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Volumn 109, Issue 44, 2012, Pages 17772-17776

Folding pathways of proteins with increasing degree of sequence identities but different structure and function

Author keywords

Kinetics; Protein engineering; Protein folding; Protein G

Indexed keywords

SUBTILISIN;

EID: 84868122220     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1201794109     Document Type: Article
Times cited : (24)

References (36)
  • 1
    • 58049200632 scopus 로고    scopus 로고
    • Comparison of successive transition states for folding reveals alternative early folding pathways of two homologous proteins
    • Calosci N, et al. (2008) Comparison of successive transition states for folding reveals alternative early folding pathways of two homologous proteins. Proc Natl Acad Sci USA 105:19241-19246.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 19241-19246
    • Calosci, N.1
  • 2
    • 33847712992 scopus 로고    scopus 로고
    • A conserved folding mechanism for PDZ domains
    • Chi CN, et al. (2007) A conserved folding mechanism for PDZ domains. FEBS Lett 581:1109-1113.
    • (2007) FEBS Lett , vol.581 , pp. 1109-1113
    • Chi, C.N.1
  • 3
    • 0033200251 scopus 로고    scopus 로고
    • Folding studies of Ig-like beta-sandwich proteins suggest they share a common folding pathway
    • Clarke J, Cota E, Fowler SB, Hamill SJ (1999) Folding studies of Ig-like beta-sandwich proteins suggest they share a common folding pathway. Structure 7:1145-1153.
    • (1999) Structure , vol.7 , pp. 1145-1153
    • Clarke, J.1    Cota, E.2    Fowler, S.B.3    Hamill, S.J.4
  • 4
    • 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 CT, Capaldi AP, Radford SE (2003) 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 36:293-305.
    • (2003) J Mol Biol , vol.36 , pp. 293-305
    • Friel, C.T.1    Capaldi, A.P.2    Radford, S.E.3
  • 5
    • 0032750509 scopus 로고    scopus 로고
    • The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved
    • Martínez JC, Serrano L (1999) The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat Struct Biol 6:1010-1016.
    • (1999) Nat Struct Biol , vol.6 , pp. 1010-1016
    • Martínez, J.C.1    Serrano, L.2
  • 6
    • 0032734515 scopus 로고    scopus 로고
    • Experiment and theory highlight role of native state topology in SH3 folding
    • Riddle DS, et al. (1999) Experiment and theory highlight role of native state topology in SH3 folding. Nat Struct Biol 6:1016-1024.
    • (1999) Nat Struct Biol , vol.6 , pp. 1016-1024
    • Riddle, D.S.1
  • 8
    • 0142135083 scopus 로고    scopus 로고
    • Exploring the cytochrome c folding mechanism: Cytochrome c552 from Thermus thermophilus folds through an on-pathway intermediate
    • Travaglini-Allocatelli C, et al. (2003) Exploring the cytochrome c folding mechanism: Cytochrome c552 from Thermus thermophilus folds through an on-pathway intermediate. J Biol Chem 278:41136-41140.
    • (2003) J Biol Chem , vol.278 , pp. 41136-41140
    • Travaglini-Allocatelli, C.1
  • 10
    • 13844299144 scopus 로고    scopus 로고
    • The family feud: Do proteins with similar structures fold via the same pathway
    • Zarrine-Afsar A, Larson SM, Davidson AR (2005) The family feud: Do proteins with similar structures fold via the same pathway? Curr Opin Struct Biol 15:42-49.
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 42-49
    • Zarrine-Afsar, A.1    Larson, S.M.2    Davidson, A.R.3
  • 11
    • 0034604105 scopus 로고    scopus 로고
    • A surprising simplicity to protein folding
    • Baker D (2000) A surprising simplicity to protein folding. Nature 405:39-42.
    • (2000) Nature , vol.405 , pp. 39-42
    • Baker, D.1
  • 12
    • 34547499110 scopus 로고    scopus 로고
    • The design and characterization of two proteins with 88% sequence identity but different structure and function
    • Alexander PA, et al. (2007) The design and characterization of two proteins with 88% sequence identity but different structure and function. Proc Natl Acad Sci USA 104:11963-11968.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 11963-11968
    • Alexander, P.A.1
  • 13
    • 55749108537 scopus 로고    scopus 로고
    • NMR structures of two designed proteins with high sequence identity but different fold and function
    • He Y, Chen Y, Alexander P, Bryan PN, Orban J (2008) NMR structures of two designed proteins with high sequence identity but different fold and function. Proc Natl Acad Sci USA 105:14412-14417.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 14412-14417
    • He, Y.1    Chen, Y.2    Alexander, P.3    Bryan, P.N.4    Orban, J.5
  • 14
    • 79952805688 scopus 로고    scopus 로고
    • The denatured state dictates the topology of two proteins with almost identical sequence but different native structure and function
    • Morrone A, et al. (2011) The denatured state dictates the topology of two proteins with almost identical sequence but different native structure and function. J Biol Chem 286:3863-3872.
    • (2011) J Biol Chem , vol.286 , pp. 3863-3872
    • Morrone, A.1
  • 15
    • 75849116590 scopus 로고    scopus 로고
    • A minimal sequence code for switching protein structure and function
    • Alexander PA, et al. (2009) A minimal sequence code for switching protein structure and function. Proc Natl Acad Sci USA 106:21149-21154.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 21149-21154
    • Alexander, P.A.1
  • 16
    • 0026511656 scopus 로고
    • The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding
    • Fersht AR, Matouschek A, Serrano L (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
    • Fersht, A.R.1    Matouschek, A.2    Serrano, L.3
  • 17
    • 2542599277 scopus 로고    scopus 로고
    • Phi-value analysis and the nature of protein-folding transition states
    • Fersht AR, Sato S (2004) Phi-value analysis and the nature of protein-folding transition states. Proc Natl Acad Sci USA 101:7976-7981.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 7976-7981
    • Fersht, A.R.1    Sato, S.2
  • 18
    • 40049086810 scopus 로고    scopus 로고
    • Characterisation of transition state structures for protein folding using 'high,' 'medium,' and 'low' {Phi}-values
    • Geierhaas CD, Salvatella X, Clarke J, Vendruscolo M (2008) Characterisation of transition state structures for protein folding using 'high,' 'medium,' and 'low' {Phi}-values. Protein Eng Des Sel 21:215-222.
    • (2008) Protein Eng des Sel , vol.21 , pp. 215-222
    • Geierhaas, C.D.1    Salvatella, X.2    Clarke, J.3    Vendruscolo, M.4
  • 19
    • 78649885501 scopus 로고    scopus 로고
    • Structural characterization of a misfolded intermediate populated during the folding process of a PDZ domain
    • Gianni S, et al. (2010) Structural characterization of a misfolded intermediate populated during the folding process of a PDZ domain. Nat Struct Mol Biol 17:1431-1437.
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 1431-1437
    • Gianni, S.1
  • 20
    • 69049115135 scopus 로고    scopus 로고
    • Engineered symmetric connectivity of secondary structure elements highlights malleability of protein folding pathways
    • Ivarsson Y, Travaglini-Allocatelli C, Brunori M, Gianni S (2009) Engineered symmetric connectivity of secondary structure elements highlights malleability of protein folding pathways. J Am Chem Soc 131:11727-11733.
    • (2009) J Am Chem Soc , vol.131 , pp. 11727-11733
    • Ivarsson, Y.1    Travaglini-Allocatelli, C.2    Brunori, M.3    Gianni, S.4
  • 21
    • 80054705419 scopus 로고    scopus 로고
    • Gb1 is not a two-state folder: Identification and characterization of an on-pathway intermediate
    • Morrone A, et al. (2011) Gb1 is not a two-state folder: Identification and characterization of an on-pathway intermediate. Biophys J 101:1-8.
    • (2011) Biophys J , vol.101 , pp. 1-8
    • Morrone, A.1
  • 22
    • 0028791393 scopus 로고
    • An integrated kinetic analysis of intermediates and transition states in protein folding reactions
    • Parker MJ, Spencer J, Clarke AR (1995) An integrated kinetic analysis of intermediates and transition states in protein folding reactions. J Mol Biol 253:771-786.
    • (1995) J Mol Biol , vol.253 , pp. 771-786
    • Parker, M.J.1    Spencer, J.2    Clarke, A.R.3
  • 23
    • 0030796986 scopus 로고    scopus 로고
    • Three-state model for lysozyme folding: Triangular folding mechanism with an energetically trapped intermediate
    • Wildegger G, Kiefhaber T (1997) Three-state model for lysozyme folding: Triangular folding mechanism with an energetically trapped intermediate. J Mol Biol 270:294-304.
    • (1997) J Mol Biol , vol.270 , pp. 294-304
    • Wildegger, G.1    Kiefhaber, T.2
  • 24
    • 0028024928 scopus 로고
    • Specific nucleus as the transition state for protein folding: Evidence from the lattice model
    • Abkevich VI, Gutin AM, Shakhnovich EI (1994) Specific nucleus as the transition state for protein folding: Evidence from the lattice model. Biochemistry 33:10026-10036.
    • (1994) Biochemistry , vol.33 , pp. 10026-10036
    • Abkevich, V.I.1    Gutin, A.M.2    Shakhnovich, E.I.3
  • 25
    • 0028868995 scopus 로고
    • The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: Evidence for a nucleation-condensation mechanism for protein folding
    • Itzhaki LS, Otzen DE, Fersht AR (1995) The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: Evidence for a nucleation-condensation mechanism for protein folding. J Mol Biol 254:260-288.
    • (1995) J Mol Biol , vol.254 , pp. 260-288
    • Itzhaki, L.S.1    Otzen, D.E.2    Fersht, A.R.3
  • 26
    • 33846916730 scopus 로고    scopus 로고
    • Malleability of protein folding pathways: A simple reason for complex behavior
    • Lindberg MO, Oliveberg M (2007) Malleability of protein folding pathways: A simple reason for complex behavior. Curr Opin Struct Biol 17:21-29.
    • (2007) Curr Opin Struct Biol , vol.17 , pp. 21-29
    • Lindberg, M.O.1    Oliveberg, M.2
  • 27
    • 55549098922 scopus 로고    scopus 로고
    • Changes of protein folding pathways by circular permutation. Overlapping nuclei promote global cooperativity
    • Haglund E, Lindberg MO, OlivebergM (2008) Changes of protein folding pathways by circular permutation. Overlapping nuclei promote global cooperativity. J Biol Chem 283:27904-27915.
    • (2008) J Biol Chem , vol.283 , pp. 27904-27915
    • Haglund, E.1    Lindberg, M.O.2    Olivebergm3
  • 28
    • 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, Serrano L (1997) Development of the multiple sequence approximation within the AGADIR model of alpha-helix formation: Comparison with Zimm-Bragg and Lifson-Roig formalisms. Biopolymers 41:495-509.
    • (1997) Biopolymers , vol.41 , pp. 495-509
    • Munoz, V.1    Serrano, L.2
  • 29
    • 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
  • 30
    • 47749083052 scopus 로고    scopus 로고
    • From the first protein structures to our current knowledge of protein folding: Delights and scepticisms
    • Fersht AR (2008) From the first protein structures to our current knowledge of protein folding: Delights and scepticisms. Nat Rev Mol Cell Biol 9:650-654.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 650-654
    • Fersht, A.R.1
  • 31
    • 33646759974 scopus 로고    scopus 로고
    • Sub-microsecond protein folding
    • Kubelka J, et al. (2006) Sub-microsecond protein folding. J Mol Biol 359:546-553.
    • (2006) J Mol Biol , vol.359 , pp. 546-553
    • Kubelka, J.1
  • 32
    • 0028856785 scopus 로고
    • Optimization of rates of protein folding: The nucleation-condensation mechanism and its implications
    • Fersht AR (1995) Optimization of rates of protein folding: The nucleation-condensation mechanism and its implications. Proc Natl Acad Sci USA 21:10869-10873.
    • (1995) Proc Natl Acad Sci USA , vol.21 , pp. 10869-10873
    • Fersht, A.R.1
  • 33
    • 0038502170 scopus 로고    scopus 로고
    • Folding dynamics and mechanism of beta-hairpin formation
    • Munoz V, Thompson PA, Hofrichter J, Eaton WA(1997) Folding dynamics and mechanism of beta-hairpin formation. Nature 390:196-199.
    • (1997) Nature , vol.390 , pp. 196-199
    • Munoz, V.1    Thompson, P.A.2    Hofrichter, J.3    Eaton, W.A.4
  • 34
    • 8744294716 scopus 로고    scopus 로고
    • Engineering subtilisin into a fluoride-triggered processing protease useful for one-step protein purification
    • Ruan B, et al. (2004) Engineering subtilisin into a fluoride-triggered processing protease useful for one-step protein purification. Biochemistry 43:14539-14546.
    • (2004) Biochemistry , vol.43 , pp. 14539-14546
    • Ruan, B.1
  • 35
    • 0030958760 scopus 로고    scopus 로고
    • Transient aggregates in protein folding are easily mistaken for folding intermediates
    • Silow M, Oliveberg M (1997) Transient aggregates in protein folding are easily mistaken for folding intermediates. Proc Natl Acad Sci USA 94:6084-6086.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 6084-6086
    • Silow, M.1    Oliveberg, M.2
  • 36
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants
    • Santoro MM, Bolen DW (1988) Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants. Biochemistry 27:8063-8068.
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2


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