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Volumn 87, Issue 6, 2004, Pages 4122-4134

Phase diagrams describing fibrillization by polyalanine peptides

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; PEPTIDE; POLYANILINE;

EID: 10044280719     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.104.047159     Document Type: Article
Times cited : (59)

References (62)
  • 1
    • 36849126204 scopus 로고
    • Studies in molecular dynamics. I. General method
    • Alder, B. J., and T. E. Wainwright. 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
  • 2
    • 36749107785 scopus 로고
    • Molecular dynamics simulations at constant temperature and/or pressure
    • Andersen, H. C. 1980. Molecular dynamics simulations at constant temperature and/or pressure. J. Chem. Phys. 72:2384-2393.
    • (1980) J. Chem. Phys. , vol.72 , pp. 2384-2393
    • Andersen, H.C.1
  • 3
    • 84946639640 scopus 로고
    • Molecular dynamics of rigid and non-rigid necklaces of hard discs
    • Bellemans, A., J. Orban, and D. VanBelle. 1980. Molecular dynamics of rigid and non-rigid necklaces of hard discs. Mol. Phys. 39:781-782.
    • (1980) Mol. Phys. , vol.39 , pp. 781-782
    • Bellemans, A.1    Orban, J.2    VanBelle, D.3
  • 4
    • 0030853453 scopus 로고    scopus 로고
    • Polyalanine-based peptides as models for self-associated β-sheet complexes
    • Blondelle, S. E., B. Forood, R. A. Houghten, and E. Perez-Paya. 1997. Polyalanine-based peptides as models for self-associated β-sheet complexes. Biochemistry. 36:8393-8400.
    • (1997) Biochemistry , vol.36 , pp. 8393-8400
    • Blondelle, S.E.1    Forood, B.2    Houghten, R.A.3    Perez-Paya, E.4
  • 6
    • 0024359551 scopus 로고
    • Thermal stabilities of globular proteins
    • Dill, K. A., D. O. V. Alonzo, and K. Hutchinson. 1989. Thermal stabilities of globular proteins. Biochemistry. 28:5439-5449.
    • (1989) Biochemistry , vol.28 , pp. 5439-5449
    • Dill, K.A.1    Alonzo, D.O.V.2    Hutchinson, K.3
  • 7
    • 0036228167 scopus 로고    scopus 로고
    • Exploring protein aggregation and self-propagation using lattice models: Phase diagram and kinetics
    • Dima, R. I., and D. Thirumalai. 2002. Exploring protein aggregation and self-propagation using lattice models: phase diagram and kinetics. Prot. Sci. 11:1036-1049.
    • (2002) Prot. Sci. , vol.11 , pp. 1036-1049
    • Dima, R.I.1    Thirumalai, D.2
  • 8
    • 0036923039 scopus 로고    scopus 로고
    • Molecular dynamics simulations of the SH3 domain aggregation suggests a generic amyloidogenesis mechanism
    • Ding, F., N. V. Dokholyan, S. V. Buldyrev, H. E. Stanley, and E. I. Shakhnovich. 2002. Molecular dynamics simulations of the SH3 domain aggregation suggests a generic amyloidogenesis mechanism. J. Mol. Biol. 324:851-857.
    • (2002) J. Mol. Biol. , vol.324 , pp. 851-857
    • Ding, F.1    Dokholyan, N.V.2    Buldyrev, S.V.3    Stanley, H.E.4    Shakhnovich, E.I.5
  • 10
    • 0035961329 scopus 로고    scopus 로고
    • The structural basis of protein folding and its links with human disease
    • Dobson, C. M. 2001. The structural basis of protein folding and its links with human disease. Phil. Trans. R. Soc. Lond. B. 356:133-145.
    • (2001) Phil. Trans. R. Soc. Lond. B , vol.356 , pp. 133-145
    • Dobson, C.M.1
  • 12
    • 0037048673 scopus 로고    scopus 로고
    • Solvent environment conducive to protein aggregation
    • Fernandez, A., and M. D. L. Boland. 2002. Solvent environment conducive to protein aggregation. FEBS Lett. 529:298-302.
    • (2002) FEBS Lett. , vol.529 , pp. 298-302
    • Fernandez, A.1    Boland, M.D.L.2
  • 13
    • 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:R9-23.
    • (1998) Fold. Des. , vol.3
    • Fink, A.L.1
  • 15
    • 0032729982 scopus 로고    scopus 로고
    • Computationally derived structural models of the β-amyloid found in Alzheimer's disease plaques and the interaction with possible aggregation inhibitors
    • George, A. R., and D. R. Howlett. 1999. Computationally derived structural models of the β-amyloid found in Alzheimer's disease plaques and the interaction with possible aggregation inhibitors. Biopolymers. 50:733-741.
    • (1999) Biopolymers , vol.50 , pp. 733-741
    • George, A.R.1    Howlett, D.R.2
  • 16
    • 0037627715 scopus 로고    scopus 로고
    • The role of side-chain interactions in the early steps of aggregation: Molecular dynamics simulations of an amyloid-forming peptide from the yeast prion Sup35
    • Gsponer, J., U. Haberthur, and A. Caflisch. 2003. The role of side-chain interactions in the early steps of aggregation: molecular dynamics simulations of an amyloid-forming peptide from the yeast prion Sup35. Proc. Natl. Acad. Sci. USA. 100:5154-5159.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 5154-5159
    • Gsponer, J.1    Haberthur, U.2    Caflisch, A.3
  • 17
    • 0030601851 scopus 로고    scopus 로고
    • Kinetics and thermodynamics of folding of a de novo designed four-helix bundle protein
    • Guo, Z., and D. Thirumalai. 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
    • Guo, Z.1    Thirumalai, D.2
  • 18
    • 0033582587 scopus 로고    scopus 로고
    • Thermodynamics of model prions and its implications for the problem of prion protein folding
    • Harrison, P. M., H. S. Chan, S. B. Prusiner, and F. E. Cohen. 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
  • 19
    • 0030728039 scopus 로고    scopus 로고
    • Deadly conformations-protein misfolding in prion disease
    • Horwich, A. L., and J. S. Weissman. 1997. Deadly conformations-protein misfolding in prion disease. Cell. 89:499-510.
    • (1997) Cell , vol.89 , pp. 499-510
    • Horwich, A.L.1    Weissman, J.S.2
  • 20
    • 0037259922 scopus 로고    scopus 로고
    • Supramolecular structure of helical ribbons self-assembled from a β-sheet peptide
    • Hwang, W., D. M. Marini, R. D. Kamm, and S. Zhang. 2003. Supramolecular structure of helical ribbons self-assembled from a β-sheet peptide. J. Chem. Phys. 118:389-397.
    • (2003) J. Chem. Phys. , vol.118 , pp. 389-397
    • Hwang, W.1    Marini, D.M.2    Kamm, R.D.3    Zhang, S.4
  • 21
    • 0031974669 scopus 로고    scopus 로고
    • Conformational studies of human islet amyloid peptide using molecular dynamics and simulated annealing methods
    • Dangovan, U., and A. Ramamoorthy. 1998. Conformational studies of human islet amyloid peptide using molecular dynamics and simulated annealing methods. Biopolymers. 45:9-20.
    • (1998) Biopolymers , vol.45 , pp. 9-20
    • Dangovan, U.1    Ramamoorthy, A.2
  • 22
  • 23
    • 0346688724 scopus 로고    scopus 로고
    • Assembly and kinetic folding pathways of a tetrameric β-sheet complex: Molecular dynamics simulations on simplified off-lattice protein models
    • Jang, H., C. K. Hall, and Y. Zhou. 2004a. Assembly and kinetic folding pathways of a tetrameric β-sheet complex: molecular dynamics simulations on simplified off-lattice protein models. Biophys. J. 86:31-49.
    • (2004) Biophys. J. , vol.86 , pp. 31-49
    • Jang, H.1    Hall, C.K.2    Zhou, Y.3
  • 24
    • 0347364624 scopus 로고    scopus 로고
    • Thermodynamics and stability of a β-sheet complex: Molecular dynamics simulations on simplified off-lattice protein models
    • Jang, H., C. K. Hall, and Y. Zhou. 2004b. Thermodynamics and stability of a β-sheet complex: molecular dynamics simulations on simplified off-lattice protein models. Prot. Sci. 13:40-53.
    • (2004) Prot. Sci. , vol.13 , pp. 40-53
    • Jang, H.1    Hall, C.K.2    Zhou, Y.3
  • 25
    • 0032006678 scopus 로고    scopus 로고
    • The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways
    • Kelly, J. W. 1998. The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways. Curr. Opin. Struct. Biol. 8:101-106.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 101-106
    • Kelly, J.W.1
  • 26
    • 0036238472 scopus 로고    scopus 로고
    • Towards an understanding of amyloidogenesis
    • Kelly, J. W. 2002. Towards an understanding of amyloidogenesis. Nat. Struct. Biol. 9:323-325.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 323-325
    • Kelly, J.W.1
  • 27
    • 0345818833 scopus 로고
    • Deciphering the rules of protein folding
    • King, J. 1989. Deciphering the rules of protein folding. Chem. Eng. News. 34: 32-54.
    • (1989) Chem. Eng. News , vol.34 , pp. 32-54
    • King, J.1
  • 28
    • 0022547855 scopus 로고
    • X-ray diffraction from intraneuronal paired helical filaments and extraneuronal amyloid fibers in Alzheimer disease indicates cross-β conformation
    • Kirschner, D. A., C. Abraham, and D. J. Selkoe. 1986. X-ray diffraction from intraneuronal paired helical filaments and extraneuronal amyloid fibers in Alzheimer disease indicates cross-β conformation. Proc. Natl. Acad. Sci. USA. 83:503-507.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 503-507
    • Kirschner, D.A.1    Abraham, C.2    Selkoe, D.J.3
  • 29
    • 0035832699 scopus 로고    scopus 로고
    • Effect of Ala-substitution, N- and C-terminal modification and the presence of counter ions on the structure of amyloid peptide fragment 25-35
    • Kortvelyesi, T., G. Kiss, R. F. Murphy, B. Penke, and S. Lovas. 2001. Effect of Ala-substitution, N- and C-terminal modification and the presence of counter ions on the structure of amyloid peptide fragment 25-35. J. Mol. Struct. 545:215-223.
    • (2001) J. Mol. Struct. , vol.545 , pp. 215-223
    • Kortvelyesi, T.1    Kiss, G.2    Murphy, R.F.3    Penke, B.4    Lovas, S.5
  • 31
    • 0037176280 scopus 로고    scopus 로고
    • Dynamics and fluidity of amyloid fibrils: A model of fibrous protein aggregates
    • Lakdawala, A. S., D. M. Morgan, D. C. Liotta, D. G. Lynn, and J. P. Snyder. 2002. Dynamics and fluidity of amyloid fibrils: a model of fibrous protein aggregates. J. Am. Chem. Soc. 124:15150-15151.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 15150-15151
    • Lakdawala, A.S.1    Morgan, D.M.2    Liotta, D.C.3    Lynn, D.G.4    Snyder, J.P.5
  • 32
    • 0033040551 scopus 로고    scopus 로고
    • An atomic model for the pleated β-sheet structure of Aβ amyloid protofilaments
    • Li, L., T. A. Darden, L. Bartolotti, D. Kominos, and L. G. Pedersen. 1999. An atomic model for the pleated β-sheet structure of Aβ amyloid protofilaments. Biophys. J. 76:2871-2878.
    • (1999) Biophys. J. , vol.76 , pp. 2871-2878
    • Li, L.1    Darden, T.A.2    Bartolotti, L.3    Kominos, D.4    Pedersen, L.G.5
  • 33
    • 0036784617 scopus 로고    scopus 로고
    • Molecular dynamics simulations of alanine rich β-sheet oligomers: Insight into amyloid formation
    • Ma, B., and R. Nussinov. 2002a. Molecular dynamics simulations of alanine rich β-sheet oligomers: insight into amyloid formation. Prot. Sci. 11:2335-2350.
    • (2002) Prot. Sci. , vol.11 , pp. 2335-2350
    • Ma, B.1    Nussinov, R.2
  • 35
    • 0010589011 scopus 로고    scopus 로고
    • Molecular simulation of the amyloid β-peptide Aβ (1-42) of Alzheimer's disease
    • Mager, P. P. 1998a. Molecular simulation of the amyloid β-peptide Aβ (1-42) of Alzheimer's disease. Mol. Sim. 20:201-222.
    • (1998) Mol. Sim. , vol.20 , pp. 201-222
    • Mager, P.P.1
  • 36
    • 0031766850 scopus 로고    scopus 로고
    • Molecular simulation of the primary and secondary structures of the Aβ(1-42)-peptide of Alzheimer's disease
    • Mager, P. P. 1998b. Molecular simulation of the primary and secondary structures of the Aβ(1-42)-peptide of Alzheimer's disease. Med. Res. Rev. 18:403-430.
    • (1998) Med. Res. Rev. , vol.18 , pp. 403-430
    • Mager, P.P.1
  • 37
    • 0346488919 scopus 로고    scopus 로고
    • Molecular simulation to aid in the understanding of the Aβ(1-42) peptide of Alzheimer's disease
    • Mager, P. P., R. Reinhardt, and K. Fischer. 2001. Molecular simulation to aid in the understanding of the Aβ(1-42) peptide of Alzheimer's disease. Mol. Sim. 26:367-379.
    • (2001) Mol. Sim. , vol.26 , pp. 367-379
    • Mager, P.P.1    Reinhardt, R.2    Fischer, K.3
  • 38
    • 0034901811 scopus 로고    scopus 로고
    • Probing the origins of increased activity of the E22Q Dutch mutant Alzheimer's β-amyloid peptide
    • Massi, F., and J. E. Straub. 2001a. Probing the origins of increased activity of the E22Q Dutch mutant Alzheimer's β-amyloid peptide. Biophys. J. 81:697-709.
    • (2001) Biophys. J. , vol.81 , pp. 697-709
    • Massi, F.1    Straub, J.E.2
  • 39
    • 0037472829 scopus 로고    scopus 로고
    • Structural and dynamical analysis of the hydration of the Alzheimer's β-amyloid peptide
    • Massi, F., and J. E. Straub. 2001b. Structural and dynamical analysis of the hydration of the Alzheimer's β-amyloid peptide. J. Comput. Chem. 24:143-153.
    • (2001) J. Comput. Chem. , vol.24 , pp. 143-153
    • Massi, F.1    Straub, J.E.2
  • 40
    • 0035133048 scopus 로고    scopus 로고
    • Simulation study of the structure and dynamics of the Alzheimer's amyloid peptide congener in solution
    • Massi, F., J. W. Peng, J. P. Lee, and J. E. Straub. 2001. Simulation study of the structure and dynamics of the Alzheimer's amyloid peptide congener in solution. Biophys. J. 81:31-44.
    • (2001) Biophys. J. , vol.81 , pp. 31-44
    • Massi, F.1    Peng, J.W.2    Lee, J.P.3    Straub, J.E.4
  • 41
    • 0036081257 scopus 로고    scopus 로고
    • Charge states rather than propensity for β-structure determine enhanced fibrillogenesis in wild-type Alzheimer's β-amyloid peptide compared to E22Q Dutch mutant
    • Massi, F., D. Klimov, D. Thirumalai, and J. E. Straub. 2002. Charge states rather than propensity for β-structure determine enhanced fibrillogenesis in wild-type Alzheimer's β-amyloid peptide compared to E22Q Dutch mutant. Prot. Sci. 11:1639-1647.
    • (2002) Prot. Sci. , vol.11 , pp. 1639-1647
    • Massi, F.1    Klimov, D.2    Thirumalai, D.3    Straub, J.E.4
  • 42
    • 0037381819 scopus 로고    scopus 로고
    • Simulations of human lysozyme: Probing the conformations triggering amyloidosis
    • Moraitakis, G., and J. M. Goodfellow. 2003. Simulations of human lysozyme: probing the conformations triggering amyloidosis. Biophys. J. 84:2149-2158.
    • (2003) Biophys. J. , vol.84 , pp. 2149-2158
    • Moraitakis, G.1    Goodfellow, J.M.2
  • 43
    • 7244253280 scopus 로고    scopus 로고
    • Solvent effects on the conformational transition of a model polyalanine peptide
    • Nguyen, H. D., A. J. Marchut, and C. K. Hall. 2004. Solvent effects on the conformational transition of a model polyalanine peptide. Prot. Sci. 13:2909-2924.
    • (2004) Prot. Sci. , vol.13 , pp. 2909-2924
    • Nguyen, H.D.1    Marchut, A.J.2    Hall, C.K.3
  • 44
    • 9244260521 scopus 로고    scopus 로고
    • Molecular dynamics simulations of spontaneous fibril formation
    • Nguyen, H. D., and C. K. Hall. 2004. Molecular dynamics simulations of spontaneous fibril formation. Proc. Natl. Acad. Sci. USA. 101:16180-16185.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 16180-16185
    • Nguyen, H.D.1    Hall, C.K.2
  • 45
    • 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-L217.
    • (1978) J. Phys. A Math. Gen. , vol.11
    • Rapaport, D.C.1
  • 46
    • 0000439253 scopus 로고
    • Molecular dynamics simulation of polymer chains in solution
    • Rapaport, D. C. 1979. Molecular dynamics simulation of polymer chains in solution. J. Chem. Phys. 71:3299-3303.
    • (1979) J. Chem. Phys. , vol.71 , pp. 3299-3303
    • Rapaport, D.C.1
  • 48
    • 0034272188 scopus 로고    scopus 로고
    • Temperature dependence of hydrophobic interactions: A mean force perspective, effects of water density, and nonadditivity of thermodynamic signatures
    • Shimizu, S., and H. S. Chan. 2000. Temperature dependence of hydrophobic interactions: a mean force perspective, effects of water density, and nonadditivity of thermodynamic signatures. J. Chem. Phys. 113: 4683-4700.
    • (2000) J. Chem. Phys. , vol.113 , pp. 4683-4700
    • Shimizu, S.1    Chan, H.S.2
  • 50
    • 0035882559 scopus 로고    scopus 로고
    • Alpha-helix formation: Discontinuous molecular dynamics on an intermediate-resolution protein model
    • Smith, A. V., and C. K. Hall. 2001a. Alpha-helix formation: discontinuous molecular dynamics on an intermediate-resolution protein model. Proteins Struct. Funct. Genet. 44:344-360.
    • (2001) Proteins Struct. Funct. Genet. , vol.44 , pp. 344-360
    • Smith, A.V.1    Hall, C.K.2
  • 51
    • 0035882537 scopus 로고    scopus 로고
    • Assembly of a tetrameric α-helical bundle: Computer simulations on an intermediate-resolution protein model
    • Smith, A. V., and C. K. Hall. 2001b. Assembly of a tetrameric α-helical bundle: computer simulations on an intermediate-resolution protein model. Proteins Struct. Funct. Genet. 44:376-391.
    • (2001) Proteins Struct. Funct. Genet. , vol.44 , pp. 376-391
    • Smith, A.V.1    Hall, C.K.2
  • 52
    • 0035823222 scopus 로고    scopus 로고
    • Protein refolding versus aggregation: Computer simulations on an intermediate-resolution protein model
    • Smith, A. V., and C. K. Hall. 2001c. Protein refolding versus aggregation: computer simulations on an intermediate-resolution protein model. J. Mol. Biol. 312:187-202.
    • (2001) J. Mol. Biol. , vol.312 , pp. 187-202
    • Smith, A.V.1    Hall, C.K.2
  • 53
    • 0031161658 scopus 로고    scopus 로고
    • Molecular dynamics for polymeric fluids using discontinuous potentials
    • Smith, S. W., C. K. Hall, and B. D. Freeman. 1997. Molecular dynamics for polymeric fluids using discontinuous potentials. J. Comp. Phys. 134: 16-30.
    • (1997) J. Comp. Phys. , vol.134 , pp. 16-30
    • Smith, S.W.1    Hall, C.K.2    Freeman, B.D.3
  • 54
    • 0036280438 scopus 로고    scopus 로고
    • Long time dynamic simulations: Exploring the folding pathways of an Alzheimer's amyloid Aβ-peptide
    • Straub, J. E., J. Guevara, S. Huo, and J. P. Lee. 2002. Long time dynamic simulations: exploring the folding pathways of an Alzheimer's amyloid Aβ-peptide. Acc. Chem. Res. 35:473-481.
    • (2002) Acc. Chem. Res. , vol.35 , pp. 473-481
    • Straub, J.E.1    Guevara, J.2    Huo, S.3    Lee, J.P.4
  • 55
    • 0001616080 scopus 로고    scopus 로고
    • Replica-exchange molecular dynamics method for protein folding
    • Sugita, Y., and Y. Okamoto. 1999. Replica-exchange molecular dynamics method for protein folding. Chem. Phys. Lett. 314:141-151.
    • (1999) Chem. Phys. Lett. , vol.314 , pp. 141-151
    • Sugita, Y.1    Okamoto, Y.2
  • 56
    • 0030801746 scopus 로고    scopus 로고
    • The structure of amyloid fibrils by electron microscopy and x-ray diffraction
    • Sunde, M., and C. Blake. 1997. The structure of amyloid fibrils by electron microscopy and x-ray diffraction. Adv. Prot. Chem. 50:123-159.
    • (1997) Adv. Prot. Chem. , vol.50 , pp. 123-159
    • Sunde, M.1    Blake, C.2
  • 57
    • 0028298127 scopus 로고
    • Mutations and off-pathway aggregation of proteins
    • Wetzel, R. 1994. Mutations and off-pathway aggregation of proteins. Trends Biotech. 12:193-198.
    • (1994) Trends Biotech. , vol.12 , pp. 193-198
    • Wetzel, R.1
  • 58
    • 0037907526 scopus 로고    scopus 로고
    • 55 transthyretin variant the most amyloidogenic: Insights from molecular dynamics simulations of transthyretin monomers
    • 55 transthyretin variant the most amyloidogenic: insights from molecular dynamics simulations of transthyretin monomers. Prot. Sci. 12:1222-1231.
    • (2003) Prot. Sci. , vol.12 , pp. 1222-1231
    • Yang, M.1    Lei, M.2    Huo, S.3
  • 59
    • 0038274079 scopus 로고    scopus 로고
    • The sequence dependence of fiber organization. A comparative molecular dynamics study of the islet amyloid polypeptide segments 22-27 and 22-29
    • Zanuy, D., and R. Nussinov. 2003. The sequence dependence of fiber organization. A comparative molecular dynamics study of the islet amyloid polypeptide segments 22-27 and 22-29. J. Mol. Biol. 329:565-584.
    • (2003) J. Mol. Biol. , vol.329 , pp. 565-584
    • Zanuy, D.1    Nussinov, R.2
  • 60
    • 0037339326 scopus 로고    scopus 로고
    • Short peptide amyloid organization: Stabilities and conformations of the islet amyloid peptide NFGAIL
    • Zanuy, D., B. Ma, and R. Nussinov. 2003. Short peptide amyloid organization: stabilities and conformations of the islet amyloid peptide NFGAIL. Biophys. J. 84:1884-1894.
    • (2003) Biophys. J. , vol.84 , pp. 1884-1894
    • Zanuy, D.1    Ma, B.2    Nussinov, R.3
  • 61
    • 0036377156 scopus 로고    scopus 로고
    • Amyloid-fibril formation. Proposed mechanisms and relevance to conformational disease
    • Zerovnik, E. 2002. Amyloid-fibril formation. Proposed mechanisms and relevance to conformational disease. Eur. J. Biochem. 269:3362-3371.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 3362-3371
    • Zerovnik, E.1
  • 62
    • 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., M. Karplus, J. M. Wiehert, and C. K. Hall. 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    Wiehert, J.M.3    Hall, C.K.4


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