메뉴 건너뛰기




Volumn 7, Issue 7, 2012, Pages

Atomic-level structure characterization of an ultrafast folding mini-protein denatured state

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN; PROTEIN TC5B; UNCLASSIFIED DRUG; UREA;

EID: 84864402338     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0041301     Document Type: Article
Times cited : (17)

References (80)
  • 1
    • 0028958601 scopus 로고
    • Characterizing transition states in protein folding: an essential step in the puzzle
    • Fersht AR,(1995) Characterizing transition states in protein folding: an essential step in the puzzle. Curr Opin Struct Bio 5: 79-84.
    • (1995) Curr Opin Struct Bio , vol.5 , pp. 79-84
    • Fersht, A.R.1
  • 2
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson CM,(2003) Protein folding and misfolding. Nature 426: 884-890.
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 3
    • 17044446282 scopus 로고    scopus 로고
    • NMR Studies of Structure and Function of Biological Macromolecules (Nobel Lecture)
    • Wüthrich K,(2003) NMR Studies of Structure and Function of Biological Macromolecules (Nobel Lecture). Angew Chem Int Edit 42: 3340-3363.
    • (2003) Angew Chem Int Edit , vol.42 , pp. 3340-3363
    • Wüthrich, K.1
  • 4
    • 4344707281 scopus 로고    scopus 로고
    • Unfolded Proteins and Protein Folding Studied by NMR
    • Dyson HJ, Wright PE,(2004) Unfolded Proteins and Protein Folding Studied by NMR. Chem Rev 104: 3607-3622.
    • (2004) Chem Rev , vol.104 , pp. 3607-3622
    • Dyson, H.J.1    Wright, P.E.2
  • 5
    • 0026672305 scopus 로고
    • NMR Determination of Residual Structure in a Urea-Denatured Protein, the 434-Repressor
    • Neri D, Billeter M, Wider G, Wüthrich K,(1992) NMR Determination of Residual Structure in a Urea-Denatured Protein, the 434-Repressor. Science 257: 1559-1563.
    • (1992) Science , vol.257 , pp. 1559-1563
    • Neri, D.1    Billeter, M.2    Wider, G.3    Wüthrich, K.4
  • 6
    • 0030320442 scopus 로고    scopus 로고
    • The concept of a random coil - Residual structure in peptides and denatured proteins
    • Smith LJ, Fiebig KM, Schwalbe H, Dobson CM,(1996) The concept of a random coil - Residual structure in peptides and denatured proteins. Fold Des 1: R95-R106.
    • (1996) Fold Des , vol.1
    • Smith, L.J.1    Fiebig, K.M.2    Schwalbe, H.3    Dobson, C.M.4
  • 8
    • 33846913510 scopus 로고    scopus 로고
    • Atomic-level characterization of disordered protein ensembles
    • Mittag T, Forman-Kay JD,(2007) Atomic-level characterization of disordered protein ensembles. Curr Opin Struct Bio 17: 3-14.
    • (2007) Curr Opin Struct Bio , vol.17 , pp. 3-14
    • Mittag, T.1    Forman-Kay, J.D.2
  • 10
    • 0034610360 scopus 로고    scopus 로고
    • Protein folding and unfolding in microseconds to nanoseconds by experiment and simulation
    • Mayor U, Johnson CM, Daggett V, Fersht AR,(2000) Protein folding and unfolding in microseconds to nanoseconds by experiment and simulation. Proc Natl Acad Sci U S A 97: 13518-13522.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 13518-13522
    • Mayor, U.1    Johnson, C.M.2    Daggett, V.3    Fersht, A.R.4
  • 11
    • 0037065310 scopus 로고    scopus 로고
    • The Trp Cage: Folding kinetics and unfolded state topology via molecular dynamics simulations
    • Snow CD, Zagrovic B, Pande VS,(2002) The Trp Cage: Folding kinetics and unfolded state topology via molecular dynamics simulations. J Am Chem Soc 124: 14548-14549.
    • (2002) J Am Chem Soc , vol.124 , pp. 14548-14549
    • Snow, C.D.1    Zagrovic, B.2    Pande, V.S.3
  • 12
    • 0037470691 scopus 로고    scopus 로고
    • Ab initio folding simulation of the Trp-cage mini-protein approaches NMR resolution
    • Chowdhury S, Lee MC, Xiong GM, Duan Y,(2003) Ab initio folding simulation of the Trp-cage mini-protein approaches NMR resolution. J Mol Biol 327: 711-717.
    • (2003) J Mol Biol , vol.327 , pp. 711-717
    • Chowdhury, S.1    Lee, M.C.2    Xiong, G.M.3    Duan, Y.4
  • 13
    • 0344824394 scopus 로고    scopus 로고
    • Trp-cage: Folding free energy landscape in explicit water
    • Zhou RH,(2003) Trp-cage: Folding free energy landscape in explicit water. Proc Natl Acad Sci U S A 100: 13280-13285.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 13280-13285
    • Zhou, R.H.1
  • 14
    • 4544223597 scopus 로고    scopus 로고
    • Characterizing the rate-limiting step of Trp-cage folding by all-atom molecular dynamics simulations
    • Chowdhury S, Lee MC, Duan Y,(2004) Characterizing the rate-limiting step of Trp-cage folding by all-atom molecular dynamics simulations. J Phys Chem B 108: 13855-13865.
    • (2004) J Phys Chem B , vol.108 , pp. 13855-13865
    • Chowdhury, S.1    Lee, M.C.2    Duan, Y.3
  • 15
    • 11244291006 scopus 로고    scopus 로고
    • Folding Trp-cage to NMR resolution native structure using a coarse-grained protein model
    • Ding F, Buldyrev SV, Dokholyan NV,(2005) Folding Trp-cage to NMR resolution native structure using a coarse-grained protein model. Biophys J 88: 147-155.
    • (2005) Biophys J , vol.88 , pp. 147-155
    • Ding, F.1    Buldyrev, S.V.2    Dokholyan, N.V.3
  • 16
    • 33846088229 scopus 로고    scopus 로고
    • Computational study of the Trp-cage miniprotein based on the ECEPP/3 force field
    • Zhan LX, Chen JZY, Liu WK,(2007) Computational study of the Trp-cage miniprotein based on the ECEPP/3 force field. Proteins: Struc, Funct, Bioinf 66: 436-443.
    • (2007) Proteins: Struc, Funct, Bioinf , vol.66 , pp. 436-443
    • Zhan, L.X.1    Chen, J.Z.Y.2    Liu, W.K.3
  • 17
    • 56649083699 scopus 로고    scopus 로고
    • Computing the stability diagram of the Trp-cage miniprotein
    • Paschek D, Hempel S, Garcia AE,(2008) Computing the stability diagram of the Trp-cage miniprotein. Proc Natl Acad Sci U S A 105: 17754-17759.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 17754-17759
    • Paschek, D.1    Hempel, S.2    Garcia, A.E.3
  • 18
    • 77955487466 scopus 로고    scopus 로고
    • Multiscale Coarse-Graining of the Protein Energy Landscape
    • Hills RD Jr, Lu LY, Voth GA,(2010) Multiscale Coarse-Graining of the Protein Energy Landscape. PLoS Comput Biol 6: e1000827.
    • (2010) PLoS Comput Biol , vol.6
    • Hills Jr., R.D.1    Lu, L.Y.2    Voth, G.A.3
  • 19
    • 34248363240 scopus 로고    scopus 로고
    • VCD spectroscopic and molecular dynamics analysis of the Trp-cage miniprotein TC5b
    • Copps J, Murphy RF, Lovas S,(2007) VCD spectroscopic and molecular dynamics analysis of the Trp-cage miniprotein TC5b. Biopolymers 88: 427-437.
    • (2007) Biopolymers , vol.88 , pp. 427-437
    • Copps, J.1    Murphy, R.F.2    Lovas, S.3
  • 20
    • 38349097833 scopus 로고    scopus 로고
    • Cooperation between a salt bridge and the hydrophobic core triggers fold stabilization in a Trp-cage miniprotein
    • Hudáky P, Stráner P, Farkas V, Váradi G, Tóth G, et al.(2008) Cooperation between a salt bridge and the hydrophobic core triggers fold stabilization in a Trp-cage miniprotein. Biochemistry 47: 1007-1016.
    • (2008) Biochemistry , vol.47 , pp. 1007-1016
    • Hudáky, P.1    Stráner, P.2    Farkas, V.3    Váradi, G.4    Tóth, G.5
  • 23
    • 33846917230 scopus 로고    scopus 로고
    • Ultrafast and downhill protein folding
    • Dyer RB,(2007) Ultrafast and downhill protein folding. Curr Opin Struct Bio 17: 38-47.
    • (2007) Curr Opin Struct Bio , vol.17 , pp. 38-47
    • Dyer, R.B.1
  • 24
    • 0037032225 scopus 로고    scopus 로고
    • Smaller and faster: The 20-residue Trp-cage protein folds in 4 μs
    • Qiu LL, Pabit SA, Roitberg AE, Hagen SJ,(2002) Smaller and faster: The 20-residue Trp-cage protein folds in 4 μs. J Am Chem Soc 124: 12952-12953.
    • (2002) J Am Chem Soc , vol.124 , pp. 12952-12953
    • Qiu, L.L.1    Pabit, S.A.2    Roitberg, A.E.3    Hagen, S.J.4
  • 25
    • 33644880010 scopus 로고    scopus 로고
    • Ultrafast Folding of a Computationally Designed Trp-Cage Mutant: Trp2-Cage
    • Bunagan MR, Yang X, Saven JG, Gai F,(2006) Ultrafast Folding of a Computationally Designed Trp-Cage Mutant: Trp2-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
  • 27
    • 28044460071 scopus 로고    scopus 로고
    • A microscopic view of miniprotein folding: Enhanced folding efficiency through formation of an intermediate
    • Neuweiler H, Doose S, Sauer M,(2005) A microscopic view of miniprotein folding: Enhanced folding efficiency through formation of an intermediate. Proc Natl Acad Sci U S A 102: 16650-16655.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 16650-16655
    • Neuweiler, H.1    Doose, S.2    Sauer, M.3
  • 28
    • 34247577665 scopus 로고    scopus 로고
    • A pre-existing hydrophobic collapse in the unfolded state of an ultrafast folding protein
    • Mok KH, Kuhn LT, Goez M, Day IJ, Lin JC, et al.(2007) A pre-existing hydrophobic collapse in the unfolded state of an ultrafast folding protein. Nature 447: 106-109.
    • (2007) Nature , vol.447 , pp. 106-109
    • Mok, K.H.1    Kuhn, L.T.2    Goez, M.3    Day, I.J.4    Lin, J.C.5
  • 29
    • 12044259775 scopus 로고
    • Quantitative J Correlation: A New Approach for Measuring Homonuclear Three-Bond J(HNHα) Coupling-Constants in 15N-Enriched Proteins
    • Vuister GW, Bax A,(1993) Quantitative J Correlation: A New Approach for Measuring Homonuclear Three-Bond J(HNHα) Coupling-Constants in 15N-Enriched Proteins. J Am Chem Soc 115: 7772-7777.
    • (1993) J Am Chem Soc , vol.115 , pp. 7772-7777
    • Vuister, G.W.1    Bax, A.2
  • 30
    • 0028393784 scopus 로고
    • The C-13 chemical-shift index - a simple method for the identification of protein secondary structure using C-13 chemical-shift data
    • Wishart DS, Sykes BD,(1994) The C-13 chemical-shift index- a simple method for the identification of protein secondary structure using C-13 chemical-shift data. J Biomol NMR 4: 171-180.
    • (1994) J Biomol NMR , vol.4 , pp. 171-180
    • Wishart, D.S.1    Sykes, B.D.2
  • 32
    • 0037159208 scopus 로고    scopus 로고
    • Molecular Hinges in Protein Folding: the Urea-Denatured State of Apomyoglobin
    • Schwarzinger S, Wright PE, Dyson HJ,(2002) Molecular Hinges in Protein Folding: the Urea-Denatured State of Apomyoglobin. Biochemistry 41: 12681-12686.
    • (2002) Biochemistry , vol.41 , pp. 12681-12686
    • Schwarzinger, S.1    Wright, P.E.2    Dyson, H.J.3
  • 33
    • 0030759665 scopus 로고    scopus 로고
    • Structural and dynamical properties of a denatured protein. Heteronuclear 3D NMR experiments and theoretical simulations of lysozyme in 8 M urea
    • Schwalbe H, Fiebig KM, Buck M, Jones JA, Grimshaw SB, et al.(1997) Structural and dynamical properties of a denatured protein. Heteronuclear 3D NMR experiments and theoretical simulations of lysozyme in 8 M urea. Biochemistry 36: 8977-8991.
    • (1997) Biochemistry , vol.36 , pp. 8977-8991
    • Schwalbe, H.1    Fiebig, K.M.2    Buck, M.3    Jones, J.A.4    Grimshaw, S.B.5
  • 34
    • 23944444257 scopus 로고    scopus 로고
    • Clusters in an intrinsically disordered protein create a protein-binding site: The TolB-binding region of colicin E9
    • Tozawa K, Macdonald CJ, Penfold CN, James R, Kleanthous C, et al.(2005) Clusters in an intrinsically disordered protein create a protein-binding site: The TolB-binding region of colicin E9. Biochemistry 44: 11496-11507.
    • (2005) Biochemistry , vol.44 , pp. 11496-11507
    • Tozawa, K.1    Macdonald, C.J.2    Penfold, C.N.3    James, R.4    Kleanthous, C.5
  • 36
    • 0024449503 scopus 로고
    • Backbone Dynamics of Proteins as Studied by N-15 Inverse Detected Heteronuclear NMR-Spectroscopy - Application to Staphylococcal Nuclease
    • Kay LE, Torchia DA, Bax A,(1989) Backbone Dynamics of Proteins as Studied by N-15 Inverse Detected Heteronuclear NMR-Spectroscopy - Application to Staphylococcal Nuclease. Biochemistry 28: 8972-8979.
    • (1989) Biochemistry , vol.28 , pp. 8972-8979
    • Kay, L.E.1    Torchia, D.A.2    Bax, A.3
  • 37
    • 33746592145 scopus 로고    scopus 로고
    • Motional properties of unfolded ubiquitin: a model for a random coil protein
    • Wirmer J, Peti W, Schwalbe H,(2006) Motional properties of unfolded ubiquitin: a model for a random coil protein. J Biomol NMR 35: 175-186.
    • (2006) J Biomol NMR , vol.35 , pp. 175-186
    • Wirmer, J.1    Peti, W.2    Schwalbe, H.3
  • 38
    • 0035957221 scopus 로고    scopus 로고
    • NMR structural and dynamic characterization of the acid-unfolded state of apomyoglobin provides insights into the early events in protein folding
    • Yao J, Chung J, Eliezer D, Wright PE, Dyson HJ,(2001) NMR structural and dynamic characterization of the acid-unfolded state of apomyoglobin provides insights into the early events in protein folding. Biochemistry 40: 3561-3571.
    • (2001) Biochemistry , vol.40 , pp. 3561-3571
    • Yao, J.1    Chung, J.2    Eliezer, D.3    Wright, P.E.4    Dyson, H.J.5
  • 39
    • 33750962168 scopus 로고    scopus 로고
    • Characterisation of the conformational properties of urea-unfolded Im7: Implications for the early stages of protein folding
    • Le Duff CS, Whittaker SBM, Radford SE, Moore GR,(2006) Characterisation of the conformational properties of urea-unfolded Im7: Implications for the early stages of protein folding. J Mol Biol 364: 824-835.
    • (2006) J Mol Biol , vol.364 , pp. 824-835
    • Le Duff, C.S.1    Whittaker, S.B.M.2    Radford, S.E.3    Moore, G.R.4
  • 40
    • 0026784152 scopus 로고
    • Mapping of the spectral densities of nitrogen-hydrogen bond motions in Eglin c using heteronuclear relaxation experiments
    • Peng JW, Wagner G,(1992) Mapping of the spectral densities of nitrogen-hydrogen bond motions in Eglin c using heteronuclear relaxation experiments. Biochemistry 31: 8571-8586.
    • (1992) Biochemistry , vol.31 , pp. 8571-8586
    • Peng, J.W.1    Wagner, G.2
  • 41
    • 0029623152 scopus 로고
    • Frequency Spectrum of NH Bonds in Eglin c from Spectral Density Mapping at Multiple Fields
    • Peng JW, Wagner G,(1995) Frequency Spectrum of NH Bonds in Eglin c from Spectral Density Mapping at Multiple Fields. Biochemistry 34: 16733-16752.
    • (1995) Biochemistry , vol.34 , pp. 16733-16752
    • Peng, J.W.1    Wagner, G.2
  • 42
    • 0029367044 scopus 로고
    • Spectral Density-Function Mapping Using N-15 Relaxation Data Exclusively
    • Farrow NA, Zhang OW, Szabo A, Torchia DA, Kay LE,(1995) Spectral Density-Function Mapping Using N-15 Relaxation Data Exclusively. J Biomol NMR 6: 153-162.
    • (1995) J Biomol NMR , vol.6 , pp. 153-162
    • Farrow, N.A.1    Zhang, O.W.2    Szabo, A.3    Torchia, D.A.4    Kay, L.E.5
  • 43
    • 0031027137 scopus 로고    scopus 로고
    • Characterization of the Backbone Dynamics of Folded and Denatured States of an SH3 Domain Biochemistry
    • Farrow NA, Zhang O, Forman-Kay JD, Kay LE,(1997) Characterization of the Backbone Dynamics of Folded and Denatured States of an SH3 Domain Biochemistry. 36: 2390-2402.
    • (1997) , vol.36 , pp. 2390-2402
    • Farrow, N.A.1    Zhang, O.2    Forman-Kay, J.D.3    Kay, L.E.4
  • 44
    • 4243155782 scopus 로고    scopus 로고
    • NMR Characterization of the Dynamics of Biomacromolecules
    • Palmer AG III,(2004) NMR Characterization of the Dynamics of Biomacromolecules. Chem Rev 104: 3623-3640.
    • (2004) Chem Rev , vol.104 , pp. 3623-3640
    • Palmer III, A.G.1
  • 45
    • 20144365610 scopus 로고    scopus 로고
    • Structural and dynamic characterization of the acid-unfolded state of hUBF HMG box 1 provides clues for the early events in protein folding
    • Zhang XC, Xu YQ, Zhang JH, Wu JH, Shi YY,(2005) Structural and dynamic characterization of the acid-unfolded state of hUBF HMG box 1 provides clues for the early events in protein folding. Biochemistry 44: 8117-8125.
    • (2005) Biochemistry , vol.44 , pp. 8117-8125
    • Zhang, X.C.1    Xu, Y.Q.2    Zhang, J.H.3    Wu, J.H.4    Shi, Y.Y.5
  • 46
    • 0032553332 scopus 로고    scopus 로고
    • Elucidating the folding problem of alpha-helices: Local motifs, long-range electrostatics, ionic-strength dependence and prediction of NMR parameters
    • Lacroix E, Viguera AR, Serrano L,(1998) Elucidating the folding problem of alpha-helices: Local motifs, long-range electrostatics, ionic-strength dependence and prediction of NMR parameters. J Mol Biol 284: 173-191.
    • (1998) J Mol Biol , vol.284 , pp. 173-191
    • Lacroix, E.1    Viguera, A.R.2    Serrano, L.3
  • 47
    • 0028297302 scopus 로고
    • Structural Characterization of the FK506 Binding Protein Unfolded in Urea and Guanidine Hydrochloride
    • Logan TM, Thériault Y, Fesik SW,(1994) Structural Characterization of the FK506 Binding Protein Unfolded in Urea and Guanidine Hydrochloride. J Mol Biol 236: 637-648.
    • (1994) J Mol Biol , vol.236 , pp. 637-648
    • Logan, T.M.1    Thériault, Y.2    Fesik, S.W.3
  • 48
    • 0028806684 scopus 로고
    • A Comparison of the pH, Urea, and Temperature-denatured States of Barnase by Heteronuclear NMR: Implications for the Initiation of Protein Folding
    • Arcus VL, Vuilleumier S, Freund SMV, Bycroft M, Fersht AR,(1995) A Comparison of the pH, Urea, and Temperature-denatured States of Barnase by Heteronuclear NMR: Implications for the Initiation of Protein Folding. J Mol Biol 254: 305-321.
    • (1995) J Mol Biol , vol.254 , pp. 305-321
    • Arcus, V.L.1    Vuilleumier, S.2    Freund, S.M.V.3    Bycroft, M.4    Fersht, A.R.5
  • 49
    • 33748349224 scopus 로고    scopus 로고
    • The role of hydrophobic interactions in initiation and propagation of protein folding
    • Dyson HJ, Wright PE, Scheraga HA,(2006) The role of hydrophobic interactions in initiation and propagation of protein folding. Proc Natl Acad Sci U S A 103: 13057-13061.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 13057-13061
    • Dyson, H.J.1    Wright, P.E.2    Scheraga, H.A.3
  • 50
    • 44049097465 scopus 로고    scopus 로고
    • Modeling transient collapsed states of an unfolded protein to provide insights into early folding events
    • Felitsky DJ, Lietzow MA, Dyson HJ, Wright PE,(2008) Modeling transient collapsed states of an unfolded protein to provide insights into early folding events. Proc Natl Acad Sci U S A 105: 6278-6283.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 6278-6283
    • Felitsky, D.J.1    Lietzow, M.A.2    Dyson, H.J.3    Wright, P.E.4
  • 51
    • 0029858909 scopus 로고    scopus 로고
    • A speed limit for protein folding
    • McCammon JA,(1996) A speed limit for protein folding. Proc Natl Acad Sci U S A 93: 11426-11427.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 11426-11427
    • McCammon, J.A.1
  • 53
    • 84555202613 scopus 로고    scopus 로고
    • The Trp-cage miniprotein with single-site mutations: Studies of stability and dynamics using molecular dynamics
    • Wu XM, Yang G, Zu YG, Fu YJ, Zhou LJ, et al.(2011) The Trp-cage miniprotein with single-site mutations: Studies of stability and dynamics using molecular dynamics. Comput Theor Chem 973: 1-8.
    • (2011) Comput Theor Chem , vol.973 , pp. 1-8
    • Wu, X.M.1    Yang, G.2    Zu, Y.G.3    Fu, Y.J.4    Zhou, L.J.5
  • 54
    • 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 U S A 92: 10869-10873.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 10869-10873
    • Fersht, A.R.1
  • 55
  • 56
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels Nat Struct Biol
    • Dill KA, Chan HS,(1997) From Levinthal to pathways to funnels Nat Struct Biol. 4: 10-19.
    • (1997) , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 57
    • 0009586942 scopus 로고    scopus 로고
    • Understanding protein folding via free-energy surfaces from theory and experiment
    • Dinner AR, Šali A, Smith LJ, Dobson CM, Karplus M,(2000) Understanding protein folding via free-energy surfaces from theory and experiment. Trends Biochem Sci 25: 331-339.
    • (2000) Trends Biochem Sci , vol.25 , pp. 331-339
    • Dinner, A.R.1    Šali, A.2    Smith, L.J.3    Dobson, C.M.4    Karplus, M.5
  • 58
    • 0037221599 scopus 로고    scopus 로고
    • Is there a unifying mechanism for protein folding
    • Daggett V, Fersht AR,(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
  • 59
    • 0020024242 scopus 로고
    • Specific Intermediates in the Folding Reactions of Small Proteins and the Mechanism of Protein Folding
    • Kim PS, Baldwin RL,(1982) Specific Intermediates in the Folding Reactions of Small Proteins and the Mechanism of Protein Folding. Annu Rev Biochem 51: 459-489.
    • (1982) Annu Rev Biochem , vol.51 , pp. 459-489
    • Kim, P.S.1    Baldwin, R.L.2
  • 60
    • 0023626273 scopus 로고
    • Protein folding: Hypotheses and experiments
    • Ptitsyn OB,(1987) Protein folding: Hypotheses and experiments. Journal of Protein Chemistry 6: 273-293.
    • (1987) Journal of Protein Chemistry , vol.6 , pp. 273-293
    • Ptitsyn, O.B.1
  • 61
    • 0025345415 scopus 로고
    • Intermediates in the Folding Reactions of Small Proteins
    • Kim PS, Baldwin RL,(1990) Intermediates in the Folding Reactions of Small Proteins. Annu Rev Biochem 59: 631-660.
    • (1990) Annu Rev Biochem , vol.59 , pp. 631-660
    • Kim, P.S.1    Baldwin, R.L.2
  • 62
    • 0017251893 scopus 로고
    • Protein-folding dynamics
    • Karplus M, Weaver DL,(1976) Protein-folding dynamics. Nature 260: 404-406.
    • (1976) Nature , vol.260 , pp. 404-406
    • Karplus, M.1    Weaver, D.L.2
  • 63
    • 0032127769 scopus 로고    scopus 로고
    • A structural comparison of the colicin immunity proteins Im7 and Im9 gives new insights into the molecular determinants of immunity-protein specificity
    • Dennis CA, Videler H, Pauptit RA, Wallis R, James R, et al.(1998) A structural comparison of the colicin immunity proteins Im7 and Im9 gives new insights into the molecular determinants of immunity-protein specificity. Biochem J 333: 183-191.
    • (1998) Biochem J , vol.333 , pp. 183-191
    • Dennis, C.A.1    Videler, H.2    Pauptit, R.A.3    Wallis, R.4    James, R.5
  • 64
    • 0037432188 scopus 로고    scopus 로고
    • Protein folding: could hydrophobic collapse be coupled with hydrogen-bond formation
    • Fernández A, Kardos J, Goto Y,(2003) Protein folding: could hydrophobic collapse be coupled with hydrogen-bond formation? FEBS letters 536: 187-192.
    • (2003) FEBS Letters , vol.536 , pp. 187-192
    • Fernández, A.1    Kardos, J.2    Goto, Y.3
  • 65
    • 0037181484 scopus 로고    scopus 로고
    • The chicken-egg scenario of protein folding revisited
    • Uversky VN, Fink AL,(2002) The chicken-egg scenario of protein folding revisited. FEBS letters 515: 79-83.
    • (2002) FEBS Letters , vol.515 , pp. 79-83
    • Uversky, V.N.1    Fink, A.L.2
  • 66
    • 0024417964 scopus 로고
    • The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure
    • Kuwajima K,(1989) The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure. Proteins: Struc, Funct, Bioinf 6: 87-103.
    • (1989) Proteins: Struc, Funct, Bioinf , vol.6 , pp. 87-103
    • Kuwajima, K.1
  • 67
    • 0029160445 scopus 로고
    • How the molten globule became
    • Ptitsyn OB,(1995) How the molten globule became. Trends Biochem Sci 20: 376-379.
    • (1995) Trends Biochem Sci , vol.20 , pp. 376-379
    • Ptitsyn, O.B.1
  • 68
    • 80855133540 scopus 로고    scopus 로고
    • Achieving Secondary Structural Resolution in Kinetic Measurements of Protein Folding: A Case Study of the Folding Mechanism of Trp-cage
    • Culik RM, Serrano AL, Bunagan MR, Gai F,(2011) Achieving Secondary Structural Resolution in Kinetic Measurements of Protein Folding: A Case Study of the Folding Mechanism of Trp-cage. Angew Chem Int Edit 50: 10884-10887.
    • (2011) Angew Chem Int Edit , vol.50 , pp. 10884-10887
    • Culik, R.M.1    Serrano, A.L.2    Bunagan, M.R.3    Gai, F.4
  • 69
    • 0037174385 scopus 로고    scopus 로고
    • All-Atom Structure Prediction and Folding Simulations of a Stable Protein
    • Simmerling C, Strockbine B, Roitberg AE,(2002) All-Atom Structure Prediction and Folding Simulations of a Stable Protein. J Am Chem Soc 124: 11258-11259.
    • (2002) J Am Chem Soc , vol.124 , pp. 11258-11259
    • Simmerling, C.1    Strockbine, B.2    Roitberg, A.E.3
  • 70
    • 23744503388 scopus 로고    scopus 로고
    • UV-resonance Raman thermal unfolding study of Trp-cage shows that it is not a simple two-state miniprotein
    • Ahmed Z, Beta IA, Mikhonin AV, Asher SA,(2005) UV-resonance Raman thermal unfolding study of Trp-cage shows that it is not a simple two-state miniprotein. J. Am. Chem. Soc. 127: 10943-10950.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 10943-10950
    • Ahmed, Z.1    Beta, I.A.2    Mikhonin, A.V.3    Asher, S.A.4
  • 71
    • 0029400480 scopus 로고
    • NMRPIPE - A Multidimensional Spectral Processing System Based on UNIX Pipes
    • Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, et al.(1995) NMRPIPE - A Multidimensional Spectral Processing System Based on UNIX Pipes. J Biomol NMR 6: 277-293.
    • (1995) J Biomol NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5
  • 73
    • 34249765651 scopus 로고
    • NMR VIEW - A Computer-Program for the Visualization and Analysis of NMR Data
    • Johnson BA, Blevins RA,(1994) NMR VIEW - A Computer-Program for the Visualization and Analysis of NMR Data. J Biomol NMR 4: 603-614.
    • (1994) J Biomol NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 74
    • 2442460927 scopus 로고
    • Molecular-dynamics analysis of nmr relaxation in a zinc-finger peptide
    • Palmer AG III, Case DA,(1992) Molecular-dynamics analysis of nmr relaxation in a zinc-finger peptide. J Am Chem Soc 114: 9059-9067.
    • (1992) J Am Chem Soc , vol.114 , pp. 9059-9067
    • Palmer III, A.G.1    Case, D.A.2
  • 75
    • 0001144784 scopus 로고    scopus 로고
    • Monitoring Macromolecular Motions on Microsecond to Millisecond Time Scales by R1ρ-R1 Constant Relaxation Time NMR Spectroscopy
    • Akke M, Palmer AG III,(1996) Monitoring Macromolecular Motions on Microsecond to Millisecond Time Scales by R1ρ-R1 Constant Relaxation Time NMR Spectroscopy. J. Am. Chem. Soc. 118: 911-912.
    • (1996) J. Am. Chem. Soc , vol.118 , pp. 911-912
    • Akke, M.1    Palmer III, A.G.2
  • 76
    • 0028389502 scopus 로고
    • A General Enhancement Scheme in Heteronuclear Multidimensional NMR Employing Pulsed-Field Gradients
    • Schleucher J, Schwendinger M, Sattler M, Schmidt P, Schedletzky O, et al.(1994) A General Enhancement Scheme in Heteronuclear Multidimensional NMR Employing Pulsed-Field Gradients. J Biomol NMR 4: 301-306.
    • (1994) J Biomol NMR , vol.4 , pp. 301-306
    • Schleucher, J.1    Schwendinger, M.2    Sattler, M.3    Schmidt, P.4    Schedletzky, O.5
  • 77
    • 0026637797 scopus 로고
    • Backbone dynamics of the Bacillus subtilis glucose permease IIA domain determined from nitrogen-15 NMR relaxation measurements
    • Stone MJ, Fairbrother WJ, Palmer AG III, Reizer J, Saier MH, et al.(1992) Backbone dynamics of the Bacillus subtilis glucose permease IIA domain determined from nitrogen-15 NMR relaxation measurements. Biochemistry 31: 4394-4406.
    • (1992) Biochemistry , vol.31 , pp. 4394-4406
    • Stone, M.J.1    Fairbrother, W.J.2    Palmer III, A.G.3    Reizer, J.4    Saier, M.H.5
  • 78
    • 0027393188 scopus 로고
    • Comparison of backbone and tryptophan side-chain dynamics of reduced and oxidized Escherichia coli thioredoxin using nitrogen-15 NMR relaxation measurements
    • Stone MJ, Chandrasekhar K, Holmgren A, Wright PE, Dyson HJ,(1993) Comparison of backbone and tryptophan side-chain dynamics of reduced and oxidized Escherichia coli thioredoxin using nitrogen-15 NMR relaxation measurements. Biochemistry 32: 426-435.
    • (1993) Biochemistry , vol.32 , pp. 426-435
    • Stone, M.J.1    Chandrasekhar, K.2    Holmgren, A.3    Wright, P.E.4    Dyson, H.J.5
  • 79
    • 0028240897 scopus 로고
    • A New-Generation of Information-Retrevial Tools for Biologists - the Example of the EXPASY WWW Server
    • Appel RD, Bairoch A, Hochstrasser DF,(1994) A New-Generation of Information-Retrevial Tools for Biologists- the Example of the EXPASY WWW Server. Trends Biochem Sci 19: 258-260.
    • (1994) Trends Biochem Sci , vol.19 , pp. 258-260
    • Appel, R.D.1    Bairoch, A.2    Hochstrasser, D.F.3
  • 80
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi R, Billeter M, Wüthrich K,(1996) MOLMOL: A program for display and analysis of macromolecular structures. J Mol Graph 14: 51-55.
    • (1996) J Mol Graph , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.