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Volumn 47, Issue 7, 2008, Pages 2064-2070

Probing the kinetic cooperativity of β-sheet folding perpendicular to the strand direction

Author keywords

[No Author keywords available]

Indexed keywords

ENERGY BARRIERS; FREE ENERGY; MELTING POINT; REACTION KINETICS; RELAXATION PROCESSES;

EID: 39649104098     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi702195c     Document Type: Article
Times cited : (13)

References (68)
  • 1
    • 0028947257 scopus 로고
    • Funnels, pathways, and the energy landscape of protein-folding - A synthesis
    • Bryngelson, J. D., Onuchic, J. N., Socci, N. D., and Wolynes, P. G. (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
  • 2
    • 0003166498 scopus 로고    scopus 로고
    • Protein folding in the landscape perspective: Chevron plots and non-Arrhenius kinetics
    • Chan, H. S., and Dill, K. A. (1998) Protein folding in the landscape perspective: Chevron plots and non-Arrhenius kinetics, Proteins 30, 2-33.
    • (1998) Proteins , vol.30 , pp. 2-33
    • Chan, H.S.1    Dill, K.A.2
  • 3
    • 0037686252 scopus 로고    scopus 로고
    • The present view of the mechanism of protein folding
    • Daggett, V., and Fersht, A. (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.2
  • 4
    • 33846917230 scopus 로고    scopus 로고
    • Ultrafast and downhill protein folding
    • Dyer, R. B. (2007) Ultrafast and downhill protein folding, Curr. Opin. Struct. Biol. 17, 38-47.
    • (2007) Curr. Opin. Struct. Biol , vol.17 , pp. 38-47
    • Dyer, R.B.1
  • 6
    • 0030593029 scopus 로고    scopus 로고
    • Design of a monomeric 23-residue polypeptide with defined tertiary structure
    • Struthers, M. D., Cheng, R. P., and Imperiali, B. (1996) Design of a monomeric 23-residue polypeptide with defined tertiary structure, Science 271, 342-345.
    • (1996) Science , vol.271 , pp. 342-345
    • Struthers, M.D.1    Cheng, R.P.2    Imperiali, B.3
  • 9
    • 0036405903 scopus 로고    scopus 로고
    • Redesign of a four-helix bundle protein by phage display coupled with proteolysis and structural characterization by NMR and X-ray crystallography
    • Chu, R., Takei, J., Knowlton, J. R., Andrykovitch, M., Pei, W. H., Kajava, A. V., Steinbach, P. J., Ji, X. H., and Bai, Y. W. (2002) Redesign of a four-helix bundle protein by phage display coupled with proteolysis and structural characterization by NMR and X-ray crystallography, J. Mol. Biol. 323, 253-262.
    • (2002) J. Mol. Biol , vol.323 , pp. 253-262
    • Chu, R.1    Takei, J.2    Knowlton, J.R.3    Andrykovitch, M.4    Pei, W.H.5    Kajava, A.V.6    Steinbach, P.J.7    Ji, X.H.8    Bai, Y.W.9
  • 10
    • 0041530316 scopus 로고    scopus 로고
    • NMR and temperature-jump measurements of de novo designed proteins demonstrate rapid folding in the absence of explicit selection for kinetics
    • Gillespie, B., Vu, D. M., Shah, P. S., Marshall, S. A., Dyer, R. B., Mayo, S. L., and Plaxco, K. W. (2003) NMR and temperature-jump measurements of de novo designed proteins demonstrate rapid folding in the absence of explicit selection for kinetics, J. Mol. Biol. 220, 813-819.
    • (2003) J. Mol. Biol , vol.220 , pp. 813-819
    • Gillespie, B.1    Vu, D.M.2    Shah, P.S.3    Marshall, S.A.4    Dyer, R.B.5    Mayo, S.L.6    Plaxco, K.W.7
  • 13
    • 13444302392 scopus 로고    scopus 로고
    • Computational de novo design and characterization of a four-helix bundle protein that selectively binds a nonbiological cofactor
    • Cochran, F. V., Wu, S. P., Wang, W., Nanda, V., Saven, J. G., Therien, M. J., and DeGrado, W. F. (2005) Computational de novo design and characterization of a four-helix bundle protein that selectively binds a nonbiological cofactor, J. Am. Chem. Soc. 127, 1346-1347.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 1346-1347
    • Cochran, F.V.1    Wu, S.P.2    Wang, W.3    Nanda, V.4    Saven, J.G.5    Therien, M.J.6    DeGrado, W.F.7
  • 14
    • 24344464777 scopus 로고    scopus 로고
    • Engineering beta-sheet protein toward the folding speed limit
    • Nguyen, H., Jäger, M., Kelly, J. W., and Gruebele, M. (2005) Engineering beta-sheet protein toward the folding speed limit, J. Phys. Chem. B 109, 15182-15186.
    • (2005) J. Phys. Chem. B , vol.109 , pp. 15182-15186
    • Nguyen, H.1    Jäger, M.2    Kelly, J.W.3    Gruebele, M.4
  • 15
    • 33644880010 scopus 로고    scopus 로고
    • Ultrafast folding of a computationally designed Trp-cage mutant: Trp(2)-cage
    • Bunagan, M. R., Yang, X., Saven, J. G., and Gai, F. (2006) Ultrafast folding of a computationally designed Trp-cage mutant: Trp(2)-cage, J. Phys. Chem. B 110, 3759-3763.
    • (2006) J. Phys. Chem. B , vol.110 , pp. 3759-3763
    • Bunagan, M.R.1    Yang, X.2    Saven, J.G.3    Gai, F.4
  • 16
    • 33750717540 scopus 로고    scopus 로고
    • Understanding the folding mechanism of an alpha-helical hairpin
    • Du, D. G., and Gai, F. (2006) Understanding the folding mechanism of an alpha-helical hairpin, Biochemistry 45, 13131-13139.
    • (2006) Biochemistry , vol.45 , pp. 13131-13139
    • Du, D.G.1    Gai, F.2
  • 17
    • 33746608515 scopus 로고    scopus 로고
    • Model systems for beta-hairpins and beta-sheets
    • Hughes, R. M., and Waters, M. L. (2006) Model systems for beta-hairpins and beta-sheets, Curr. Opin. Struct. Biol. 16, 514-524.
    • (2006) Curr. Opin. Struct. Biol , vol.16 , pp. 514-524
    • Hughes, R.M.1    Waters, M.L.2
  • 18
    • 33846708445 scopus 로고    scopus 로고
    • The highly cooperative folding of small naturally occurring proteins is likely the result of natural selection
    • Watters, A. L., Deka, P., Corrent, C., Callender, D., Varani, C., Sosnick, T., and Baker, D. (2007) The highly cooperative folding of small naturally occurring proteins is likely the result of natural selection, Cell 128, 613-624.
    • (2007) Cell , vol.128 , pp. 613-624
    • Watters, A.L.1    Deka, P.2    Corrent, C.3    Callender, D.4    Varani, C.5    Sosnick, T.6    Baker, D.7
  • 19
    • 34547151184 scopus 로고    scopus 로고
    • The helix-turn-helix motif as an ultrafast independently folding domain: The pathway of folding of Engrailed homeodomain
    • Religa, T. L., Johnson, C. M., Vu, D. M., Brewer, S. H., Dyer, R. B., and Fersht, A. R. (2007) The helix-turn-helix motif as an ultrafast independently folding domain: The pathway of folding of Engrailed homeodomain, Proc. Natl. Acad. Sci. U.S.A. 104, 9272-9277.
    • (2007) Proc. Natl. Acad. Sci. U.S.A , vol.104 , pp. 9272-9277
    • Religa, T.L.1    Johnson, C.M.2    Vu, D.M.3    Brewer, S.H.4    Dyer, R.B.5    Fersht, A.R.6
  • 20
    • 0038502170 scopus 로고    scopus 로고
    • Folding dynamics and mechanism of beta-hairpin formation
    • Muñoz, V., Thompson, P. A., Hofrichter, J., and Eaton, W. A. (1997) Folding dynamics and mechanism of beta-hairpin formation, Nature 390, 196-199.
    • (1997) Nature , vol.390 , pp. 196-199
    • Muñoz, V.1    Thompson, P.A.2    Hofrichter, J.3    Eaton, W.A.4
  • 21
    • 0033529908 scopus 로고    scopus 로고
    • Molecular dynamics simulations of unfolding and refolding of a beta-hairpin fragment of protein G
    • Pande, V. S., and Rokhsar, D. S. (1999) Molecular dynamics simulations of unfolding and refolding of a beta-hairpin fragment of protein G, Proc. Natl. Acad. Sci. U.S.A. 96, 9062-9067.
    • (1999) Proc. Natl. Acad. Sci. U.S.A , vol.96 , pp. 9062-9067
    • Pande, V.S.1    Rokhsar, D.S.2
  • 22
    • 0034646218 scopus 로고    scopus 로고
    • Mechanisms and kinetics of beta-hairpin formation
    • Klimov, D. K., and Thirumalai, D. (2000) Mechanisms and kinetics of beta-hairpin formation, Proc. Natl. Acad. Sci. U.S.A. 97, 2544-2549.
    • (2000) Proc. Natl. Acad. Sci. U.S.A , vol.97 , pp. 2544-2549
    • Klimov, D.K.1    Thirumalai, D.2
  • 23
    • 0035909921 scopus 로고    scopus 로고
    • The free energy landscape for beta hairpin folding in explicit water
    • Zhou, R. H., Berne, B. J., and Germain, R. (2001) The free energy landscape for beta hairpin folding in explicit water, Proc. Natl. Acad. Sci. U.S.A. 98, 14931-14936.
    • (2001) Proc. Natl. Acad. Sci. U.S.A , vol.98 , pp. 14931-14936
    • Zhou, R.H.1    Berne, B.J.2    Germain, R.3
  • 24
    • 0038546798 scopus 로고    scopus 로고
    • Optical spectroscopic investigations of model beta-sheet hairpins in aqueous solution
    • Hilario, J., Kubelka, J., and Keiderling, T. A. (2003) Optical spectroscopic investigations of model beta-sheet hairpins in aqueous solution, J. Am. Chem. Soc. 125, 7562-7574.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 7562-7574
    • Hilario, J.1    Kubelka, J.2    Keiderling, T.A.3
  • 25
    • 8644237364 scopus 로고    scopus 로고
    • Understanding the key factors that control the rate of beta-hairpin folding
    • Du, D. G., Zhu, Y. J., Huang, C. Y., and Gai, F. (2004) Understanding the key factors that control the rate of beta-hairpin folding, Proc. Natl. Acad. Sci. U.S.A. 101, 15915-15920.
    • (2004) Proc. Natl. Acad. Sci. U.S.A , vol.101 , pp. 15915-15920
    • Du, D.G.1    Zhu, Y.J.2    Huang, C.Y.3    Gai, F.4
  • 28
    • 23044464791 scopus 로고    scopus 로고
    • Hairpin folding dynamics: The cold-denatured state is predisposed for rapid refolding
    • Dyer, R. B., Maness, S. J., Franzen, S., Fesinmeyer, R. M., Olsen, K. A., and Andersen, N. H. (2004) Hairpin folding dynamics: The cold-denatured state is predisposed for rapid refolding, Biochemistry 44, 10406-10415.
    • (2004) Biochemistry , vol.44 , pp. 10406-10415
    • Dyer, R.B.1    Maness, S.J.2    Franzen, S.3    Fesinmeyer, R.M.4    Olsen, K.A.5    Andersen, N.H.6
  • 29
    • 11244289252 scopus 로고    scopus 로고
    • Kinetic pathways of beta-hairpin (un)folding in explicit solvent
    • Bolhuis, P. G. (2005) Kinetic pathways of beta-hairpin (un)folding in explicit solvent, Biophys. J. 88, 50-61.
    • (2005) Biophys. J , vol.88 , pp. 50-61
    • Bolhuis, P.G.1
  • 30
    • 33644516904 scopus 로고    scopus 로고
    • Understanding the mechanism of beta-hairpin folding via phi-value analysis
    • Du, D. G., Tucker, M. J., and Gai, F. (2006) Understanding the mechanism of beta-hairpin folding via phi-value analysis, Biochemistry 45, 2668-2678.
    • (2006) Biochemistry , vol.45 , pp. 2668-2678
    • Du, D.G.1    Tucker, M.J.2    Gai, F.3
  • 31
    • 33645420726 scopus 로고    scopus 로고
    • Strange temperature dependence of the folding rate of a 16-residue beta-hairpin
    • Xu, Y., Wang, T., and Gai, F. (2006) Strange temperature dependence of the folding rate of a 16-residue beta-hairpin, Chem. Phys. 323, 21-27.
    • (2006) Chem. Phys , vol.323 , pp. 21-27
    • Xu, Y.1    Wang, T.2    Gai, F.3
  • 32
    • 0032479010 scopus 로고    scopus 로고
    • Cooperative interaction between the three strands of a designed antiparallel beta-sheet
    • Sharman, G. J., and Searle, M. S. (1998) Cooperative interaction between the three strands of a designed antiparallel beta-sheet, J. Am. Chem. Soc. 120, 5291-5300.
    • (1998) J. Am. Chem. Soc , vol.120 , pp. 5291-5300
    • Sharman, G.J.1    Searle, M.S.2
  • 33
    • 0032917075 scopus 로고    scopus 로고
    • De novo design of a monomeric three-stranded antiparallel beta-sheet
    • de Alba, E., Santoro, J., Rico, M., and Jimenez, M. A. (1999) De novo design of a monomeric three-stranded antiparallel beta-sheet, Protein Sci. 8, 854-865.
    • (1999) Protein Sci , vol.8 , pp. 854-865
    • de Alba, E.1    Santoro, J.2    Rico, M.3    Jimenez, M.A.4
  • 34
    • 0033824762 scopus 로고    scopus 로고
    • Structure, folding, and energetics of cooperative interactions between the beta-strands of a de novo designed three-stranded antiparallel beta-sheet peptide
    • Griffiths-Jones, S. R., and Searle, M. S. (2000) Structure, folding, and energetics of cooperative interactions between the beta-strands of a de novo designed three-stranded antiparallel beta-sheet peptide, J.. Am. Chem. Soc. 122, 8350-8356.
    • (2000) J.. Am. Chem. Soc , vol.122 , pp. 8350-8356
    • Griffiths-Jones, S.R.1    Searle, M.S.2
  • 35
    • 0035834063 scopus 로고    scopus 로고
    • Length-dependent stability and strand length limits in antiparallel beta-sheet secondary structure
    • Stanger, H. E., Syud, F. A., Espinosa, J. F., Giriat, I., Muir, T., and Gellman, S. H. (2001) Length-dependent stability and strand length limits in antiparallel beta-sheet secondary structure, Proc. Natl. Acad. Sci. U.S.A. 98, 12015-12020.
    • (2001) Proc. Natl. Acad. Sci. U.S.A , vol.98 , pp. 12015-12020
    • Stanger, H.E.1    Syud, F.A.2    Espinosa, J.F.3    Giriat, I.4    Muir, T.5    Gellman, S.H.6
  • 36
    • 0037436347 scopus 로고    scopus 로고
    • Influence of strand number on antiparallel beta-sheet stability in designed three- and four-stranded beta-sheets
    • Syud, F. A., Stanger, H. E., Mortell, H. S., Espinosa, J. F., Fisk, J. D., Fry, C. G., and Gellman, S. H. (2003) Influence of strand number on antiparallel beta-sheet stability in designed three- and four-stranded beta-sheets, J. Mol. Biol. 326, 553-568.
    • (2003) J. Mol. Biol , vol.326 , pp. 553-568
    • Syud, F.A.1    Stanger, H.E.2    Mortell, H.S.3    Espinosa, J.F.4    Fisk, J.D.5    Fry, C.G.6    Gellman, S.H.7
  • 37
    • 0037040804 scopus 로고    scopus 로고
    • Mechanisms of cooperativity underlying sequence-independent beta-sheet formation
    • Guo, C. L., Cheung, M. S., Levine, H., and Kessler, D. A. (2002) Mechanisms of cooperativity underlying sequence-independent beta-sheet formation, J. Chem. Phys. 116, 4353-4365.
    • (2002) J. Chem. Phys , vol.116 , pp. 4353-4365
    • Guo, C.L.1    Cheung, M.S.2    Levine, H.3    Kessler, D.A.4
  • 38
    • 33750589653 scopus 로고    scopus 로고
    • Measuring cooperativity in the formation of a three-stranded beta sheet (double hairpin)
    • Hudson, F. M., and Andersen, N. H. (2006) Measuring cooperativity in the formation of a three-stranded beta sheet (double hairpin), Biopolymers 83, 424-433.
    • (2006) Biopolymers , vol.83 , pp. 424-433
    • Hudson, F.M.1    Andersen, N.H.2
  • 39
    • 33845403686 scopus 로고    scopus 로고
    • Nanosecond folding dynamics of a three-stranded beta-sheet
    • Xu, Y., Purkayastha, P., and Gai, F. (2006) Nanosecond folding dynamics of a three-stranded beta-sheet, J. Am. Chem. Soc. 128, 15836-15842.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 15836-15842
    • Xu, Y.1    Purkayastha, P.2    Gai, F.3
  • 40
    • 0034718553 scopus 로고    scopus 로고
    • Folding simulations of a three-stranded antiparallel beta-sheet peptide
    • Ferrara, P., and Caflisch, A. (2000) Folding simulations of a three-stranded antiparallel beta-sheet peptide, Proc. Natl. Acad. Sci. U.S.A. 97, 10780-10785.
    • (2000) Proc. Natl. Acad. Sci. U.S.A , vol.97 , pp. 10780-10785
    • Ferrara, P.1    Caflisch, A.2
  • 41
    • 0037093655 scopus 로고    scopus 로고
    • Weak temperature dependence of the free energy surface and folding pathways of structured peptides
    • Cavalli, A., Ferrara, P., and Caflisch, A. (2002) Weak temperature dependence of the free energy surface and folding pathways of structured peptides, Proteins: Struct., Funct., Genet. 47, 305-314.
    • (2002) Proteins: Struct., Funct., Genet , vol.47 , pp. 305-314
    • Cavalli, A.1    Ferrara, P.2    Caflisch, A.3
  • 42
    • 0023008334 scopus 로고
    • Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins
    • Krimm, S., and Bandekar, J. (1986) Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins, Adv. Protein Chem. 38, 181-364.
    • (1986) Adv. Protein Chem , vol.38 , pp. 181-364
    • Krimm, S.1    Bandekar, J.2
  • 43
    • 0343532738 scopus 로고
    • Infrared spectra of polypeptides in various conformations - Amide I and II band
    • Miyazawa, T., and Blout, E. R. (1961) Infrared spectra of polypeptides in various conformations - Amide I and II band, J. Am. Chem. Soc. 83, 712-719.
    • (1961) J. Am. Chem. Soc , vol.83 , pp. 712-719
    • Miyazawa, T.1    Blout, E.R.2
  • 44
    • 0016721511 scopus 로고
    • Transition dipole coupling in amide I modes of beta polypeptides
    • Moore, W. H., and Krimm, S. (1975) Transition dipole coupling in amide I modes of beta polypeptides, Proc. Natl. Acad. Sci. U.S.A. 72, 4933-4935.
    • (1975) Proc. Natl. Acad. Sci. U.S.A , vol.72 , pp. 4933-4935
    • Moore, W.H.1    Krimm, S.2
  • 45
    • 4944264263 scopus 로고    scopus 로고
    • Determining beta-sheet stability by Fourier transform infrared difference spectra
    • Wang, T., Xu, Y., Du, D. G., and Gai, F. (2004) Determining beta-sheet stability by Fourier transform infrared difference spectra, Biopolymer 75, 163-172.
    • (2004) Biopolymer , vol.75 , pp. 163-172
    • Wang, T.1    Xu, Y.2    Du, D.G.3    Gai, F.4
  • 46
    • 34249098940 scopus 로고    scopus 로고
    • Infrared study of the effect of hydration on the amide I band and aggregation properties of helical peptides
    • Mukherjee, S., Chowdhury, P., and Gai, F. (2007) Infrared study of the effect of hydration on the amide I band and aggregation properties of helical peptides, J. Phys. Chem. B 111, 4596-4602.
    • (2007) J. Phys. Chem. B , vol.111 , pp. 4596-4602
    • Mukherjee, S.1    Chowdhury, P.2    Gai, F.3
  • 48
    • 6344230036 scopus 로고    scopus 로고
    • Length dependent helix-coil transition kinetics of nine alanine-based peptides
    • Wang, T., Zhu, Y. J., Getahun, Z., Du, D. G., Huang, C. Y., DeGrado, W. F., and Gai, F. (2004) Length dependent helix-coil transition kinetics of nine alanine-based peptides, J. Phys. Chem. B 108, 15301-15310.
    • (2004) J. Phys. Chem. B , vol.108 , pp. 15301-15310
    • Wang, T.1    Zhu, Y.J.2    Getahun, Z.3    Du, D.G.4    Huang, C.Y.5    DeGrado, W.F.6    Gai, F.7
  • 49
    • 0033520751 scopus 로고    scopus 로고
    • Folding free energy surface of a three-stranded beta-sheet protein
    • Bursulaya, B. D., and Brooks, C. L., III (1999) Folding free energy surface of a three-stranded beta-sheet protein, J. Am. Chem. Soc., 121, 9947-9951.
    • (1999) J. Am. Chem. Soc , vol.121 , pp. 9947-9951
    • Bursulaya, B.D.1    Brooks III, C.L.2
  • 50
    • 0034620730 scopus 로고    scopus 로고
    • Molecular dynamics simulations of three-strand beta-sheet folding
    • Wang, H. W., and Sung, S. S. (2000) Molecular dynamics simulations of three-strand beta-sheet folding, J. Am. Chem. Soc. 122, 1999-2009.
    • (2000) J. Am. Chem. Soc , vol.122 , pp. 1999-2009
    • Wang, H.W.1    Sung, S.S.2
  • 51
    • 0036499409 scopus 로고    scopus 로고
    • Folding and stability of the three-stranded beta-sheet peptide betanova: Insights from molecular dynamics simulations
    • Colombo, G., Roccatano, D., and Mark, A. E. (2002) Folding and stability of the three-stranded beta-sheet peptide betanova: Insights from molecular dynamics simulations, Proteins 46, 380-392.
    • (2002) Proteins , vol.46 , pp. 380-392
    • Colombo, G.1    Roccatano, D.2    Mark, A.E.3
  • 52
    • 0041842498 scopus 로고    scopus 로고
    • Fast protein folding on downhill energy landscape
    • Cavalli, A., Haberthur, U., Paci, E., and Caflisch, A. (2003) Fast protein folding on downhill energy landscape, Protein Sci. 12, 1801-1803.
    • (2003) Protein Sci , vol.12 , pp. 1801-1803
    • Cavalli, A.1    Haberthur, U.2    Paci, E.3    Caflisch, A.4
  • 53
    • 23944494644 scopus 로고    scopus 로고
    • Folding cooperativity in a three-stranded beta-sheet model
    • Roe, D. R., Hornak, V., and Simmerling, C. (2005) Folding cooperativity in a three-stranded beta-sheet model, J. Mol. Biol. 352, 370-381.
    • (2005) J. Mol. Biol , vol.352 , pp. 370-381
    • Roe, D.R.1    Hornak, V.2    Simmerling, C.3
  • 54
    • 0036113724 scopus 로고    scopus 로고
    • Analysis of the factors that stabilize a designed two-stranded antiparallel beta-sheet
    • Espinosa, J. F., Syud, F. A., and Gellman, S. H. (2002) Analysis of the factors that stabilize a designed two-stranded antiparallel beta-sheet, Protein Sci. 11, 1492-1505.
    • (2002) Protein Sci , vol.11 , pp. 1492-1505
    • Espinosa, J.F.1    Syud, F.A.2    Gellman, S.H.3
  • 55
    • 0345352750 scopus 로고    scopus 로고
    • Spectroscopic studies of structural changes in two beta-sheet-forming peptides show an ensemble of structures that unfold noncooperatively
    • Kuznetsov, S. V., Hilario, J., Keiderling, T. A., and Ansari, A. (2003) Spectroscopic studies of structural changes in two beta-sheet-forming peptides show an ensemble of structures that unfold noncooperatively, Biochemistry 42, 4321-4332.
    • (2003) Biochemistry , vol.42 , pp. 4321-4332
    • Kuznetsov, S.V.1    Hilario, J.2    Keiderling, T.A.3    Ansari, A.4
  • 56
    • 0037225280 scopus 로고    scopus 로고
    • Origin of unusual Phi-values in protein folding: Evidence against specific nucleation sites
    • Sanchez, I. E., and Kiefhaber, T. (2003) Origin of unusual Phi-values in protein folding: Evidence against specific nucleation sites, J. Mol. Biol. 325, 367-376.
    • (2003) J. Mol. Biol , vol.325 , pp. 367-376
    • Sanchez, I.E.1    Kiefhaber, T.2
  • 57
  • 59
    • 31544472338 scopus 로고    scopus 로고
    • Effect of finite size on cooperativity and rates of protein folding
    • Kouza, M., Li, M. S., O'Brien, E. P., Jr., Hu, C. K., and Thirumalai, D. (2006) Effect of finite size on cooperativity and rates of protein folding, J. Phys. Chem. A 110, 671-676.
    • (2006) J. Phys. Chem. A , vol.110 , pp. 671-676
    • Kouza, M.1    Li, M.S.2    O'Brien Jr., E.P.3    Hu, C.K.4    Thirumalai, D.5
  • 60
    • 33748487166 scopus 로고    scopus 로고
    • Truncation of a cross-linked GCN4-p1 coiled coil leads to ultrafast folding
    • Bunagan, M. R., Cristian, L., DeGrado, W. F., and Gai, F. (2006) Truncation of a cross-linked GCN4-p1 coiled coil leads to ultrafast folding, Biochemistry 45, 10981-10986.
    • (2006) Biochemistry , vol.45 , pp. 10981-10986
    • Bunagan, M.R.1    Cristian, L.2    DeGrado, W.F.3    Gai, F.4
  • 61
    • 0025700218 scopus 로고
    • Intramolecular diffusion-controlled reactions in polymers in the optimized Rouse-Zimm approach. 1. The effect of chain stiffness, reactive site positions, and site numbers
    • Perico, A., and Beggiato, M. (1990) Intramolecular diffusion-controlled reactions in polymers in the optimized Rouse-Zimm approach. 1. The effect of chain stiffness, reactive site positions, and site numbers, Macromolecules 23, 797-803.
    • (1990) Macromolecules , vol.23 , pp. 797-803
    • Perico, A.1    Beggiato, M.2
  • 62
    • 0032205097 scopus 로고    scopus 로고
    • Intramolecular reaction rates of flexible polymers. 1. Simulation results and the classical theory
    • Ortiz-Repiso, M., Freire, J. J., and Rey, A. (1998) Intramolecular reaction rates of flexible polymers. 1. Simulation results and the classical theory, Macromolecules 31, 8356-8362.
    • (1998) Macromolecules , vol.31 , pp. 8356-8362
    • Ortiz-Repiso, M.1    Freire, J.J.2    Rey, A.3
  • 63
    • 33846438226 scopus 로고    scopus 로고
    • End-to-end vs interior loop formation kinetics in unfolded polypeptide chains
    • Fierz, B., and Kiefhaber, T. (2007) End-to-end vs interior loop formation kinetics in unfolded polypeptide chains, J. Am. Chem. Soc. 129, 672-679.
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 672-679
    • Fierz, B.1    Kiefhaber, T.2
  • 64
    • 34047193364 scopus 로고    scopus 로고
    • Kinetics of internal-loop formation in polypeptide chains: A simulation study
    • Doucet, D., Roitberg, A., and Hagen, S. J. (2007) Kinetics of internal-loop formation in polypeptide chains: A simulation study, Biophys. J. 92, 2281-2289.
    • (2007) Biophys. J , vol.92 , pp. 2281-2289
    • Doucet, D.1    Roitberg, A.2    Hagen, S.J.3
  • 65
    • 34247880253 scopus 로고    scopus 로고
    • Protein folding kinetics: Barrier effects in chemical and thermal denaturation experiments
    • Naganathan, A. N., Doshi, U., and Muñoz, V. (2007) Protein folding kinetics: Barrier effects in chemical and thermal denaturation experiments, J. Am. Chem. Soc. 129, 5673-5682.
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 5673-5682
    • Naganathan, A.N.1    Doshi, U.2    Muñoz, V.3
  • 66
    • 34247639441 scopus 로고    scopus 로고
    • Folding free-energy landscape of villin headpiece subdomain from molecular dynamics simulations
    • Lei, H., Wu, C., Liu, H. C., and Duan, Y. (2007) Folding free-energy landscape of villin headpiece subdomain from molecular dynamics simulations, Proc. Natl. Acad. Sci. U.S.A. 104, 4925-4930.
    • (2007) Proc. Natl. Acad. Sci. U.S.A , vol.104 , pp. 4925-4930
    • Lei, H.1    Wu, C.2    Liu, H.C.3    Duan, Y.4
  • 67
    • 34948869804 scopus 로고    scopus 로고
    • The ultimate speed limit to protein folding is conformational searching
    • Ghosh, K., Ozkan, S. B., and Dill, K. A. (2007) The ultimate speed limit to protein folding is conformational searching, J. Am. Chem. Soc. 129, 11920-11927.
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 11920-11927
    • Ghosh, K.1    Ozkan, S.B.2    Dill, K.A.3
  • 68
    • 35648943228 scopus 로고    scopus 로고
    • Ensign, D. L., Kasson, P. M., and Vijay, Pande, S., V. S. (2007) Heterogeneity even at the speed limit of folding: Large-scale molecular dynamics study of a fast-folding variant of the villin headpiece, J. Mol. Biol. 374, 806-816.
    • Ensign, D. L., Kasson, P. M., and Vijay, Pande, S., V. S. (2007) Heterogeneity even at the speed limit of folding: Large-scale molecular dynamics study of a fast-folding variant of the villin headpiece, J. Mol. Biol. 374, 806-816.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.