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Volumn 99, Issue 12, 2010, Pages 3863-3869

How sequence determines elasticity of disordered proteins

Author keywords

[No Author keywords available]

Indexed keywords

ANISOPTERA (DRAGONFLIES); ARANEAE;

EID: 78650220836     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2010.10.011     Document Type: Article
Times cited : (56)

References (39)
  • 1
    • 33846250450 scopus 로고    scopus 로고
    • Proline and glycine control protein self-organization into elastomeric or amyloid fibrils
    • Rauscher, S., S. Baud,., R. Pomès. 2006. Proline and glycine control protein self-organization into elastomeric or amyloid fibrils. Structure. 14:1667-1676.
    • (2006) Structure. , vol.14 , pp. 1667-1676
    • Rauscher, S.1    Baud, S.2    Pomès, R.3
  • 2
    • 52249085709 scopus 로고    scopus 로고
    • The unfoldomics decade: An update on intrinsically disordered proteins
    • Dunker, A. K., C. J. Oldfield, ., V. Uversk. 2008. The unfoldomics decade: an update on intrinsically disordered proteins. BMC Genomics. 9:S1.
    • (2008) BMC Genomics. , vol.9
    • Dunker, A.K.1    Oldfield, C.J.2    Uversk, V.3
  • 3
    • 58149242893 scopus 로고    scopus 로고
    • Investigating by CD the molecular mechanism of elasticity of elastomeric proteins
    • Bochicchio, B., A. Pepe, and A. M. Tamburro. 2008. Investigating by CD the molecular mechanism of elasticity of elastomeric proteins. Chirality. 20:985-994.
    • (2008) Chirality. , vol.20 , pp. 985-994
    • Bochicchio, B.1    Pepe, A.2    Tamburro, A.M.3
  • 4
    • 38849119675 scopus 로고    scopus 로고
    • Structural disorder in silk proteins reveals the emergence of elastomericity
    • Dicko, C., D. Porter, ., F. Vollrath. 2008. Structural disorder in silk proteins reveals the emergence of elastomericity. Biomacromolecules. 9:216-221.
    • (2008) Biomacromolecules. , vol.9 , pp. 216-221
    • Dicko, C.1    Porter, D.2    Vollrath, F.3
  • 5
    • 33745451968 scopus 로고    scopus 로고
    • Flexible phenylalanineglycine nucleoporins as entropic barriers to nucleocytoplasmic transport
    • Lim, R. Y. H., N. P. Huang,., U. Aebi. 2006. Flexible phenylalanineglycine nucleoporins as entropic barriers to nucleocytoplasmic transport. Proc. Natl. Acad. Sci. USA. 103:9512-9517.
    • (2006) Proc. Natl. Acad. Sci. USA. , vol.103 , pp. 9512-9517
    • Lim, R.Y.H.1    Huang, N.P.2    Aebi, U.3
  • 6
    • 34249940831 scopus 로고    scopus 로고
    • Signatures of hydrophobic collapse in extended proteins captured with force spectroscopy
    • Walther, K. A., F. Gräter, ., J. M. Fernandez. 2007. Signatures of hydrophobic collapse in extended proteins captured with force spectroscopy. Proc. Natl. Acad. Sci. USA. 104:7916-7921.
    • (2007) Proc. Natl. Acad. Sci. USA. , vol.104 , pp. 7916-7921
    • Walther, K.A.1    Gräter, F.2    Fernandez, J.M.3
  • 7
    • 51349115045 scopus 로고    scopus 로고
    • Dissecting entropic coiling and poor solvent effects in protein collapse
    • Gräter, F., P. Heider, ., B. J. Berne. 2008. Dissecting entropic coiling and poor solvent effects in protein collapse. J. Am. Chem. Soc. 130:11578-11579.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 11578-11579
    • Gräter, F.1    Heider, P.2    Berne, B.J.3
  • 8
    • 0028071373 scopus 로고
    • Entropic elasticity of l-phage DNA
    • Bustamante, C., J. F. Marko, ., S. Smith. 1994. Entropic elasticity of l-phage DNA. Science. 265:1599-1600.
    • (1994) Science. , vol.265 , pp. 1599-1600
    • Bustamante, C.1    Marko, J.F.2    Smith, S.3
  • 9
    • 77953017595 scopus 로고    scopus 로고
    • Hydrophilic linkers and polar contacts affect aggregation of FG repeat peptides
    • Dölker, N., U. Zachariae, and H. Grubmüller. 2010. Hydrophilic linkers and polar contacts affect aggregation of FG repeat peptides. Biophys. J. 98:2653-2661.
    • (2010) Biophys. J. , vol.98 , pp. 2653-2661
    • Dölker, N.1    Zachariae, U.2    Grubmüller, H.3
  • 10
    • 33750701489 scopus 로고    scopus 로고
    • FG-rich repeats of nuclear pore proteins form a three-dimensional meshwork with hydrogel-like properties
    • Frey, S., R. P. Richter, and D. Görlich. 2006. FG-rich repeats of nuclear pore proteins form a three-dimensional meshwork with hydrogel-like properties. Science. 314:815-817.
    • (2006) Science. , vol.314 , pp. 815-817
    • Frey, S.1    Richter, R.P.2    Görlich, D.3
  • 11
    • 64549159284 scopus 로고    scopus 로고
    • Structural analysis of the nuclear pore complex by integrated approaches
    • Elad, N., T. Maimon, ., O. Medalia. 2009. Structural analysis of the nuclear pore complex by integrated approaches. Curr. Opin. Struct. Biol. 19:226-232.
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 226-232
    • Elad, N.1    Maimon, T.2    Medalia, O.3
  • 12
    • 61449201281 scopus 로고    scopus 로고
    • Transport-related structures and processes of the nuclear pore complex studied through molecular dynamics
    • Miao, L., and K. Schulten. 2009. Transport-related structures and processes of the nuclear pore complex studied through molecular dynamics. Structure. 17:449-459.
    • (2009) Structure. , vol.17 , pp. 449-459
    • Miao, L.1    Schulten, K.2
  • 13
    • 27144527038 scopus 로고    scopus 로고
    • Synthesis and properties of crosslinked recombinant pro-resilin
    • Elvin, C. M., A. G. Carr, ., N. E. Dixon. 2005. Synthesis and properties of crosslinked recombinant pro-resilin. Nature. 437:999-1002.
    • (2005) Nature. , vol.437 , pp. 999-1002
    • Elvin, C.M.1    Carr, A.G.2    Dixon, N.E.3
  • 14
    • 55949100825 scopus 로고    scopus 로고
    • A synthetic resilin is largely unstructured
    • Nairn, K. M., R. E. Lyons,., C. M. Elvin. 2008. A synthetic resilin is largely unstructured. Biophys. J. 95:3358-3365.
    • (2008) Biophys. J. , vol.95 , pp. 3358-3365
    • Nairn, K.M.1    Lyons, R.E.2    Elvin, C.M.3
  • 15
    • 0034866354 scopus 로고    scopus 로고
    • Tentative identification of a resilin gene in Drosophila melanogaster
    • Ardell, D. H., and S. O. Andersen. 2001. Tentative identification of a resilin gene in Drosophila melanogaster. Insect Biochem. Mol. Biol. 31:965-970.
    • (2001) Insect Biochem. Mol. Biol. , vol.31 , pp. 965-970
    • Ardell, D.H.1    Andersen, S.O.2
  • 16
    • 0035845557 scopus 로고    scopus 로고
    • Multiple conformations of PEVK proteins detected by single-molecule techniques
    • Li, H., A. F. Oberhauser, ., J. M. Fernandez. 2001. Multiple conformations of PEVK proteins detected by single-molecule techniques. Proc. Natl. Acad. Sci. USA. 98:10682-10686.
    • (2001) Proc. Natl. Acad. Sci. USA. , vol.98 , pp. 10682-10686
    • Li, H.1    Oberhauser, A.F.2    Fernandez, J.M.3
  • 17
    • 14844297706 scopus 로고    scopus 로고
    • The elasticity of individual titin PEVK exons measured by single molecule atomic force microscopy
    • Sarkar, A., S. Caamano, and J. M. Fernandez. 2005. The elasticity of individual titin PEVK exons measured by single molecule atomic force microscopy. J. Biol. Chem. 280:6261-6264.
    • (2005) J. Biol. Chem. , vol.280 , pp. 6261-6264
    • Sarkar, A.1    Caamano, S.2    Fernandez, J.M.3
  • 18
    • 0035342456 scopus 로고    scopus 로고
    • Identification of new repeating motifs in titin
    • Greaser, M. 2001. Identification of new repeating motifs in titin. Proteins. 43:145-149.
    • (2001) Proteins. , vol.43 , pp. 145-149
    • Greaser, M.1
  • 19
    • 0033377495 scopus 로고    scopus 로고
    • The mechanical design of spider silks: From fibroin sequence to mechanical function
    • Gosline, J. M., P. A. Guerette,., K. N. Savage. 1999. The mechanical design of spider silks: from fibroin sequence to mechanical function. J. Exp. Biol. 202:3295-3303.
    • (1999) J. Exp. Biol. , vol.202 , pp. 3295-3303
    • Gosline, J.M.1    Guerette, P.A.2    Savage, K.N.3
  • 20
    • 0037197885 scopus 로고    scopus 로고
    • Segmented nanofibers of spider dragline silk: Atomic force microscopy and single-molecule force spectroscopy
    • Oroudjev, E., J. Soares,., H. G. Hansma. 2002. Segmented nanofibers of spider dragline silk: atomic force microscopy and single-molecule force spectroscopy. Proc. Natl. Acad. Sci. USA. 99 (Suppl 2):6460-6465.
    • (2002) Proc. Natl. Acad. Sci. USA. , vol.99 , Issue.SUPPL 2 , pp. 6460-6465
    • Oroudjev, E.1    Soares., J.2    Hansma, H.G.3
  • 22
    • 33645941402 scopus 로고
    • The OPLS [optimized potentials for liquid simulations] potential functions for proteins, energy minimizations for crystals of cyclic peptides and crambin
    • Jorgensen, W. L., and J. Tirado-Rives. 1988. The OPLS [optimized potentials for liquid simulations] potential functions for proteins, energy minimizations for crystals of cyclic peptides and crambin. J. Am. Chem. Soc. 110:1657-1666.
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 1657-1666
    • Jorgensen, W.L.1    Tirado-Rives, J.2
  • 23
    • 0004016501 scopus 로고
    • Comparison of simple potential functions for simulating liquid water
    • Jorgensen, W. L., J. Chandrasekhar, and J. D. Madura. 1983. Comparison of simple potential functions for simulating liquid water. J. Chem. Phys. 79:926-935.
    • (1983) J. Chem. Phys. , vol.79 , pp. 926-935
    • Jorgensen, W.L.1    Chandrasekhar, J.2    Madura, J.D.3
  • 26
    • 0004067382 scopus 로고
    • Reidel, Dordrecht, The Netherlands
    • Bernard, P., editor. 1981. Intermolecular Forces. Reidel, Dordrecht, The Netherlands.
    • (1981) Intermolecular Forces
    • Bernard, P.1
  • 27
    • 33645104033 scopus 로고    scopus 로고
    • Force field evaluation for biomolecular simulation: Free enthalpies of solvation of polar and apolar compounds in various solvents
    • Geerke, D. P., andW. F. van Gunsteren. 2006. Force field evaluation for biomolecular simulation: free enthalpies of solvation of polar and apolar compounds in various solvents. ChemPhysChem. 7:671-678.
    • (2006) ChemPhysChem. , vol.7 , pp. 671-678
    • Geerke, D.P.1    Van Gunsteren, W.F.2
  • 28
    • 4444282928 scopus 로고    scopus 로고
    • A biomolecular force field based on the free enthalpy of hydration and solvation: The GROMOS force-field parameter sets 53A5 and 53A6
    • Oostenbrink, C., A. Villa, ., W. F. van Gunsteren. 2004. A biomolecular force field based on the free enthalpy of hydration and solvation: the GROMOS force-field parameter sets 53A5 and 53A6. J. Comput. Chem. 25:1656-1676.
    • (2004) J. Comput. Chem. , vol.25 , pp. 1656-1676
    • Oostenbrink, C.1    Villa, A.2    Van Gunsteren, W.F.3
  • 29
    • 0142250484 scopus 로고    scopus 로고
    • Calculation of the watercyclohexane transfer free energies of neutral amino acid side-chain analogs using the OPLS all-atom force field
    • MacCallum, J. L., and D. P. Tieleman. 2003. Calculation of the watercyclohexane transfer free energies of neutral amino acid side-chain analogs using the OPLS all-atom force field. J. Comput. Chem. 24:1930-1935.
    • (2003) J. Comput. Chem. , vol.24 , pp. 1930-1935
    • MacCallum, J.L.1    Tieleman, D.P.2
  • 30
    • 84986519238 scopus 로고
    • The weighted histogram analysis method for free-energy calculations on biomolecules. I. the method
    • Kumar, S., J. M. Rosenberg, ., P. A. Kollman. 1992. The weighted histogram analysis method for free-energy calculations on biomolecules. I. The method. J. Comput. Chem. 13:1011-1021.
    • (1992) J. Comput. Chem. , vol.13 , pp. 1011-1021
    • Kumar, S.1    Rosenberg, J.M.2    Kollman, P.A.3
  • 31
    • 36849103820 scopus 로고
    • Role of repulsive forces in determining the equilibrium structure of simple liquids
    • Weeks, J. D., D. Chandler, and H. C. Andersen. 1971. Role of repulsive forces in determining the equilibrium structure of simple liquids. J. Chem. Phys. 54:5237-5247.
    • (1971) J. Chem. Phys. , vol.54 , pp. 5237-5247
    • Weeks, J.D.1    Chandler, D.2    Andersen, H.C.3
  • 32
    • 38949197123 scopus 로고    scopus 로고
    • Proline and processing of spider silks
    • Liu, Y., A. Sponner, ., F. Vollrath. 2008. Proline and processing of spider silks. Biomacromolecules. 9:116-121.
    • (2008) Biomacromolecules. , vol.9 , pp. 116-121
    • Liu, Y.1    Sponner, A.2    Vollrath, F.3
  • 33
    • 47749135624 scopus 로고    scopus 로고
    • The role of proline in the elastic mechanism of hydrated spider silks
    • Savage, K. N., and J. M. Gosline. 2008. The role of proline in the elastic mechanism of hydrated spider silks. J. Exp. Biol. 211:1948-1957.
    • (2008) J. Exp. Biol. , vol.211 , pp. 1948-1957
    • Savage, K.N.1    Gosline, J.M.2
  • 34
    • 0036035968 scopus 로고    scopus 로고
    • Polyproline II structure in proteins: Identification by chiroptical spectroscopies, stability, and functions
    • Bochicchio, B., and A. M. Tamburro. 2002. Polyproline II structure in proteins: identification by chiroptical spectroscopies, stability, and functions. Chirality. 14:782-792.
    • (2002) Chirality. , vol.14 , pp. 782-792
    • Bochicchio, B.1    Tamburro, A.M.2
  • 35
    • 23844465902 scopus 로고    scopus 로고
    • Unusual compactness of a polyproline type II structure
    • Zagrovic, B., J. Lipfert, ., V. S. Pande. 2005. Unusual compactness of a polyproline type II structure. Proc. Natl. Acad. Sci. USA. 102: 11698-11703.
    • (2005) Proc. Natl. Acad. Sci. USA. , vol.102 , pp. 11698-11703
    • Zagrovic, B.1    Lipfert, J.2    Pande, V.S.3
  • 36
    • 0036129072 scopus 로고    scopus 로고
    • Polyproline II helical structure in protein unfolded states: Lysine peptides revisited
    • Rucker, A. L., and T. P. Creamer. 2002. Polyproline II helical structure in protein unfolded states: lysine peptides revisited. Protein Sci. 11:980-985.
    • (2002) Protein Sci. , vol.11 , pp. 980-985
    • Rucker, A.L.1    Creamer, T.P.2
  • 37
    • 14944346760 scopus 로고    scopus 로고
    • Effect of proline and glycine residues on dynamics and barriers of loop formation in polypeptide chains
    • Krieger, F., A. Möglich, and T. Kiefhaber. 2005. Effect of proline and glycine residues on dynamics and barriers of loop formation in polypeptide chains. J. Am. Chem. Soc. 127:3346-3352.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 3346-3352
    • Krieger, F.1    Möglich, A.2    Kiefhaber, T.3
  • 38
    • 47749138891 scopus 로고    scopus 로고
    • The effect of proline on the network structure of major ampullate silks as inferred from their mechanical and optical properties
    • Savage, K. N., and J. M. Gosline. 2008. The effect of proline on the network structure of major ampullate silks as inferred from their mechanical and optical properties. J. Exp. Biol. 211:1937-1947.
    • (2008) J. Exp. Biol. , vol.211 , pp. 1937-1947
    • Savage, K.N.1    Gosline, J.M.2
  • 39
    • 77951645923 scopus 로고    scopus 로고
    • Sequence determinants of compaction in intrinsically disordered proteins
    • Marsh, J. A., and J. D. Forman-Kay. 2010. Sequence determinants of compaction in intrinsically disordered proteins. Biophys. J. 98: 2383-2390.
    • (2010) Biophys. J. , vol.98 , pp. 2383-2390
    • Marsh, J.A.1    Forman-Kay, J.D.2


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