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Volumn 9, Issue 76, 2012, Pages 2911-2922

Pseudoelastic behaviour of a natural material is achieved via reversible changes in protein backbone conformation

Author keywords

Biopolymer; Coiled coil; Conformation; Protein; Pseudoelasticity

Indexed keywords

BIOMOLECULES; BIOPOLYMERS; CONFORMATIONS; POLYMERS; SHELLFISH;

EID: 84867471533     PISSN: 17425689     EISSN: 17425662     Source Type: Journal    
DOI: 10.1098/rsif.2012.0310     Document Type: Article
Times cited : (36)

References (36)
  • 1
    • 0000136773 scopus 로고
    • Role of encapsulation in invertebrate life histories
    • doi:10.1086/283533
    • Pechenik, J. A. 1979 Role of encapsulation in invertebrate life histories. Am. Nat. 114, 859-870. (doi:10.1086/283533)
    • (1979) Am. Nat. , vol.114 , pp. 859-870
    • Pechenik, J.A.1
  • 2
    • 0036163639 scopus 로고    scopus 로고
    • Mechanical characterization of an unusual elastic biomaterial from the egg capsules of marine snails (Busycon spp.)
    • doi:10.1021/bm0155470
    • Rapoport, H. S. & Shadwick, R. E. 2002 Mechanical characterization of an unusual elastic biomaterial from the egg capsules of marine snails (Busycon spp.). Biomacromolecules 3, 42-50. (doi:10.1021/bm0155470)
    • (2002) Biomacromolecules , vol.3 , pp. 42-50
    • Rapoport, H.S.1    Shadwick, R.E.2
  • 3
    • 33746029122 scopus 로고    scopus 로고
    • Adaptations to physical stresses in the intertidal zone: The egg capsules of neogastropod molluscs
    • doi:10.1093/icb/39.2.230
    • Rawlings, T. A. 1999 Adaptations to physical stresses in the intertidal zone: the egg capsules of neogastropod molluscs. Am. Zool. 39, 230-243. (doi:10.1093/icb/39.2.230)
    • (1999) Am. Zool. , vol.39 , pp. 230-243
    • Rawlings, T.A.1
  • 4
    • 80052950582 scopus 로고    scopus 로고
    • Superelasticity and self-healing of proteinaceous biomaterials
    • doi:10.1016/j.proeng.2011.04.432
    • Kazakevicuite-Makovska, R. & Steeb, H. 2011 Superelasticity and self-healing of proteinaceous biomaterials. Proc. Eng. 10, 2597-2602. (doi:10.1016/j.proeng.2011.04.432)
    • (2011) Proc. Eng. , vol.10 , pp. 2597-2602
    • Kazakevicuite-Makovska, R.1    Steeb, H.2
  • 5
    • 70350575287 scopus 로고    scopus 로고
    • Non-entropic and reversible long-range deformation of an encapsulating bioelastomer
    • doi:10.1038/ nmat2547
    • Miserez, A., Wasko, S. S., Carpenter, C. F. & Waite, J. H. 2009 Non-entropic and reversible long-range deformation of an encapsulating bioelastomer. Nat. Mater. 8, 910-916. (doi:10.1038/ nmat2547)
    • (2009) Nat. Mater. , vol.8 , pp. 910-916
    • Miserez, A.1    Wasko, S.S.2    Carpenter, C.F.3    Waite, J.H.4
  • 7
    • 0034890493 scopus 로고    scopus 로고
    • Comparison of the spinning of selachian egg case ply sheets and orb web spider dragline filaments
    • doi:10.1021/ bm0001446
    • Knight, D. P. & Vollrath, F. 2001 Comparison of the spinning of selachian egg case ply sheets and orb web spider dragline filaments. Biomacromolecules 2, 323-334. (doi:10.1021/ bm0001446)
    • (2001) Biomacromolecules , vol.2 , pp. 323-334
    • Knight, D.P.1    Vollrath, F.2
  • 8
    • 1042302712 scopus 로고    scopus 로고
    • Molecular design of the a-keratin composite: Insights from a matrix-free model, hagfish slime threads
    • doi:10.1098/ rspb.2003.2591
    • Fudge, D. S. & Gosline, J. M. 2004 Molecular design of the a-keratin composite: insights from a matrix-free model, hagfish slime threads. Proc. R. Soc. Lond. B 271, 291-299. (doi:10.1098/ rspb.2003.2591)
    • (2004) Proc. R. Soc. Lond. B , vol.271 , pp. 291-299
    • Fudge, D.S.1    Gosline, J.M.2
  • 9
    • 0035252931 scopus 로고    scopus 로고
    • Coiled coils: A highly versatile protein folding motif
    • doi:10.1016/S0962-8924(00)01898-5
    • Burkhard, P., Stetefeld, J. & Strelkov, S. V. 2001 Coiled coils: a highly versatile protein folding motif. Trends Cell Biol. 11, 82-88. (doi:10.1016/S0962-8924(00)01898-5)
    • (2001) Trends Cell Biol. , vol.11 , pp. 82-88
    • Burkhard, P.1    Stetefeld, J.2    Strelkov, S.V.3
  • 10
    • 0041319662 scopus 로고    scopus 로고
    • The mechanical properties of hydrated intermediate filaments: Insights from hagfish slime threads
    • doi:10.1016/S0006-3495(03)74629-3
    • Fudge, D. S., Gardner, K. H., Forsyth, V. T., Riekel, C. & Gosline, J. M. 2003 The mechanical properties of hydrated intermediate filaments: insights from hagfish slime threads. Biophys. J. 85, 2015-2027. (doi:10.1016/S0006-3495(03)74629-3)
    • (2003) Biophys. J. , vol.85 , pp. 2015-2027
    • Fudge, D.S.1    Gardner, K.H.2    Forsyth, V.T.3    Riekel, C.4    Gosline, J.M.5
  • 11
    • 3042816944 scopus 로고    scopus 로고
    • New aspects of the a-helix to b-sheet transition in stretched hard a-keratin fibers
    • doi:10.1529/biophysj.103.036749
    • Kreplak, L., Doucet, J., Dumas, P. & Briki, F. 2004 New aspects of the a-helix to b-sheet transition in stretched hard a-keratin fibers. Biophys. J. 87, 640-647. (doi:10.1529/biophysj.103.036749)
    • (2004) Biophys. J. , vol.87 , pp. 640-647
    • Kreplak, L.1    Doucet, J.2    Dumas, P.3    Briki, F.4
  • 12
    • 0036977558 scopus 로고    scopus 로고
    • The myosin coiled-coil is a truly elastic protein structure
    • doi:10.1038/nmat776
    • Schwaiger, I., Sattler, C., Hostetter, D. R. & Rief, M. 2002 The myosin coiled-coil is a truly elastic protein structure. Nat. Mater. 1, 232-235. (doi:10.1038/nmat776)
    • (2002) Nat. Mater. , vol.1 , pp. 232-235
    • Schwaiger, I.1    Sattler, C.2    Hostetter, D.R.3    Rief, M.4
  • 13
    • 33847774117 scopus 로고    scopus 로고
    • Forced unfolding of coiled-coils in fibrinogen by single-molecule AFM
    • doi:10.1529/biophysj.106.101261
    • Brown, A. E. X., Litvinov, R. I., Discher, D. E. & Weisel, J.W. 2007 Forced unfolding of coiled-coils in fibrinogen by single-molecule AFM. Biophys. J. 92, L39-L41. (doi:10.1529/biophysj.106.101261)
    • (2007) Biophys. J. , vol.92
    • Brown, A.E.X.1    Litvinov, R.I.2    Discher, D.E.3    Weisel, J.W.4
  • 14
    • 40049099583 scopus 로고    scopus 로고
    • Molecular basis of fibrin clot elasticity
    • doi:10.1016/j.str.2007.12.019
    • Lim, B. B. C., Lee, E. H., Sotomayor, M. & Schulten, K. 2008 Molecular basis of fibrin clot elasticity. Structure 16, 449-459. (doi:10.1016/j.str.2007.12.019)
    • (2008) Structure , vol.16 , pp. 449-459
    • Lim, B.B.C.1    Lee, E.H.2    Sotomayor, M.3    Schulten, K.4
  • 15
    • 70350747497 scopus 로고    scopus 로고
    • Designing the folding mechanics of coiled coils
    • doi:10.1002/cphc.200900575
    • Bornschlögl, T., Gebhardt, J. C. M. & Rief, M. 2009 Designing the folding mechanics of coiled coils. Chemphyschem 10, 2800-2804. (doi:10.1002/cphc.200900575)
    • (2009) Chemphyschem , vol.10 , pp. 2800-2804
    • Bornschlögl, T.1    Gebhardt, J.C.M.2    Rief, M.3
  • 16
    • 33845199750 scopus 로고    scopus 로고
    • Cooperative deformation of mineral and collagen in bone at the nanoscale
    • doi:10.1073/pnas.0604237103
    • Gupta, H. S., Seto, J., Wagermaier, W., Zaslansky, P., Boesecke, P. & Fratzl, P. 2006 Cooperative deformation of mineral and collagen in bone at the nanoscale. Proc. Natl Acad. Sci. USA 103, 17 741-17 746. (doi:10.1073/pnas. 0604237103)
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 17741-17746
    • Gupta, H.S.1    Seto, J.2    Wagermaier, W.3    Zaslansky, P.4    Boesecke, P.5    Fratzl, P.6
  • 17
    • 34248388591 scopus 로고    scopus 로고
    • A new experimental station for simultaneous X-ray microbeam scanning for small- And wide-angle scattering and fluorescence at BESSY II
    • doi:10.1107/S0021889806045444
    • Paris, O., Li, C. H., Siegel, S., Weseloh, G., Emmerling, F., Riesemeier, H., Erko, A. & Fratzl, P. 2007 A new experimental station for simultaneous X-ray microbeam scanning for small- and wide-angle scattering and fluorescence at BESSY II. J. Appl. Crystallogr. 40, S466-S470. (doi:10.1107/ S0021889806045444)
    • (2007) J. Appl. Crystallogr. , vol.40
    • Paris, O.1    Li, C.H.2    Siegel, S.3    Weseloh, G.4    Emmerling, F.5    Riesemeier, H.6    Erko, A.7    Fratzl, P.8
  • 19
    • 33748297414 scopus 로고    scopus 로고
    • Orientation-insensitive spectra for Raman microspectroscopy
    • doi:10.1366/000370206778062039
    • Lefevre, T., Rousseau, M. E. & Pezolet, M. 2006 Orientation- insensitive spectra for Raman microspectroscopy. Appl. Spectrosc. 60, 841-846. (doi:10.1366/000370206778062039)
    • (2006) Appl. Spectrosc. , vol.60 , pp. 841-846
    • Lefevre, T.1    Rousseau, M.E.2    Pezolet, M.3
  • 20
    • 33846469974 scopus 로고    scopus 로고
    • Reversibly labile, sclerotization-induced elastic properties in a keratin analog from marine snails: Whelk egg capsule biopolymer (WECB)
    • doi:10.1242/jeb.02613
    • Rapoport, H. S. & Shadwick, R. E. 2007 Reversibly labile, sclerotization-induced elastic properties in a keratin analog from marine snails: whelk egg capsule biopolymer (WECB). J. Exp. Biol. 210, 12-26. (doi:10.1242/jeb.02613)
    • (2007) J. Exp. Biol. , vol.210 , pp. 12-26
    • Rapoport, H.S.1    Shadwick, R.E.2
  • 21
    • 0026507761 scopus 로고
    • Amide modes and protein conformation
    • doi:10.1016/0167-4838(92)90261-B
    • Bandekar, J. 1992 Amide modes and protein conformation. Biochim. Biophys. Acta 1120, 123-143. (doi:10.1016/0167-4838(92)90261-B)
    • (1992) Biochim. Biophys. Acta , vol.1120 , pp. 123-143
    • Bandekar, J.1
  • 22
    • 78651105014 scopus 로고    scopus 로고
    • Redrawing the Ramachandran plot after inclusion of hydrogen-bonding constraints
    • doi:10.1073/pnas.1014674107
    • Porter, L. L. & Rose, G. D. 2011 Redrawing the Ramachandran plot after inclusion of hydrogen-bonding constraints. Proc. Natl Acad. Sci. USA 108, 109-113. (doi:10.1073/pnas.1014674107)
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 109-113
    • Porter, L.L.1    Rose, G.D.2
  • 23
    • 34248197448 scopus 로고    scopus 로고
    • Nanomechanics of single keratin fibres: A Raman study of the α-helix → β-sheet transition and the effect of water
    • doi:10.1002/jrs.1672
    • Paquin, R. & Colomban, P. 2007 Nanomechanics of single keratin fibres: a Raman study of the α-helix → β-sheet transition and the effect of water. J. Raman Spectrosc. 38, 504-514. (doi:10.1002/jrs.1672)
    • (2007) J. Raman Spectrosc. , vol.38 , pp. 504-514
    • Paquin, R.1    Colomban, P.2
  • 24
    • 34548727333 scopus 로고    scopus 로고
    • Raman spectroscopy of biological tissues
    • doi:10.1080/05704920701551530
    • Movasaghi, Z., Rehman, S. & Rehman, I. U. 2007 Raman spectroscopy of biological tissues. Appl. Spectrosc. Rev. 42, 493-541. (doi:10.1080/ 05704920701551530)
    • (2007) Appl. Spectrosc. Rev. , vol.42 , pp. 493-541
    • Movasaghi, Z.1    Rehman, S.2    Rehman, I.U.3
  • 25
    • 32544446167 scopus 로고    scopus 로고
    • Peptide secondary structure folding reaction coordinate: Correlation between UV Raman amide III frequency, ψ Ramachandran angle, and hydrogen bonding
    • doi:10.1021/jp054593h
    • Mikhonin, A. V., Bykov, S. V., Myshakina, N. S. & Asher, S.A. 2006 Peptide secondary structure folding reaction coordinate: correlation between UV Raman amide III frequency, ψ Ramachandran angle, and hydrogen bonding. J. Phys. Chem. B 110, 1928-1943. (doi:10.1021/jp054593h)
    • (2006) J. Phys. Chem. B , vol.110 , pp. 1928-1943
    • Mikhonin, A.V.1    Bykov, S.V.2    Myshakina, N.S.3    Asher, S.A.4
  • 26
    • 0035965724 scopus 로고    scopus 로고
    • Dihedral ψ angle dependence of the amide III vibration: A uniquely sensitive UV resonance Raman secondary structural probe
    • doi:10.1021/ja0039738
    • Asher, S. A., Ianoul, A., Mix, G., Boyden, M. N., Karnoup, A., Diem, M. & Schweitzer-Stenner, R. 2001 Dihedral ψ angle dependence of the amide III vibration: a uniquely sensitive UV resonance Raman secondary structural probe. J. Am. Chem. Soc. 123, 11 775-11 781. (doi:10.1021/ja0039738)
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 11775-11781
    • Asher, S.A.1    Ianoul, A.2    Mix, G.3    Boyden, M.N.4    Karnoup, A.5    Diem, M.6    Schweitzer-Stenner, R.7
  • 29
    • 0010868253 scopus 로고
    • Disorder-driven first order phase transformations: A model for hysteresis
    • doi:10.1063/ 1.355522
    • Dahmen, K., Kartha, S., Krumhansl, J. A., Roberts, B. W., Sethna, J. P. & Shore, J. D. 1994 Disorder-driven first order phase transformations: a model for hysteresis. J. Appl. Phys. 75, 5946-5948. (doi:10.1063/ 1.355522)
    • (1994) J. Appl. Phys. , vol.75 , pp. 5946-5948
    • Dahmen, K.1    Kartha, S.2    Krumhansl, J.A.3    Roberts, B.W.4    Sethna, J.P.5    Shore, J.D.6
  • 30
    • 0000526768 scopus 로고
    • Hysteresis and hierearchies: Dynamics of disorder-driven first order phase transformations
    • doi:10.1103/ PhysRevLett.70.3347
    • Sethna, J. P., Dahmen, K., Kartha, S., Krumhansl, J. A., Roberts, B. W. & Shore, J. D. 1993 Hysteresis and hierearchies: dynamics of disorder-driven first order phase transformations. Phys. Rev. Lett. 70, 3347-3350. (doi:10.1103/ PhysRevLett.70.3347)
    • (1993) Phys. Rev. Lett. , vol.70 , pp. 3347-3350
    • Sethna, J.P.1    Dahmen, K.2    Kartha, S.3    Krumhansl, J.A.4    Roberts, B.W.5    Shore, J.D.6
  • 32
    • 1242319505 scopus 로고    scopus 로고
    • Modular domain structure: A biomimetic strategy for advanced polymeric materials
    • doi:10.1021/ja039127p
    • Guan, Z. B., Roland, J. T., Bai, J. Z., Ma, S. X., McIntire, T. M. & Nguyen, M. 2004 Modular domain structure: a biomimetic strategy for advanced polymeric materials. J. Am. Chem. Soc. 126, 2058-2065. (doi:10.1021/ja039127p)
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 2058-2065
    • Guan, Z.B.1    Roland, J.T.2    Bai, J.Z.3    Ma, S.X.4    McIntire, T.M.5    Nguyen, M.6
  • 34
    • 0028071373 scopus 로고
    • Entropic elasticity of lambda-phage DNA
    • doi:10.1126/science.8079175
    • Bustamante, C., Marko, J. F., Siggia, E. D. & Smith, S. 1994 Entropic elasticity of lambda-phage DNA. Science 265, 1599-1600. (doi:10.1126/science. 8079175)
    • (1994) Science , vol.265 , pp. 1599-1600
    • Bustamante, C.1    Marko, J.F.2    Siggia, E.D.3    Smith, S.4
  • 36
    • 0000579305 scopus 로고    scopus 로고
    • DNA persistence length revisited
    • doi:10.1002/ bip.10151
    • Lu, Y. J., Weers, B. & Stellwagen, N. C. 2001 DNA persistence length revisited. Biopolymers 61, 261-275. (doi:10.1002/ bip.10151)
    • (2001) Biopolymers , vol.61 , pp. 261-275
    • Lu, Y.J.1    Weers, B.2    Stellwagen, N.C.3


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