097289 scopus 로고    scopus 로고
    • Analysis of protein-folding cooperativity
    • Zhou Z, Bai Y (2007) Analysis of protein-folding cooperativity. Nature 445:E16-E17.
    • (2007) Nature , vol.445
    • Zhou, Z.1    Bai, Y.2
  • 22
    • 33847120702 scopus 로고    scopus 로고
    • Sadqi M, Fushman D, Muñoz V (2007) Sadqi et al. reply. Nature 445:E17-E18.
    • Sadqi M, Fushman D, Muñoz V (2007) Sadqi et al. reply. Nature 445:E17-E18.
  • 23
    • 11144223201 scopus 로고    scopus 로고
    • Exploring protein-folding ensembles: A variable-barrier model for the analysis of equilibrium unfolding experiments
    • Muñoz V, Sanchez-Ruiz JM (2004) Exploring protein-folding ensembles: A variable-barrier model for the analysis of equilibrium unfolding experiments. Proc Natl Acad Sci USA 101:17646-17651.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 17646-17651
    • Muñoz, V.1    Sanchez-Ruiz, J.M.2
  • 24
  • 25
    • 33746325516 scopus 로고    scopus 로고
    • Proteins downhill all the way
    • Kelly JW (2006) Proteins downhill all the way. Nature 442:255-256.
    • (2006) Nature , vol.442 , pp. 255-256
    • Kelly, J.W.1
  • 26
    • 0033613165 scopus 로고    scopus 로고
    • A simple model for calculating the kinetics of protein folding from three-dimensional structures
    • Muñoz V, Eaton WA (1999) A simple model for calculating the kinetics of protein folding from three-dimensional structures. Proc Natl Acad Sci USA 96:11311-11316.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 11311-11316
    • Muñoz, V.1    Eaton, W.A.2
  • 27
    • 8644232696 scopus 로고    scopus 로고
    • Combinatorial modeling of protein folding kinetics: Free energy profiles and rates
    • Henry ER, Eaton WA (2004) Combinatorial modeling of protein folding kinetics: Free energy profiles and rates. Chem Phys 307:163-185.
    • (2004) Chem Phys , vol.307 , pp. 163-185
    • Henry, E.R.1    Eaton, W.A.2
  • 28
    • 42049109634 scopus 로고    scopus 로고
    • Case DA, et al. (2004) AMBER 8 (Univ of California, San Francisco).
    • Case DA, et al. (2004) AMBER 8 (Univ of California, San Francisco).
  • 29
    • 0037166875 scopus 로고    scopus 로고
    • Exact solution of the Muñoz-Eaton model for protein folding
    • Bruscolini P, Pelizzola A (2002) Exact solution of the Muñoz-Eaton model for protein folding. Phys Rev Lett 88:258101.
    • (2002) Phys Rev Lett , vol.88 , pp. 258101
    • Bruscolini, P.1    Pelizzola, A.2
  • 30
    • 4344572930 scopus 로고    scopus 로고
    • What can one learn from experiments about the elusive transition state?
    • Chang I, Cieplak M, Banavar JR, Maritan A (2004) What can one learn from experiments about the elusive transition state? Protein Sci 13:2446-2457.
    • (2004) Protein Sci , vol.13 , pp. 2446-2457
    • Chang, I.1    Cieplak, M.2    Banavar, J.R.3    Maritan, A.4
  • 34
    • 0027318781 scopus 로고
    • Kinetics and thermodynamics of folding in model proteins
    • Camacho CJ, Thirumalai D (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
  • 35
    • 0031047914 scopus 로고    scopus 로고
    • Submillisecond protein folding kinetics studied by ultrarapid mixing
    • Chan CK, et al. (1997) Submillisecond protein folding kinetics studied by ultrarapid mixing. Proc Natl Acad Sci USA 94:1779-1784.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 1779-1784
    • Chan, C.K.1
  • 36
    • 0001229818 scopus 로고    scopus 로고
    • Temperature dependence of the folding rate in a simple protein model: Search for a glass transition
    • Gutin A, Sali A, Abkevich V, Karplus M, Shakhnovich E (1998) Temperature dependence of the folding rate in a simple protein model: Search for a glass transition. Chem Phys 108:6466-6483.
    • (1998) Chem Phys , vol.108 , pp. 6466-6483
    • Gutin, A.1    Sali, A.2    Abkevich, V.3    Karplus, M.4    Shakhnovich, E.5
  • 37
    • 27744500841 scopus 로고    scopus 로고
    • Solvation and desolvation effects in protein folding: Native flexibility, kinetic cooperativity and enthalpic barriers under isostability conditions
    • Liu Z, Chan HS (2005) Solvation and desolvation effects in protein folding: Native flexibility, kinetic cooperativity and enthalpic barriers under isostability conditions. Phys Biol 2:S75-S85.
    • (2005) Phys Biol , vol.2
    • Liu, Z.1    Chan, H.S.2
  • 38
    • 0034284060 scopus 로고    scopus 로고
    • Polymer principles of protein calorimetric two-state cooperativity
    • Kaya H, Chan HS (2000) Polymer principles of protein calorimetric two-state cooperativity. Proteins 40:637-661.
    • (2000) Proteins , vol.40 , pp. 637-661
    • Kaya, H.1    Chan, H.S.2
  • 39
    • 0034112774 scopus 로고    scopus 로고
    • Kinetics, thermodynamics and evolution of non-native interactions in a protein folding nucleus
    • Li L, Mirny LA, Shakhnovich EI (2000) Kinetics, thermodynamics and evolution of non-native interactions in a protein folding nucleus. Nat Struct Biol 7:336-342.
    • (2000) Nat Struct Biol , vol.7 , pp. 336-342
    • Li, L.1    Mirny, L.A.2    Shakhnovich, E.I.3
  • 40
    • 0035370662 scopus 로고    scopus 로고
    • Multiple protein folding nuclei and the transition state ensemble in two-state proteins
    • Klimov DK, Thirumalai D (2001) Multiple protein folding nuclei and the transition state ensemble in two-state proteins. Proteins 43:465-475.
    • (2001) Proteins , vol.43 , pp. 465-475
    • Klimov, D.K.1    Thirumalai, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.