메뉴 건너뛰기




Volumn 365, Issue 3, 2007, Pages 870-880

The Folding Pathway of T4 Lysozyme: The High-resolution Structure and Folding of a Hidden Intermediate

Author keywords

hidden intermediate; hydrogen exchange; intermediate structure; protein folding; T4 lysozyme

Indexed keywords

APOCYTOCHROME B562; CYTOCHROME B; HYDROGEN; LYSOZYME; T4 LYSOZYME;

EID: 33845622937     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.10.047     Document Type: Article
Times cited : (32)

References (35)
  • 1
    • 0002006297 scopus 로고
    • Are there pathways for protein folding?
    • Levinthal C. Are there pathways for protein folding?. J. Chim. Phys. 65 (1968) 44-45
    • (1968) J. Chim. Phys. , vol.65 , pp. 44-45
    • Levinthal, C.1
  • 2
    • 0015597839 scopus 로고
    • Nucleation, rapid folding, and globular intrachain regions in proteins
    • Wetlaufer D.B. Nucleation, rapid folding, and globular intrachain regions in proteins. Proc. Natl Acad. Sci. USA 70 (1973) 697-701
    • (1973) Proc. Natl Acad. Sci. USA , vol.70 , pp. 697-701
    • Wetlaufer, D.B.1
  • 3
    • 30144440755 scopus 로고    scopus 로고
    • Energy barriers, cooperativity, and hidden intermediates in the folding of small proteins
    • Bai Y. Energy barriers, cooperativity, and hidden intermediates in the folding of small proteins. Biochem. Biophys. Res. Commun. 340 (2006) 976-983
    • (2006) Biochem. Biophys. Res. Commun. , vol.340 , pp. 976-983
    • Bai, Y.1
  • 4
    • 0242318402 scopus 로고    scopus 로고
    • Specific non-native hydrophobic interactions in a hidden folding intermediate: implications for protein folding
    • Feng H., Takei J., Lipsitz R., Tjandra N., and Bai Y. Specific non-native hydrophobic interactions in a hidden folding intermediate: implications for protein folding. Biochemistry 42 (2003) 12461-12465
    • (2003) Biochemistry , vol.42 , pp. 12461-12465
    • Feng, H.1    Takei, J.2    Lipsitz, R.3    Tjandra, N.4    Bai, Y.5
  • 5
    • 6344291152 scopus 로고    scopus 로고
    • 562: native fold with non-native hydrophobic interactions
    • 562: native fold with non-native hydrophobic interactions. J. Mol. Biol. 343 (2004) 1477-1485
    • (2004) J. Mol. Biol. , vol.343 , pp. 1477-1485
    • Feng, H.1    Vu, N.D.2    Bai, Y.3
  • 6
    • 17044438189 scopus 로고    scopus 로고
    • A protein folding pathway with multiple folding intermediates at atomic resolution
    • Feng H., Zhou Z., and Bai Y. A protein folding pathway with multiple folding intermediates at atomic resolution. Proc. Natl Acad. Sci. USA 102 (2005) 5026-5031
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 5026-5031
    • Feng, H.1    Zhou, Z.2    Bai, Y.3
  • 7
    • 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
  • 8
    • 0037172787 scopus 로고    scopus 로고
    • Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein
    • Chu R., Pei W., Takei J., and Bai Y. Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry 41 (2002) 7998-8003
    • (2002) Biochemistry , vol.41 , pp. 7998-8003
    • Chu, R.1    Pei, W.2    Takei, J.3    Bai, Y.4
  • 9
    • 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
  • 10
    • 0026742164 scopus 로고
    • Detection and characterization of an early folding intermediate of T4 lysozyme using pulsed hydrogen exchange and two-dimensional NMR
    • Lu J., and Dahlquist F.W. Detection and characterization of an early folding intermediate of T4 lysozyme using pulsed hydrogen exchange and two-dimensional NMR. Biochemistry 31 (1992) 4749-4756
    • (1992) Biochemistry , vol.31 , pp. 4749-4756
    • Lu, J.1    Dahlquist, F.W.2
  • 11
    • 0028968018 scopus 로고
    • Studies on protein stability with T4 lysozyme
    • Matthews B.W. Studies on protein stability with T4 lysozyme. Advan. Protein Chem. 46 (1995) 249-278
    • (1995) Advan. Protein Chem. , vol.46 , pp. 249-278
    • Matthews, B.W.1
  • 12
    • 0030045089 scopus 로고    scopus 로고
    • Structural and genetic analysis of the folding and function of T4 lysozyme
    • Matthews B.W. Structural and genetic analysis of the folding and function of T4 lysozyme. FASEB J. 10 (1996) 35-41
    • (1996) FASEB J. , vol.10 , pp. 35-41
    • Matthews, B.W.1
  • 13
    • 0033517740 scopus 로고    scopus 로고
    • Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding
    • Gassner N.C., Baase W.A., Lindstrom J.D., Lu J., Dahlquist F.W., and Matthews B.W. Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. Biochemistry 38 (1999) 14451-14460
    • (1999) Biochemistry , vol.38 , pp. 14451-14460
    • Gassner, N.C.1    Baase, W.A.2    Lindstrom, J.D.3    Lu, J.4    Dahlquist, F.W.5    Matthews, B.W.6
  • 14
    • 0842347938 scopus 로고    scopus 로고
    • Relocation or duplication of the helix A sequence of T4 lysozyme causes only modest changes in structure but can increase or decrease the rate of folding
    • Sagermann M., Baase W.A., Mooers B.H., Gay L., and Matthews B.W. Relocation or duplication of the helix A sequence of T4 lysozyme causes only modest changes in structure but can increase or decrease the rate of folding. Biochemistry 43 (2004) 1296-1301
    • (2004) Biochemistry , vol.43 , pp. 1296-1301
    • Sagermann, M.1    Baase, W.A.2    Mooers, B.H.3    Gay, L.4    Matthews, B.W.5
  • 16
    • 33845796109 scopus 로고    scopus 로고
    • The folding pathway of T4 lysozyme: an on-pathway hidden folding intermediate
    • doi:10.1016/j.jmb.2006.10.048
    • Kato H., Vu N.D., Feng H., Zhou Z., and Bai Y. The folding pathway of T4 lysozyme: an on-pathway hidden folding intermediate. J. Mol. Biol. (2006) doi:10.1016/j.jmb.2006.10.048
    • (2006) J. Mol. Biol.
    • Kato, H.1    Vu, N.D.2    Feng, H.3    Zhou, Z.4    Bai, Y.5
  • 17
    • 0037108164 scopus 로고    scopus 로고
    • Populating partially unfolded forms by hydrogen exchange-directed protein engineering
    • Takei J., Pei W., Vu D., and Bai Y. Populating partially unfolded forms by hydrogen exchange-directed protein engineering. Biochemistry 41 (2002) 12308-12312
    • (2002) Biochemistry , vol.41 , pp. 12308-12312
    • Takei, J.1    Pei, W.2    Vu, D.3    Bai, Y.4
  • 18
    • 24644435356 scopus 로고    scopus 로고
    • An on-pathway hidden intermediate and the early rate-limiting transition state of Rd-apocytochrome b562 characterized by protein engineering
    • Zhou Z., Huang Y., and Bai Y. An on-pathway hidden intermediate and the early rate-limiting transition state of Rd-apocytochrome b562 characterized by protein engineering. J. Mol. Biol. 352 (2005) 757-764
    • (2005) J. Mol. Biol. , vol.352 , pp. 757-764
    • Zhou, Z.1    Huang, Y.2    Bai, Y.3
  • 19
    • 30444450687 scopus 로고    scopus 로고
    • Determination of an ensemble of structures representing the intermediate state of the bacterial immunity protein Im7
    • Gsponer J., Hopearuoho H., Whittaker S.B., Spence G.R., Moore G.R., Paci E., et al. Determination of an ensemble of structures representing the intermediate state of the bacterial immunity protein Im7. Proc. Natl Acad. Sci. USA 103 (2006) 99-104
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 99-104
    • Gsponer, J.1    Hopearuoho, H.2    Whittaker, S.B.3    Spence, G.R.4    Moore, G.R.5    Paci, E.6
  • 20
    • 0029940033 scopus 로고    scopus 로고
    • Molecular collapse: the rate-limiting step in two-state cytochrome c folding
    • Sosnick T.R., Mayne L., and Englander S.W. Molecular collapse: the rate-limiting step in two-state cytochrome c folding. Proteins: Struct. Funct. Genet. 24 (1996) 413-426
    • (1996) Proteins: Struct. Funct. Genet. , vol.24 , pp. 413-426
    • Sosnick, T.R.1    Mayne, L.2    Englander, S.W.3
  • 21
    • 4243155782 scopus 로고    scopus 로고
    • NMR characterization of the dynamics of biomacromolecules
    • Palmer III A.G. NMR characterization of the dynamics of biomacromolecules. Chem. Rev. 104 (2004) 3623-3640
    • (2004) Chem. Rev. , vol.104 , pp. 3623-3640
    • Palmer III, A.G.1
  • 22
    • 0031891493 scopus 로고    scopus 로고
    • Subdomain interactions as a determinant in the folding and stability of T4 lysozyme
    • Llinas M., and Marqusee S. Subdomain interactions as a determinant in the folding and stability of T4 lysozyme. Protein Sci. 7 (1998) 96-104
    • (1998) Protein Sci. , vol.7 , pp. 96-104
    • Llinas, M.1    Marqusee, S.2
  • 24
    • 0029643523 scopus 로고
    • Protein folding intermediates: native-state hydrogen exchange
    • Bai Y., Sosnick T.R., Mayne L., and Englander S.W. Protein folding intermediates: native-state hydrogen exchange. Science 269 (1995) 192-197
    • (1995) Science , vol.269 , pp. 192-197
    • Bai, Y.1    Sosnick, T.R.2    Mayne, L.3    Englander, S.W.4
  • 25
    • 0023358977 scopus 로고
    • Mutant sequences as probes of protein folding mechanisms
    • Matthews C.R., and Hurle M.R. Mutant sequences as probes of protein folding mechanisms. Bioessays 6 (1987) 254-257
    • (1987) Bioessays , vol.6 , pp. 254-257
    • Matthews, C.R.1    Hurle, M.R.2
  • 26
    • 0026511656 scopus 로고
    • The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding
    • Fersht A.R., Matouschek A., and Serrano L. The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding. J. Mol. Biol. 224 (1992) 771-782
    • (1992) J. Mol. Biol. , vol.224 , pp. 771-782
    • Fersht, A.R.1    Matouschek, A.2    Serrano, L.3
  • 27
    • 33644847698 scopus 로고    scopus 로고
    • The evolution of spliceosomal introns: patterns, puzzles and progress
    • Roy S.W., and Gilbert W. The evolution of spliceosomal introns: patterns, puzzles and progress. Nature Rev. Genet. 7 (2006) 211-221
    • (2006) Nature Rev. Genet. , vol.7 , pp. 211-221
    • Roy, S.W.1    Gilbert, W.2
  • 28
    • 0034730144 scopus 로고    scopus 로고
    • Novel folded protein domains generated by combinatorial shuffling of polypeptide segments
    • Riechmann L., and Winter G. Novel folded protein domains generated by combinatorial shuffling of polypeptide segments. Proc. Natl Acad. Sci. USA 97 (2000) 10068-10073
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 10068-10073
    • Riechmann, L.1    Winter, G.2
  • 29
    • 0031565728 scopus 로고    scopus 로고
    • The foldon universe: a survey of structural similarity and self-recognition of independently folding units
    • Panchenko A.R., Luthey-Schulten Z., Cole R., and Wolynes P.G. The foldon universe: a survey of structural similarity and self-recognition of independently folding units. J. Mol. Biol. 272 (1997) 95-105
    • (1997) J. Mol. Biol. , vol.272 , pp. 95-105
    • Panchenko, A.R.1    Luthey-Schulten, Z.2    Cole, R.3    Wolynes, P.G.4
  • 30
    • 12344311123 scopus 로고    scopus 로고
    • Detection of a hidden folding intermediate of the third domain of PDZ
    • Feng H., Vu N.D., and Bai Y. Detection of a hidden folding intermediate of the third domain of PDZ. J. Mol. Biol. 346 (2005) 345-353
    • (2005) J. Mol. Biol. , vol.346 , pp. 345-353
    • Feng, H.1    Vu, N.D.2    Bai, Y.3
  • 32
    • 0027169515 scopus 로고
    • Main-chain bond lengths and bond angles in protein structures
    • Laskowski R.A., Moss D.S., and Thornton J.M. Main-chain bond lengths and bond angles in protein structures. J. Mol. Biol. 231 (1993) 1049-1067
    • (1993) J. Mol. Biol. , vol.231 , pp. 1049-1067
    • Laskowski, R.A.1    Moss, D.S.2    Thornton, J.M.3
  • 34
    • 0034048847 scopus 로고    scopus 로고
    • Efficient analysis of macromolecular rotational diffusion from heteronuclear relaxation data
    • Dosset P., Hus J.C., Blackledge M., and Marion D. Efficient analysis of macromolecular rotational diffusion from heteronuclear relaxation data. J. Biomol. NMR 16 (2000) 23-28
    • (2000) J. Biomol. NMR , vol.16 , pp. 23-28
    • Dosset, P.1    Hus, J.C.2    Blackledge, M.3    Marion, D.4
  • 35
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: a program for display and analysis of macromolecular structures
    • Koradi R., Billeter M., and Wuthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14 (1996) 51-32
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-32
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.