메뉴 건너뛰기




Volumn 13, Issue 1, 2004, Pages 40-53

Thermodynamics and stability of a β-sheet complex: Molecular dynamics simulations on simplified off-lattice protein models

Author keywords

sheet complex; Amyloid; Bias gap; Discontinuous molecular dynamics; Fibril; Go type potential; Intermolecular contact parameter

Indexed keywords

MONOMER; OLIGOMER;

EID: 0347364624     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.03162804     Document Type: Article
Times cited : (29)

References (82)
  • 1
    • 36849126204 scopus 로고
    • Studies in molecular dynamics. I: General method
    • Alder, B.J. and Wainwright, T.E. 1959. Studies in molecular dynamics, I: General method. J. Chem. Phys. 31: 459-466.
    • (1959) J. Chem. Phys. , vol.31 , pp. 459-466
    • Alder, B.J.1    Wainwright, T.E.2
  • 3
    • 0034724375 scopus 로고    scopus 로고
    • Two-dimensional structure of β-amyloid(10-35) fibrils
    • -. 2000. Two-dimensional structure of β-amyloid(10-35) fibrils. Biochemistry 39: 3491-3499.
    • (2000) Biochemistry , vol.39 , pp. 3491-3499
  • 4
    • 41849083678 scopus 로고
    • Dynamics at solid liquid transition-experiments at the freezing-point
    • Bilgram, J.H. 1987. Dynamics at solid liquid transition-experiments at the freezing-point. Phys. Rep. 153: 1-89.
    • (1987) Phys. Rep. , vol.153 , pp. 1-89
    • Bilgram, J.H.1
  • 6
    • 0035151879 scopus 로고    scopus 로고
    • Competition between protein folding and aggregation: A three-dimensional lattice-model simulation
    • Bratko, D. and Blanch, H.W. 2001. Competition between protein folding and aggregation: A three-dimensional lattice-model simulation. J. Chem. Phys. 114: 561-569.
    • (2001) J. Chem. Phys. , vol.114 , pp. 561-569
    • Bratko, D.1    Blanch, H.W.2
  • 8
    • 36449000646 scopus 로고
    • Transition states and folding dynamics of proteins and heteropolymers
    • Chan, H.S. and Dill, K.A. 1994. Transition states and folding dynamics of proteins and heteropolymers. J. Chem. Phys. 100: 9238-9257.
    • (1994) J. Chem. Phys. , vol.100 , pp. 9238-9257
    • Chan, H.S.1    Dill, K.A.2
  • 10
    • 0026556822 scopus 로고
    • Phase separation inhibitors and prevention of selenite cataract
    • Clark, J. and Steele, J. 1992. Phase separation inhibitors and prevention of selenite cataract. Proc. Natl. Acad. Sci. 89: 1720-1724.
    • (1992) Proc. Natl. Acad. Sci. , vol.89 , pp. 1720-1724
    • Clark, J.1    Steele, J.2
  • 11
    • 0028966781 scopus 로고
    • Modeling protein stability as heteropolymer collapse
    • Dill, K.A. and Stigter, D. 1995. Modeling protein stability as heteropolymer collapse. Adv. Protein Chem. 46: 59-104.
    • (1995) Adv. Protein Chem. , vol.46 , pp. 59-104
    • Dill, K.A.1    Stigter, D.2
  • 12
    • 0036228167 scopus 로고    scopus 로고
    • Exploring protein aggregation and self-propagation using lattice models: Phase diagram and kinetics
    • Dima, R.I. and Thirumalai, D. 2002. Exploring protein aggregation and self-propagation using lattice models: Phase diagram and kinetics. Protein Sci. 11: 1036-1049.
    • (2002) Protein Sci. , vol.11 , pp. 1036-1049
    • Dima, R.I.1    Thirumalai, D.2
  • 13
    • 0032443390 scopus 로고    scopus 로고
    • Discrete molecular dynamics studies of the folding of a protein-like model
    • Dokholyan, N.V., Buldyrev, S.V., Stanley, H.E., and Shakhnovich, E.I. 1998. Discrete molecular dynamics studies of the folding of a protein-like model. Fold. Des. 3: 577-587.
    • (1998) Fold. Des. , vol.3 , pp. 577-587
    • Dokholyan, N.V.1    Buldyrev, S.V.2    Stanley, H.E.3    Shakhnovich, E.I.4
  • 14
    • 0034628914 scopus 로고    scopus 로고
    • Identifying the protein folding nucleus using molecular dynamics
    • -. 2000. Identifying the protein folding nucleus using molecular dynamics. J. Mol. Biol. 296: 1183-1188.
    • (2000) J. Mol. Biol. , vol.296 , pp. 1183-1188
  • 15
    • 0025276708 scopus 로고
    • Sickle cell hemoglobin polymerization
    • Eaton, W.A. and Hofrichter, J. 1990. Sickle cell hemoglobin polymerization. Adv. Protein Chem. 40: 63-279.
    • (1990) Adv. Protein Chem. , vol.40 , pp. 63-279
    • Eaton, W.A.1    Hofrichter, J.2
  • 18
    • 33646987405 scopus 로고
    • Optimized Monte Carlo data analysis
    • Ferrenberg, A.M. and Swendsen, R.H. 1989. Optimized Monte Carlo data analysis. Phys. Rev. Lett. 63: 1195-1197.
    • (1989) Phys. Rev. Lett. , vol.63 , pp. 1195-1197
    • Ferrenberg, A.M.1    Swendsen, R.H.2
  • 19
    • 0031932169 scopus 로고    scopus 로고
    • Protein aggregation: Folding aggregates, inclusion bodies and amyloid
    • Fink, A.L. 1998. Protein aggregation: Folding aggregates, inclusion bodies and amyloid. Fold. Des. 3: R9-R23.
    • (1998) Fold. Des. , vol.3
    • Fink, A.L.1
  • 21
    • 0025838381 scopus 로고
    • pH-dependent structural transitions of Alzheimer amyloid peptides
    • Fraser, P.E., Nguyen, J.T., Surewicz, W.K., and Kirschner, D.A. 1991b. pH-dependent structural transitions of Alzheimer amyloid peptides. Biophys. J. 60: 1190-1201.
    • (1991) Biophys. J. , vol.60 , pp. 1190-1201
    • Fraser, P.E.1    Nguyen, J.T.2    Surewicz, W.K.3    Kirschner, D.A.4
  • 23
    • 0000355428 scopus 로고
    • Respective roles of short range and long range interactions in protein folding
    • Go, N. and Taketomi, H. 1978. Respective roles of short range and long range interactions in protein folding. Proc. Natl. Acad. Sci. 75: 559-563.
    • (1978) Proc. Natl. Acad. Sci. , vol.75 , pp. 559-563
    • Go, N.1    Taketomi, H.2
  • 24
    • 0018475814 scopus 로고
    • Studies on protein folding, unfolding and fluctuations by computer simulation, IV: Hydrophobic interactions
    • -. 1979. Studies on protein folding, unfolding and fluctuations by computer simulation, IV: Hydrophobic interactions. Int. J. Protein Res. 13: 447-461.
    • (1979) Int. J. Protein Res. , vol.13 , pp. 447-461
  • 26
    • 0002689652 scopus 로고    scopus 로고
    • Thermodynamics of protein folding: A statistical mechanical study of a small all-β protein
    • Guo, Z. and Brooks III, C.L. 1997. Thermodynamics of protein folding: A statistical mechanical study of a small all-β protein. Biopolymers 42: 745-757.
    • (1997) Biopolymers , vol.42 , pp. 745-757
    • Guo, Z.1    Brooks III, C.L.2
  • 27
    • 0029010695 scopus 로고
    • Kinetics of protein folding: Nucleation mechanism, time scales, and pathways
    • Guo, Z., and Thirumalai, D. 1995. Kinetics of protein folding: Nucleation mechanism, time scales, and pathways. Biopolymers 36: 83-102.
    • (1995) Biopolymers , vol.36 , pp. 83-102
    • Guo, Z.1    Thirumalai, D.2
  • 28
    • 0030601851 scopus 로고    scopus 로고
    • Kinetics and thermodynamics of folding of a de novo designed four-helix bundle protein
    • -. 1996. Kinetics and thermodynamics of folding of a de novo designed four-helix bundle protein. J. Mol. Biol. 263: 323-343.
    • (1996) J. Mol. Biol. , vol.263 , pp. 323-343
  • 29
    • 0031555024 scopus 로고    scopus 로고
    • Effect of solvent conditions upon refolding pathways and intermediates for a simple lattice protein
    • Gupta, P. and Hall, C.K. 1997. Effect of solvent conditions upon refolding pathways and intermediates for a simple lattice protein. Biopolymers 42: 399-409.
    • (1997) Biopolymers , vol.42 , pp. 399-409
    • Gupta, P.1    Hall, C.K.2
  • 30
    • 0031696773 scopus 로고    scopus 로고
    • Effect of denaturant and protein concentrations upon protein refolding and aggregation: A simple lattice model
    • -. 1998. Effect of denaturant and protein concentrations upon protein refolding and aggregation: A simple lattice model. Protein Sci. 7: 2642-2652.
    • (1998) Protein Sci. , vol.7 , pp. 2642-2652
  • 31
    • 0033150721 scopus 로고    scopus 로고
    • Computer simulation of the competition between folding and aggregation
    • Gupta, P., Hall, C.K., and Voegler, A. 1999. Computer simulation of the competition between folding and aggregation. Fluid Phase Equilib. 158: 87-93.
    • (1999) Fluid Phase Equilib. , vol.158 , pp. 87-93
    • Gupta, P.1    Hall, C.K.2    Voegler, A.3
  • 32
    • 0030614627 scopus 로고    scopus 로고
    • Observation of metastableAβ amyloid protofibrils by atomic force microscopy
    • Harper, J.D., Wong, S.S., Lieber, C.M., and Lansbury Jr., P.T. 1997. Observation of metastableAβ amyloid protofibrils by atomic force microscopy. Chem. Biol. 4: 119-125.
    • (1997) Chem. Biol. , vol.4 , pp. 119-125
    • Harper, J.D.1    Wong, S.S.2    Lieber, C.M.3    Lansbury Jr., P.T.4
  • 33
    • 0033582587 scopus 로고    scopus 로고
    • Thermodynamics of model prions and its implications for the problem of prion protein folding
    • Harrison, P.M., Chan, H.S., Prusiner, S.B., and Cohen, F.E. 1999. Thermodynamics of model prions and its implications for the problem of prion protein folding. J. Mol. Biol. 286: 593-606.
    • (1999) J. Mol. Biol. , vol.286 , pp. 593-606
    • Harrison, P.M.1    Chan, H.S.2    Prusiner, S.B.3    Cohen, F.E.4
  • 34
    • 0035079856 scopus 로고    scopus 로고
    • Conformational propagation with prion-like characteristics in a simple model of protein folding
    • -. 2001. Conformational propagation with prion-like characteristics in a simple model of protein folding. Protein Sci. 10: 819-835.
    • (2001) Protein Sci. , vol.10 , pp. 819-835
  • 35
    • 0036156804 scopus 로고    scopus 로고
    • Folding thermodynamics of model four-strand antiparallel β-sheet proteins
    • Jang, H., Hall, C.K., and Zhou, Y. 2002a. Folding thermodynamics of model four-strand antiparallel β-sheet proteins. Biophys. J. 82: 646-659.
    • (2002) Biophys. J. , vol.82 , pp. 646-659
    • Jang, H.1    Hall, C.K.2    Zhou, Y.3
  • 36
    • 0035997013 scopus 로고    scopus 로고
    • Protein folding pathways and kinetics: Molecular dynamics simulations β-strand motifs
    • -. 2002b. Protein folding pathways and kinetics: Molecular dynamics simulations β-strand motifs. Biophys. J. 83: 819-835.
    • (2002) Biophys. J. , vol.83 , pp. 819-835
  • 37
    • 0346652459 scopus 로고    scopus 로고
    • Assembly and kinetic folding pathways of a tetrameric-sheet complex: Molecular dynamics simulations on simplified off-lattice protein models
    • in press
    • -. 2003. Assembly and kinetic folding pathways of a tetrameric-sheet complex: Molecular dynamics simulations on simplified off-lattice protein models. Biophys. J. (in press).
    • (2003) Biophys. J.
  • 38
    • 0036304480 scopus 로고    scopus 로고
    • Towards a consistent modeling of protein thermodynamic and kinetic cooperativity: How applicable is the transition state picture to folding and unfolding?
    • Kaya, H. and Chan, H.S. 2002. Towards a consistent modeling of protein thermodynamic and kinetic cooperativity: How applicable is the transition state picture to folding and unfolding? J. Mol. Biol. 315: 899-909.
    • (2002) J. Mol. Biol. , vol.315 , pp. 899-909
    • Kaya, H.1    Chan, H.S.2
  • 39
    • 0037459035 scopus 로고    scopus 로고
    • Solvation effects and driving forces for protein thermodynamic and kinetic cooperativity: How adequate is native-centric topological modeling?
    • -. 2003. Solvation effects and driving forces for protein thermodynamic and kinetic cooperativity: How adequate is native-centric topological modeling? J. Mol. Biol. 326: 911-931.
    • (2003) J. Mol. Biol. , vol.326 , pp. 911-931
  • 40
    • 0029981197 scopus 로고    scopus 로고
    • Alternative conformations of amyloidogenic proteins govern their behavior
    • Kelly, J.W. 1996. Alternative conformations of amyloidogenic proteins govern their behavior. Curr. Opin. Struct. Biol. 6: 11-17.
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 11-17
    • Kelly, J.W.1
  • 41
    • 0035957228 scopus 로고    scopus 로고
    • Partially folded intermediates as critical precursors of light chain amyloid fibrils and amorphous aggregates
    • Khurana, R., Gillespie, J.R., Talapatra, A., Minert, L.J., Ionescu-Zanetti, C., Millett, I., and Fink, A.L. 2001. Partially folded intermediates as critical precursors of light chain amyloid fibrils and amorphous aggregates. Biochemistry 40: 3525-3535.
    • (2001) Biochemistry , vol.40 , pp. 3525-3535
    • Khurana, R.1    Gillespie, J.R.2    Talapatra, A.3    Minert, L.J.4    Ionescu-Zanetti, C.5    Millett, I.6    Fink, A.L.7
  • 42
    • 0036708168 scopus 로고    scopus 로고
    • Paradigm shifts in Alzheimer's disease and other neurodegenerative disorders: The emerging role of oligomeric assemblies
    • Kirkitadze, M.D., Bitan, G., and Teplow, D.B. 2002. Paradigm shifts in Alzheimer's disease and other neurodegenerative disorders: The emerging role of oligomeric assemblies. J. Neurosci. Res. 69: 567-577.
    • (2002) J. Neurosci. Res. , vol.69 , pp. 567-577
    • Kirkitadze, M.D.1    Bitan, G.2    Teplow, D.B.3
  • 43
    • 0000671822 scopus 로고
    • Computer design of idealized Β-motifs
    • Kolinski, A., Galazka, W., and Skolnick, J. 1995. Computer design of idealized Β-motifs. J. Chem. Phys. 103: 10286-10297.
    • (1995) J. Chem. Phys. , vol.103 , pp. 10286-10297
    • Kolinski, A.1    Galazka, W.2    Skolnick, J.3
  • 44
    • 0032764074 scopus 로고    scopus 로고
    • Dynamics and themxodynamics of Β-hairpin assembly: Insights from various simulation techniques
    • Kolinski, A., Ilkowski, B., and Skolnick, J. 1999. Dynamics and themxodynamics of Β-hairpin assembly: Insights from various simulation techniques. Biophys. J. 77: 2942-2952.
    • (1999) Biophys. J. , vol.77 , pp. 2942-2952
    • Kolinski, A.1    Ilkowski, B.2    Skolnick, J.3
  • 45
    • 0033616587 scopus 로고    scopus 로고
    • In situ atomic force microscopy study of Alzheimer's β-amyloid peptide on different substrates: New insights into mechanism of β-sheet formation
    • Kowalewski, T. and Holtzman, D.M. 1999. In situ atomic force microscopy study of Alzheimer's β-amyloid peptide on different substrates: New insights into mechanism of β-sheet formation. Proc. Natl. Acad. Sci. 96: 3688-3693.
    • (1999) Proc. Natl. Acad. Sci. , vol.96 , pp. 3688-3693
    • Kowalewski, T.1    Holtzman, D.M.2
  • 46
    • 0024750637 scopus 로고
    • A lattice statistical mechanics model of the conformational and sequence spaces of protein
    • Lau, K.F. and Dill, K.A. 1989. A lattice statistical mechanics model of the conformational and sequence spaces of protein. Macromolecules 22: 3986-3997.
    • (1989) Macromolecules , vol.22 , pp. 3986-3997
    • Lau, K.F.1    Dill, K.A.2
  • 47
    • 0031465967 scopus 로고    scopus 로고
    • "New view" of protein folding reconciled with the old through multiple unfolding simulations
    • Lazaridis, T. and Karplus, M. 1997. "New view" of protein folding reconciled with the old through multiple unfolding simulations. Science 278: 1928-1931.
    • (1997) Science , vol.278 , pp. 1928-1931
    • Lazaridis, T.1    Karplus, M.2
  • 48
    • 0032539573 scopus 로고    scopus 로고
    • Amyloid fibrils may be assembled from β-helical protofibrils
    • Lazo, N.D. and Cowning, D.T. 1998. Amyloid fibrils may be assembled from β-helical protofibrils. Biochemistry 37: 1731-1735.
    • (1998) Biochemistry , vol.37 , pp. 1731-1735
    • Lazo, N.D.1    Cowning, D.T.2
  • 49
    • 0000936038 scopus 로고
    • The calculation of molecular vibration frequencies
    • Lindemann, F.A. 1910. The calculation of molecular vibration frequencies. Physik. Z. 11: 609-612.
    • (1910) Physik. Z. , vol.11 , pp. 609-612
    • Lindemann, F.A.1
  • 50
    • 0038679626 scopus 로고
    • Melting, freezing and colloidal suspensions
    • Löwën, H. 1994. Melting, freezing and colloidal suspensions. Phys. Rep. 237: 249-324.
    • (1994) Phys. Rep. , vol.237 , pp. 249-324
    • Löwën, H.1
  • 51
    • 0033855775 scopus 로고    scopus 로고
    • Review: Model peptides and the physicochemical approach to β-amyloids
    • Lynn, D.G. and Meredith, S.C. 2000. Review: Model peptides and the physicochemical approach to β-amyloids. J. Struct. Biol. 130: 153-173.
    • (2000) J. Struct. Biol. , vol.130 , pp. 153-173
    • Lynn, D.G.1    Meredith, S.C.2
  • 54
    • 0031158574 scopus 로고    scopus 로고
    • Transgenic analysis of prion diseases
    • Moore, R.C., and Melton, D.W. 1997. Transgenic analysis of prion diseases. Mol. Hum. Reprod. 3: 529-544.
    • (1997) Mol. Hum. Reprod. , vol.3 , pp. 529-544
    • Moore, R.C.1    Melton, D.W.2
  • 55
    • 0032568599 scopus 로고    scopus 로고
    • Folding funnels and frustration in off-lattice minimalist protein landscapes
    • Nymeyer, H., García, A.E., and Onuchic, J.N. 1998. Folding funnels and frustration in off-lattice minimalist protein landscapes. Proc. Natl. Acad. Sci. 95: 5921-5928.
    • (1998) Proc. Natl. Acad. Sci. , vol.95 , pp. 5921-5928
    • Nymeyer, H.1    García, A.E.2    Onuchic, J.N.3
  • 57
    • 0034875603 scopus 로고    scopus 로고
    • A mathematical model of the kinetics of β-amyloid fibril growth from the denatured state
    • Pallitto, M.M. and Murphy, R.M. 2001. A mathematical model of the kinetics of β-amyloid fibril growth from the denatured state. Biophys. J. 81: 1805-1822.
    • (2001) Biophys. J. , vol.81 , pp. 1805-1822
    • Pallitto, M.M.1    Murphy, R.M.2
  • 58
    • 0032539684 scopus 로고    scopus 로고
    • Is the molten globule a third phase of proteins?
    • Pande, V.S. and Rokhsar, D.S. 1998. Is the molten globule a third phase of proteins? Proc. Natl. Acad. Sci. 95: 1490-1494.
    • (1998) Proc. Natl. Acad. Sci. , vol.95 , pp. 1490-1494
    • Pande, V.S.1    Rokhsar, D.S.2
  • 59
    • 0032502839 scopus 로고    scopus 로고
    • Contact order, transition state placement and the refolding rates of single domain proteins
    • Plaxco, K.W., Simons, K.T., and Baker, D. 1998. Contact order, transition state placement and the refolding rates of single domain proteins. J. Mol. Biol. 277: 985-994.
    • (1998) J. Mol. Biol. , vol.277 , pp. 985-994
    • Plaxco, K.W.1    Simons, K.T.2    Baker, D.3
  • 60
    • 0029124248 scopus 로고
    • Molten globule and protein folding
    • Ptitsyn, O.B. 1995. Molten globule and protein folding. Adv. Protein Chem. 47: 83-230.
    • (1995) Adv. Protein Chem. , vol.47 , pp. 83-230
    • Ptitsyn, O.B.1
  • 61
    • 0032725562 scopus 로고    scopus 로고
    • The tetrameric protein transthyretin dissociates to a non-native monomer in solution: A novel model for amyloidogenesis
    • Quintas, A., Saraiva, M.J.M., and Brito, R.M.M. 1999. The tetrameric protein transthyretin dissociates to a non-native monomer in solution: A novel model for amyloidogenesis. J. Biol. Chem. 274: 32943-32949.
    • (1999) J. Biol. Chem. , vol.274 , pp. 32943-32949
    • Quintas, A.1    Saraiva, M.J.M.2    Brito, R.M.M.3
  • 62
    • 36149044755 scopus 로고
    • Molecular dynamics simulation of polymer chains with excluded volume
    • Rapaport, D.C. 1978. Molecular dynamics simulation of polymer chains with excluded volume. J. Phys. A Math. Gen. 11: L213-L216.
    • (1978) J. Phys. A Math. Gen. , vol.11
    • Rapaport, D.C.1
  • 63
    • 0028270634 scopus 로고
    • Kinetics of protein folding: A lattice model study of the requirements for folding to the native state
    • Sali, A., Shakhnovich, E.I., and Karplus, M. 1994. Kinetics of protein folding: A lattice model study of the requirements for folding to the native state. J. Mol. Biol. 235: 1614-1636.
    • (1994) J. Mol. Biol. , vol.235 , pp. 1614-1636
    • Sali, A.1    Shakhnovich, E.I.2    Karplus, M.3
  • 64
    • 0028123071 scopus 로고
    • Alzheimer's disease: A central role for amyloid
    • Selkoe, D.J. 1991. Alzheimer's disease: A central role for amyloid. J. Neuropath. Exp. Neurol. 53: 438-447.
    • (1991) J. Neuropath. Exp. Neurol. , vol.53 , pp. 438-447
    • Selkoe, D.J.1
  • 65
    • 0034718157 scopus 로고    scopus 로고
    • Alzheimer's amyloid fibrils: Structure and assembly
    • Serpell, L.C. 2000. Alzheimer's amyloid fibrils: Structure and assembly. Biochim. Biophy. Acta 1502: 16-30.
    • (2000) Biochim. Biophy. Acta , vol.1502 , pp. 16-30
    • Serpell, L.C.1
  • 66
    • 0034321011 scopus 로고    scopus 로고
    • Energetic frustration and the nature of the transition state in protein folding
    • Shea, J.-E., Onuchic, J.N., and Brooks III, C.L. 2000. Energetic frustration and the nature of the transition state in protein folding. J. Chem. Phys. 113: 7663-7671.
    • (2000) J. Chem. Phys. , vol.113 , pp. 7663-7671
    • Shea, J.-E.1    Onuchic, J.N.2    Brooks III, C.L.3
  • 67
    • 0032878322 scopus 로고    scopus 로고
    • Formation of short-lived protein aggregates directly from coil in two-state folding
    • Silow, M., Tan, Y.J., Fersht, A.R., and Oliveberg, M. 1999. Formation of short-lived protein aggregates directly from coil in two-state folding. Biochemistry 38: 13006-13012.
    • (1999) Biochemistry , vol.38 , pp. 13006-13012
    • Silow, M.1    Tan, Y.J.2    Fersht, A.R.3    Oliveberg, M.4
  • 69
    • 0025784650 scopus 로고
    • Dynamic Monte Carlo simulations of a new lattice model of globular protein folding, structure and dynamics
    • Skolnick, J. and Kolinski, A. 1991. Dynamic Monte Carlo simulations of a new lattice model of globular protein folding, structure and dynamics. J. Mol. Biol. 221: 499-531.
    • (1991) J. Mol. Biol. , vol.221 , pp. 499-531
    • Skolnick, J.1    Kolinski, A.2
  • 70
    • 0000449653 scopus 로고    scopus 로고
    • Molecular dynamic study of entangled hard-chain fluids
    • Smith, S.W., Hall, C.K., and Freeman, B.D. 1996. Molecular dynamic study of entangled hard-chain fluids. J. Chem. Phys. 104: 5616-5637.
    • (1996) J. Chem. Phys. , vol.104 , pp. 5616-5637
    • Smith, S.W.1    Hall, C.K.2    Freeman, B.D.3
  • 72
    • 11344259128 scopus 로고
    • A topographic view of super-cooled liquids and glass formation
    • Stillinger, F.H. 1995. A topographic view of super-cooled liquids and glass formation. Science 267: 1935-1939.
    • (1995) Science , vol.267 , pp. 1935-1939
    • Stillinger, F.H.1
  • 74
    • 0016696599 scopus 로고
    • Studies on protein folding, unfolding and fluctuations by computer simulation: The effect of specific amino acid sequence represented by specific inter-unit interactions
    • Taketomi, H., Ueda, Y., and Go, N. 1975. Studies on protein folding, unfolding and fluctuations by computer simulation: The effect of specific amino acid sequence represented by specific inter-unit interactions. Int. J. Pept. Protein Res. 7: 445-459.
    • (1975) Int. J. Pept. Protein Res. , vol.7 , pp. 445-459
    • Taketomi, H.1    Ueda, Y.2    Go, N.3
  • 75
    • 0017842051 scopus 로고
    • Studies on protein folding, unfolding and fluctuations by computer simulation, II: A three-dimensional lattice model of lysozyme
    • Ueda, Y., Taketomi, H., and Go, N. 1978. Studies on protein folding, unfolding and fluctuations by computer simulation, II: A three-dimensional lattice model of lysozyme. Biopolymers 17: 1531-1548.
    • (1978) Biopolymers , vol.17 , pp. 1531-1548
    • Ueda, Y.1    Taketomi, H.2    Go, N.3
  • 77
    • 0031475159 scopus 로고    scopus 로고
    • Folding thermodynamics of a model three-helix bundle protein
    • Zhou, Y. and Karplus, M. 1997a. Folding thermodynamics of a model three-helix bundle protein. Proc. Natl. Acad. Sci. 94: 14429-14432.
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , pp. 14429-14432
    • Zhou, Y.1    Karplus, M.2
  • 78
    • 0033598375 scopus 로고    scopus 로고
    • Interpreting the folding kinetics of helical proteins
    • -. 1997b. Interpreting the folding kinetics of helical proteins, Nature 401: 400-403.
    • (1997) Nature , vol.401 , pp. 400-403
  • 79
    • 0033527768 scopus 로고    scopus 로고
    • Folding of a model three-helix bundle protein: A thermodynamic and kinetic analysis
    • -. 1999. Folding of a model three-helix bundle protein: A thermodynamic and kinetic analysis. J. Mol. Biol. 293: 917-951.
    • (1999) J. Mol. Biol. , vol.293 , pp. 917-951
  • 80
    • 0001351693 scopus 로고    scopus 로고
    • First-order disorder-to-order transition in an isolated homopolymer model
    • Zhou, Y., Hall, C.K., and Karplus, M. 1996. First-order disorder-to-order transition in an isolated homopolymer model. Phys. Rev. Lett. 77: 2822-2825.
    • (1996) Phys. Rev. Lett. , vol.77 , pp. 2822-2825
    • Zhou, Y.1    Hall, C.K.2    Karplus, M.3
  • 81
    • 0001015060 scopus 로고    scopus 로고
    • Equilibrium thermodynamics of homopolymers and clusters: Molecular dynamics and Monte Carlo simulations of systems with square-well interactions
    • Zhou, Y., Karplus, M., Wichert, J.M., and Hall, C.K. 1997. Equilibrium thermodynamics of homopolymers and clusters: Molecular dynamics and Monte Carlo simulations of systems with square-well interactions. J. Chem. Phys. 107: 10691-10708.
    • (1997) J. Chem. Phys. , vol.107 , pp. 10691-10708
    • Zhou, Y.1    Karplus, M.2    Wichert, J.M.3    Hall, C.K.4
  • 82
    • 0033613906 scopus 로고    scopus 로고
    • Native proteins are surface-molten solids: Application of the Lindemann criterion for the solid versus liquid state
    • Zhou, Y., Vitkup, D., and Karplus, M. 1999. Native proteins are surface-molten solids: Application of the Lindemann criterion for the solid versus liquid state. J. Mol. Biol. 285: 1371-1375.
    • (1999) J. Mol. Biol. , vol.285 , pp. 1371-1375
    • Zhou, Y.1    Vitkup, D.2    Karplus, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.