메뉴 건너뛰기




Volumn 93, Issue 11, 2007, Pages 4076-4082

The effect of charge-charge interactions on the kinetics of α-helix formation

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; CONANTOKIN T; PEPTIDE;

EID: 36849033368     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.107.108548     Document Type: Article
Times cited : (17)

References (67)
  • 1
    • 0000372717 scopus 로고    scopus 로고
    • Discrete step model of helix-coil kinetics: Distribution of fluctuation times
    • Poland, D. 1996. Discrete step model of helix-coil kinetics: distribution of fluctuation times. J. Chem. Phys. 105:1242-1269.
    • (1996) J. Chem. Phys , vol.105 , pp. 1242-1269
    • Poland, D.1
  • 2
    • 29744451813 scopus 로고    scopus 로고
    • The effects of individual amino acids on the fast folding dynamics of α-helical peptides
    • Gooding, E. A., A. P. Ramajo, J. W. Wang, C. Palmer, E. Fouts, and M. Volk. 2005. The effects of individual amino acids on the fast folding dynamics of α-helical peptides. Chem. Commun. 48:5985-5987.
    • (2005) Chem. Commun , vol.48 , pp. 5985-5987
    • Gooding, E.A.1    Ramajo, A.P.2    Wang, J.W.3    Palmer, C.4    Fouts, E.5    Volk, M.6
  • 5
    • 6344230036 scopus 로고    scopus 로고
    • Length dependent helix-coil transition kinetics of nine alanine-based peptides
    • Wang, T., Y. Zhu, Z. Getahun, D. Du, C.-Y. Huang, W. F. DeGrado, and F. Gai. 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.2    Getahun, Z.3    Du, D.4    Huang, C.-Y.5    DeGrado, W.F.6    Gai, F.7
  • 6
    • 0037123067 scopus 로고    scopus 로고
    • Dynamics of the primary processes of protein folding: Helix nucleation
    • Werner, J. H., R. B. Dyer, R. M. Fesinmeyer, and N. H. Andersen. 2002. Dynamics of the primary processes of protein folding: helix nucleation. J. Phys. Chem. B. 106:487-494.
    • (2002) J. Phys. Chem. B , vol.106 , pp. 487-494
    • Werner, J.H.1    Dyer, R.B.2    Fesinmeyer, R.M.3    Andersen, N.H.4
  • 7
    • 0033536452 scopus 로고    scopus 로고
    • α-Helix peptide folding and unfolding activation barriers: A nanosecond UV resonance Raman study
    • Lednev, I. K., A. S. Karnoup, M. C. Sparrow, and S. A. Asher. 1999. α-Helix peptide folding and unfolding activation barriers: a nanosecond UV resonance Raman study. J. Am. Chem. Soc. 121:8074-8086.
    • (1999) J. Am. Chem. Soc , vol.121 , pp. 8074-8086
    • Lednev, I.K.1    Karnoup, A.S.2    Sparrow, M.C.3    Asher, S.A.4
  • 10
    • 0037459269 scopus 로고    scopus 로고
    • Helix-coil kinetics of two 14-residue peptides
    • Wang, T., D. Du, and F. Gai. 2003. Helix-coil kinetics of two 14-residue peptides. Chem. Phys. Lett. 370:842-848.
    • (2003) Chem. Phys. Lett , vol.370 , pp. 842-848
    • Wang, T.1    Du, D.2    Gai, F.3
  • 11
    • 0026525048 scopus 로고
    • Molecular dynamics simulations of helix denaturation
    • Daggett, V., and M. Levitt. 1992. Molecular dynamics simulations of helix denaturation. J. Mol. Biol. 223:1121-1138.
    • (1992) J. Mol. Biol , vol.223 , pp. 1121-1138
    • Daggett, V.1    Levitt, M.2
  • 12
    • 0000345166 scopus 로고    scopus 로고
    • Diffusion-controlled kinetics of the helix-coil transition with square barrier hydrogen bonds
    • Jun, B., and D. L. Weaver. 2000. Diffusion-controlled kinetics of the helix-coil transition with square barrier hydrogen bonds. J. Chem. Phys. 112:4394-4401.
    • (2000) J. Chem. Phys , vol.112 , pp. 4394-4401
    • Jun, B.1    Weaver, D.L.2
  • 13
    • 0035179018 scopus 로고    scopus 로고
    • Helix nucleation kinetics from molecular simulations in explicit solvent
    • Hummer, G., A. E. Garcia, and S. Garde. 2001. Helix nucleation kinetics from molecular simulations in explicit solvent. Proteins Struct. Funct. Genet. 42:77-84.
    • (2001) Proteins Struct. Funct. Genet , vol.42 , pp. 77-84
    • Hummer, G.1    Garcia, A.E.2    Garde, S.3
  • 14
    • 0035955148 scopus 로고    scopus 로고
    • Temperature-dependent helix-coil transition of an alanine based peptide
    • Huang, C.-Y., J. W. Klemke, Z. Getahun, W. F. DeGrado, and F. Gai. 2001. Temperature-dependent helix-coil transition of an alanine based peptide. J. Am. Chem. Soc. 123:9235-9238.
    • (2001) J. Am. Chem. Soc , vol.123 , pp. 9235-9238
    • Huang, C.-Y.1    Klemke, J.W.2    Getahun, Z.3    DeGrado, W.F.4    Gai, F.5
  • 15
    • 0035932703 scopus 로고    scopus 로고
    • Helix folding of an alanine-based peptide in explicit water
    • Wu, X., and S. Wang. 2001. Helix folding of an alanine-based peptide in explicit water. J. Phys. Chem. B. 105:2227-2235.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 2227-2235
    • Wu, X.1    Wang, S.2
  • 16
    • 0035128362 scopus 로고    scopus 로고
    • Effect of viscosity on the kinetics of α-helix and β-hairpin formation
    • Jas, G. S., W. A. Eaton, and J. Hofrichter. 2001. Effect of viscosity on the kinetics of α-helix and β-hairpin formation. J. Phys. Chem. B. 105:261-272.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 261-272
    • Jas, G.S.1    Eaton, W.A.2    Hofrichter, J.3
  • 17
    • 14044274349 scopus 로고    scopus 로고
    • α-Helix formation in a photoswitchable peptide tracked from picoseconds to microseconds by time-resolved IR spectroscopy
    • Bredenbeck, J., J. Helbing, J. R. Kumita, G. A. Woolley, and P. Hamm. 2005. α-Helix formation in a photoswitchable peptide tracked from picoseconds to microseconds by time-resolved IR spectroscopy. Proc. Natl. Acad. Sci. USA. 102:2379-2384.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 2379-2384
    • Bredenbeck, J.1    Helbing, J.2    Kumita, J.R.3    Woolley, G.A.4    Hamm, P.5
  • 18
    • 0001623168 scopus 로고    scopus 로고
    • Helix-coil kinetics: Folding time scales for helical peptides from a sequential kinetic model
    • Brooks III, C. L. 1996. Helix-coil kinetics: folding time scales for helical peptides from a sequential kinetic model. J. Phys. Chem. 100:2546-2549.
    • (1996) J. Phys. Chem , vol.100 , pp. 2546-2549
    • Brooks III, C.L.1
  • 19
    • 33751261979 scopus 로고    scopus 로고
    • Modeling of folding and unfolding mechanisms in alanine-based α-helical polypeptides
    • Morozov, A. N., and S. H. Lin. 2006. Modeling of folding and unfolding mechanisms in alanine-based α-helical polypeptides. J. Phys. Chem. B. 110:20555-20561.
    • (2006) J. Phys. Chem. B , vol.110 , pp. 20555-20561
    • Morozov, A.N.1    Lin, S.H.2
  • 20
    • 0035913510 scopus 로고    scopus 로고
    • Mean first-passage time calculations for the coil-to-helix transition: The active helix Ising model
    • Bruchete, N.-V., and J. E. Straub. 2001. Mean first-passage time calculations for the coil-to-helix transition: the active helix Ising model. J. Phys. Chem. B. 105:6684-6697.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 6684-6697
    • Bruchete, N.-V.1    Straub, J.E.2
  • 21
    • 20544435097 scopus 로고    scopus 로고
    • Exploring the helix-coil transition via all-atom equilibrium ensemble simulations
    • Sorin, E. J., and V. S. Pande. 2005. Exploring the helix-coil transition via all-atom equilibrium ensemble simulations. Biophys. J. 88:2472-2493.
    • (2005) Biophys. J , vol.88 , pp. 2472-2493
    • Sorin, E.J.1    Pande, V.S.2
  • 22
    • 33645399069 scopus 로고    scopus 로고
    • Nonequilibrium protein folding dynamics: Laser-induced pH-jump studies of the helix-coil transition
    • Causgrove, T. P., and R. B. Dyer. 2006. Nonequilibrium protein folding dynamics: laser-induced pH-jump studies of the helix-coil transition. Chem. Phys. 323:2-10.
    • (2006) Chem. Phys , vol.323 , pp. 2-10
    • Causgrove, T.P.1    Dyer, R.B.2
  • 23
    • 33645422964 scopus 로고    scopus 로고
    • Fast folding dynamics of α-helical peptides - effect of solvent additives and pH
    • Ramajo, A. P., S. A. Petty, and M. Volk. 2006. Fast folding dynamics of α-helical peptides - effect of solvent additives and pH. Chem. Phys. 323:11-20.
    • (2006) Chem. Phys , vol.323 , pp. 11-20
    • Ramajo, A.P.1    Petty, S.A.2    Volk, M.3
  • 24
    • 0037126425 scopus 로고    scopus 로고
    • Helix unfolding and intramolecular hydrogen bond dynamics in small α-helices in explicit solvent
    • Margulis, C. J., H. A. Stern, and B. J. Berne. 2002. Helix unfolding and intramolecular hydrogen bond dynamics in small α-helices in explicit solvent. J. Phys. Chem. B. 106:10748-10752.
    • (2002) J. Phys. Chem. B , vol.106 , pp. 10748-10752
    • Margulis, C.J.1    Stern, H.A.2    Berne, B.J.3
  • 25
    • 0242385345 scopus 로고    scopus 로고
    • Role of backbone hydration and salt-bridge formation in stability of α-helix in solution
    • Ghosh, T., S. Garde, and A. E. Garcia. 2003. Role of backbone hydration and salt-bridge formation in stability of α-helix in solution. Biophys. J. 85:3187-3193.
    • (2003) Biophys. J , vol.85 , pp. 3187-3193
    • Ghosh, T.1    Garde, S.2    Garcia, A.E.3
  • 26
    • 33846207122 scopus 로고    scopus 로고
    • Coarse-grained model of coil-to-helix kinetics demonstrates the importance of multiple nucleation sites in helix folding
    • van Giessen, A. E., and J. E. Straub. 2006. Coarse-grained model of coil-to-helix kinetics demonstrates the importance of multiple nucleation sites in helix folding. J. Chem. Theory Comput. 2:674-684.
    • (2006) J. Chem. Theory Comput , vol.2 , pp. 674-684
    • van Giessen, A.E.1    Straub, J.E.2
  • 27
    • 27744438094 scopus 로고    scopus 로고
    • Molecular dynamics simulation of folding of a short helical peptide with many charged residues
    • Wei, C.-C., M.-H. Ho, W.-H. Wang, and Y.-C. Sun. 2005. Molecular dynamics simulation of folding of a short helical peptide with many charged residues. J. Phys. Chem. B. 109:19980-19986.
    • (2005) J. Phys. Chem. B , vol.109 , pp. 19980-19986
    • Wei, C.-C.1    Ho, M.-H.2    Wang, W.-H.3    Sun, Y.-C.4
  • 28
    • 2942754061 scopus 로고    scopus 로고
    • Fs-21 peptides can form both single helix and helix-turn-helix
    • Zhang, W., H. Lei, S. Chowdhury, and Y. Duan. 2004. Fs-21 peptides can form both single helix and helix-turn-helix. J. Phys. Chem. B. 108:7479-7489.
    • (2004) J. Phys. Chem. B , vol.108 , pp. 7479-7489
    • Zhang, W.1    Lei, H.2    Chowdhury, S.3    Duan, Y.4
  • 29
    • 0037234367 scopus 로고    scopus 로고
    • Breaking non-native hydrophobic clusters is the rate-limiting step in the folding of an alanine-based peptide
    • Chowdhury, S., W. Zhang, C. Wu, G. Xiong, and Y. Duan. 2003. Breaking non-native hydrophobic clusters is the rate-limiting step in the folding of an alanine-based peptide. Biopolymers. 68:63-75.
    • (2003) Biopolymers , vol.68 , pp. 63-75
    • Chowdhury, S.1    Zhang, W.2    Wu, C.3    Xiong, G.4    Duan, Y.5
  • 30
    • 0038502170 scopus 로고    scopus 로고
    • Folding dynamics and mechanism of β-hairpin formation
    • Muñoz, V., P. A. Thompson, J. Hofrichter, and W. A. Eaton. 1997. Folding dynamics and mechanism of β-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
  • 32
    • 0347480547 scopus 로고    scopus 로고
    • Infrared study of the stability and folding kinetics of a 15-residue β-hairpin
    • Xu, Y., R. Oyola, and F. Gai. 2003. Infrared study of the stability and folding kinetics of a 15-residue β-hairpin. J. Am. Chem. Soc. 125:15388-15394.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 15388-15394
    • Xu, Y.1    Oyola, R.2    Gai, F.3
  • 33
    • 8644237364 scopus 로고    scopus 로고
    • Understanding the key factors that control the rate of β-hairpin folding
    • Du, D., Y. Zhu, C.-Y. Huang, and F. Gai. 2004. Understanding the key factors that control the rate of β-hairpin folding. Proc. Natl. Acad. Sci. USA. 101:15915-15920.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 15915-15920
    • Du, D.1    Zhu, Y.2    Huang, C.-Y.3    Gai, F.4
  • 35
    • 0037154980 scopus 로고    scopus 로고
    • Protein folding and unfolding at atomic resolution
    • Fersht, A. R., and V. Daggett. 2002. Protein folding and unfolding at atomic resolution. Cell. 108:573-582.
    • (2002) Cell , vol.108 , pp. 573-582
    • Fersht, A.R.1    Daggett, V.2
  • 38
    • 1842637575 scopus 로고    scopus 로고
    • Folding of a three-helix bundle at the folding speed limit
    • Wang, T., Y. Zhu, and F. Gai. 2004. Folding of a three-helix bundle at the folding speed limit. J. Phys. Chem. B. 108:3694-3697.
    • (2004) J. Phys. Chem. B , vol.108 , pp. 3694-3697
    • Wang, T.1    Zhu, Y.2    Gai, F.3
  • 39
    • 33748487166 scopus 로고    scopus 로고
    • Truncation of a cross-linked GCN4-p1 coiled coil leads to ultrafast folding
    • Bunagan, M. R., L. Cristian, W. F. DeGrado, and F. Gai. 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
  • 40
    • 33750717540 scopus 로고    scopus 로고
    • Understanding the folding mechanism of an α-helical hairpin
    • Du, D., and F. Gai. 2006. Understanding the folding mechanism of an α-helical hairpin. Biochemistry. 45:13131-13139.
    • (2006) Biochemistry , vol.45 , pp. 13131-13139
    • Du, D.1    Gai, F.2
  • 41
  • 43
    • 0031038377 scopus 로고    scopus 로고
    • Local interactions in protein folding: Lessons from the α-helix
    • Aurora, R., T. P. Creamer, R. Srinivasan, and G. D. Rose. 1997. Local interactions in protein folding: lessons from the α-helix. J. Biol. Chem. 272:1413-1416.
    • (1997) J. Biol. Chem , vol.272 , pp. 1413-1416
    • Aurora, R.1    Creamer, T.P.2    Srinivasan, R.3    Rose, G.D.4
  • 44
    • 0024707204 scopus 로고
    • Unusually stable helix formation in short alanine-based peptides
    • Marqusee, S., V. H. Robbins, and R. L. Baldwin. 1989. Unusually stable helix formation in short alanine-based peptides. Proc. Natl. Acad. Sci. USA. 86:5286-5290.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5286-5290
    • Marqusee, S.1    Robbins, V.H.2    Baldwin, R.L.3
  • 45
    • 0033607205 scopus 로고    scopus 로고
    • Structure-based conformational preferences of amino acids
    • Koehl, P., and M. Levitt. 1999. Structure-based conformational preferences of amino acids. Proc. Natl. Acad. Sci. USA. 96:12524-12529.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 12524-12529
    • Koehl, P.1    Levitt, M.2
  • 46
    • 0025663105 scopus 로고
    • Strength and co-operativity of contributions of surface salt-bridges to protein stability
    • Horovitz, A., L. Serrano, B. Avron, M. Bycroft, and A. R. Fersht. 1990. Strength and co-operativity of contributions of surface salt-bridges to protein stability. J. Mol. Biol. 216:1031-1044.
    • (1990) J. Mol. Biol , vol.216 , pp. 1031-1044
    • Horovitz, A.1    Serrano, L.2    Avron, B.3    Bycroft, M.4    Fersht, A.R.5
  • 47
    • 0027497118 scopus 로고
    • The energetics of ion-pair and hydrogen-bonding interactions in a helical peptide
    • Scholtz, J. M., H. Qian, V. H. Robbins, and R. L. Baldwin. 1993. The energetics of ion-pair and hydrogen-bonding interactions in a helical peptide. Biochemistry. 32:9668-9676.
    • (1993) Biochemistry , vol.32 , pp. 9668-9676
    • Scholtz, J.M.1    Qian, H.2    Robbins, V.H.3    Baldwin, R.L.4
  • 48
    • 0029034436 scopus 로고
    • Side-chain interactions between sulfur-containing amino acids and phenylalanine in α-helices
    • Viguera, A. R., and L. Serrano. 1995. Side-chain interactions between sulfur-containing amino acids and phenylalanine in α-helices. Biochemistry. 34:8771-8779.
    • (1995) Biochemistry , vol.34 , pp. 8771-8779
    • Viguera, A.R.1    Serrano, L.2
  • 49
    • 0028856785 scopus 로고
    • Optimization of rates of protein folding: The nucleation-condensation mechanism and its implications
    • Fersht, A. R. 1995. Optimization of rates of protein folding: the nucleation-condensation mechanism and its implications. Proc. Natl. Acad. Sci. USA. 92:10869-10873.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10869-10873
    • Fersht, A.R.1
  • 50
    • 0025241893 scopus 로고
    • Conantokin-T. A g-carboxyglutamate containing peptide with N-methyl-D-aspartate antagonist activity
    • Haack, J. A., J. Rivier, T. N. Parks, E. E. Mena, L. J. Cruz, and B. M. Olivera. 1990. Conantokin-T. A g-carboxyglutamate containing peptide with N-methyl-D-aspartate antagonist activity. J. Biol. Chem. 265:6025-6029.
    • (1990) J. Biol. Chem , vol.265 , pp. 6025-6029
    • Haack, J.A.1    Rivier, J.2    Parks, T.N.3    Mena, E.E.4    Cruz, L.J.5    Olivera, B.M.6
  • 52
    • 0031035377 scopus 로고    scopus 로고
    • Determination of the solution structures of conantokin-G and conantokin-T by CD and NMR spectroscopy
    • Skjaerbaek, N., K. J. Nielsen, R. J. Lewis, P. Alewood, and D. J. Craik. 1997. Determination of the solution structures of conantokin-G and conantokin-T by CD and NMR spectroscopy. J. Biol. Chem. 272:2291-2299.
    • (1997) J. Biol. Chem , vol.272 , pp. 2291-2299
    • Skjaerbaek, N.1    Nielsen, K.J.2    Lewis, R.J.3    Alewood, P.4    Craik, D.J.5
  • 53
    • 0031589194 scopus 로고    scopus 로고
    • Role of modified glutamic acid in the helical structure of conantokin-T
    • Lin, C. H., C. S. Chen, K. S. Hsu, D. S. King, and P. C. Lyu. 1997. Role of modified glutamic acid in the helical structure of conantokin-T. FEBS Lett. 407:243-248.
    • (1997) FEBS Lett , vol.407 , pp. 243-248
    • Lin, C.H.1    Chen, C.S.2    Hsu, K.S.3    King, D.S.4    Lyu, P.C.5
  • 54
    • 0030816685 scopus 로고    scopus 로고
    • Mechanism of helix induction by trifluoroethanol: A framework for extrapolating the helix-forming properties of peptides from trifluoroethanol/water mixtures back to water
    • Luo, P., and R. L. Baldwin. 1997. Mechanism of helix induction by trifluoroethanol: a framework for extrapolating the helix-forming properties of peptides from trifluoroethanol/water mixtures back to water. Biochemistry. 36:8413-8421.
    • (1997) Biochemistry , vol.36 , pp. 8413-8421
    • Luo, P.1    Baldwin, R.L.2
  • 57
    • 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., P. Chowdhury, and F. Gai. 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
  • 58
    • 0023667712 scopus 로고
    • Total synthesis and further characterization of the γ-carboxyglutamate-containing "sleeper" peptide from Conus geographus venom
    • Rivier, J., R. Galyean, L. Simon, L. J. Cruz, B. M. Olivera, and W. R. Gray. 1987. Total synthesis and further characterization of the γ-carboxyglutamate-containing "sleeper" peptide from Conus geographus venom. Biochemistry. 26:8508-8512.
    • (1987) Biochemistry , vol.26 , pp. 8508-8512
    • Rivier, J.1    Galyean, R.2    Simon, L.3    Cruz, L.J.4    Olivera, B.M.5    Gray, W.R.6
  • 59
    • 36849040932 scopus 로고    scopus 로고
    • Infrared T-jump study of the folding dynamics αf a-helices and β-hairpins
    • Y. Bai and R. Nussinov, editors. Humana Press, Clifton, NJ
    • Gai, F., D. Du, and Y. Xu. 2006. Infrared T-jump study of the folding dynamics αf a-helices and β-hairpins. In Methods of Molecular Biology, Vol. 350. Y. Bai and R. Nussinov, editors. Humana Press, Clifton, NJ. 1-20.
    • (2006) Methods of Molecular Biology, Vol , vol.350 , pp. 1-20
    • Gai, F.1    Du, D.2    Xu, Y.3
  • 61
    • 0026565486 scopus 로고
    • Energetic contribution of solvent-exposed ion pairs to α-helix structure
    • Lyu, P. C., P. J. Gans, and N. R. Kallenbach. 1992. Energetic contribution of solvent-exposed ion pairs to α-helix structure. J. Mol. Biol. 223:343-350.
    • (1992) J. Mol. Biol , vol.223 , pp. 343-350
    • Lyu, P.C.1    Gans, P.J.2    Kallenbach, N.R.3
  • 62
    • 1242317050 scopus 로고    scopus 로고
    • Salt-bridges can stabilize but do not accelerate the folding of the homodimeric coiled-coil peptide GCN4-p1
    • Ibarra-Molero, B., J. A. Zitzewitz, and C. R. Matthews. 2004. Salt-bridges can stabilize but do not accelerate the folding of the homodimeric coiled-coil peptide GCN4-p1. J. Mol. Biol. 336:989-996.
    • (2004) J. Mol. Biol , vol.336 , pp. 989-996
    • Ibarra-Molero, B.1    Zitzewitz, J.A.2    Matthews, C.R.3
  • 63
    • 3843135179 scopus 로고    scopus 로고
    • Diffusing and colliding: The atomic level folding/unfolding pathway of a small helical protein
    • DeMarco, M. L., D. O. V. Alonso, and V. Daggett. 2004. Diffusing and colliding: the atomic level folding/unfolding pathway of a small helical protein. J. Mol. Biol. 341:1109-1124.
    • (2004) J. Mol. Biol , vol.341 , pp. 1109-1124
    • DeMarco, M.L.1    Alonso, D.O.V.2    Daggett, V.3
  • 64
    • 0029966342 scopus 로고    scopus 로고
    • Barriers to protein folding: Formation of buried polar interactions is a slow step in acquisition of structure
    • Waldburger, C. D., T. Jonsson, and R. T. Sauer. 1996. Barriers to protein folding: formation of buried polar interactions is a slow step in acquisition of structure. Proc. Natl. Acad. Sci. USA. 93:2629-2634.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2629-2634
    • Waldburger, C.D.1    Jonsson, T.2    Sauer, R.T.3
  • 65
    • 0030067976 scopus 로고    scopus 로고
    • Importance of two buried salt-bridges in the stability and folding pathway of barnase
    • Tissot, A. C., S. Vuilleumier, and A. R. Fersht. 1996. Importance of two buried salt-bridges in the stability and folding pathway of barnase. Biochemistry. 35:6786-6794.
    • (1996) Biochemistry , vol.35 , pp. 6786-6794
    • Tissot, A.C.1    Vuilleumier, S.2    Fersht, A.R.3
  • 66
    • 1942521649 scopus 로고    scopus 로고
    • Thermodynamics and kinetics of non-native interactions in protein folding: A single point mutant significantly stabilizes the N-terminal domain of L9 by modulating non-native interactions in the denatured state
    • Cho, J.-H., S. Sato, and D. P. Raleigh. 2004. Thermodynamics and kinetics of non-native interactions in protein folding: a single point mutant significantly stabilizes the N-terminal domain of L9 by modulating non-native interactions in the denatured state. J. Mol. Biol. 338:827-837.
    • (2004) J. Mol. Biol , vol.338 , pp. 827-837
    • Cho, J.-H.1    Sato, S.2    Raleigh, D.P.3
  • 67
    • 33645552899 scopus 로고    scopus 로고
    • Importance of context in protein folding: Secondary structural propensities versus tertiary contact-assisted secondary structure formation
    • Scott, K. A., D. O. V. Alonso, Y. Pan, and V. Daggett. 2006. Importance of context in protein folding: secondary structural propensities versus tertiary contact-assisted secondary structure formation. Biochemistry. 45:4153-4163.
    • (2006) Biochemistry , vol.45 , pp. 4153-4163
    • Scott, K.A.1    Alonso, D.O.V.2    Pan, Y.3    Daggett, V.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.