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Volumn 90, Issue 4, 2006, Pages 1411-1418

Sacrificial bonds and hidden length: Unraveling molecular mesostructures in tough materials

Author keywords

[No Author keywords available]

Indexed keywords

BIOMATERIAL; POLYMER; AGGRECAN; ALUMINUM SILICATE; GLUTEN; HYALURONIC ACID; LECTIN; MICA; PROTEOCHONDROITIN SULFATE; SCLEROPROTEIN;

EID: 33645765584     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.105.069344     Document Type: Article
Times cited : (286)

References (38)
  • 2
    • 0034844170 scopus 로고    scopus 로고
    • 3D finite element modeling of mechanical response in nacre-based hybrid nanocomposites
    • Katti, D. R., K. S. Katti, J. M. Sopp, and M. Sarikaya. 2001. 3D finite element modeling of mechanical response in nacre-based hybrid nanocomposites. Comput. Theor. Polym. Sci. 11:397-404.
    • (2001) Comput. Theor. Polym. Sci. , vol.11 , pp. 397-404
    • Katti, D.R.1    Katti, K.S.2    Sopp, J.M.3    Sarikaya, M.4
  • 3
    • 0035233869 scopus 로고    scopus 로고
    • Why is nacre strong? Elastic theory and fracture mechanics for biocomposites with stratified structures
    • Okumura, K., and P. G. de Gennes. 2001. Why is nacre strong? Elastic theory and fracture mechanics for biocomposites with stratified structures. Eur. Phys. J. E. 4:121-127.
    • (2001) Eur. Phys. J. E , vol.4 , pp. 121-127
    • Okumura, K.1    De Gennes, P.G.2
  • 5
    • 11244313019 scopus 로고    scopus 로고
    • On the role of interface polymers for the mechanics of natural polymeric composites
    • Fratzl, P., I. Burgert, and H. S. Gupta. 2004. On the role of interface polymers for the mechanics of natural polymeric composites. Phys. Chem. Chem. Phys. 6:5575-5579.
    • (2004) Phys. Chem. Chem. Phys. , vol.6 , pp. 5575-5579
    • Fratzl, P.1    Burgert, I.2    Gupta, H.S.3
  • 8
    • 0037197885 scopus 로고    scopus 로고
    • Segmented nanofibers of spider dragline silk: Atomic force microscopy and single-molecule force spectroscopy
    • Oroudjev, E., J. Soares, S. Arcdiacono, J. B. Thompson, S. A. Fossey, and H. G. Hansma. 2002. Segmented nanofibers of spider dragline silk: atomic force microscopy and single-molecule force spectroscopy. Proc. Natl. Acad. Sci. USA. 99:6460-6465.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 6460-6465
    • Oroudjev, E.1    Soares, J.2    Arcdiacono, S.3    Thompson, J.B.4    Fossey, S.A.5    Hansma, H.G.6
  • 9
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by AFM
    • Rief, M., M. Gautel, F. Oesterhelt, J. M. Fernandez, and H. E. Gaub. 1997. Reversible unfolding of individual titin immunoglobulin domains by AFM. Science. 276:1109-1112.
    • (1997) Science , vol.276 , pp. 1109-1112
    • Rief, M.1    Gautel, M.2    Oesterhelt, F.3    Fernandez, J.M.4    Gaub, H.E.5
  • 10
    • 0031767965 scopus 로고    scopus 로고
    • The mechanical stability of immunoglobulin and fibronectin III domains in the muscle protein titin measured by atomic force microscopy
    • Rief, M., M. Gautel, A. Schemmel, and H. E. Gaub. 1998. The mechanical stability of immunoglobulin and fibronectin III domains in the muscle protein titin measured by atomic force microscopy. Biophys. J. 75:3008-3014.
    • (1998) Biophys. J. , vol.75 , pp. 3008-3014
    • Rief, M.1    Gautel, M.2    Schemmel, A.3    Gaub, H.E.4
  • 14
    • 0033817704 scopus 로고    scopus 로고
    • Stretching single molecules into novel conformations using the atomic force microscope
    • Fisher, T. E., P. E. Marszalek, and J. M. Fernandez. 2000. Stretching single molecules into novel conformations using the atomic force microscope. Nat. Struct. Biol. 7:719-724.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 719-724
    • Fisher, T.E.1    Marszalek, P.E.2    Fernandez, J.M.3
  • 15
    • 2142758179 scopus 로고    scopus 로고
    • Force spectroscopy of collagen fibers to investigate their mechanical properties and structural organization
    • Gutsmann, T., G. E. Fantner, J. H. Kindt, M. Venturoni, S. Danielsen, and P. K. Hansma. 2004. Force spectroscopy of collagen fibers to investigate their mechanical properties and structural organization. Biophys. J. 86:3186-3193.
    • (2004) Biophys. J. , vol.86 , pp. 3186-3193
    • Gutsmann, T.1    Fantner, G.E.2    Kindt, J.H.3    Venturoni, M.4    Danielsen, S.5    Hansma, P.K.6
  • 17
    • 0028071373 scopus 로고
    • Entropic elasticity of lambda-phage DNA
    • Bustamante, C., J. F. Marko, E. D. Siggia, and S. Smith. 1994. Entropic elasticity of lambda-phage DNA. Science. 265:1599-1600.
    • (1994) Science , vol.265 , pp. 1599-1600
    • Bustamante, C.1    Marko, J.F.2    Siggia, E.D.3    Smith, S.4
  • 18
    • 0032542229 scopus 로고    scopus 로고
    • Polysaccharide elasticity governed by chair-boat transitions of the glucopyranose ring
    • Marszalek, P. E., A. F. Oberhauser, Y. P. Pang, and J. M. Fernandez. 1998. Polysaccharide elasticity governed by chair-boat transitions of the glucopyranose ring. Nature. 396:661-664.
    • (1998) Nature , vol.396 , pp. 661-664
    • Marszalek, P.E.1    Oberhauser, A.F.2    Pang, Y.P.3    Fernandez, J.M.4
  • 19
    • 0032937079 scopus 로고    scopus 로고
    • Estimating the persistence length of a worm-like chain molecule from force-extension measurements
    • Bouchiat, C., M. D. Wang, J. F. Allemand, T. Strick, S. M. Block, and V. Croquette. 1999. Estimating the persistence length of a worm-like chain molecule from force-extension measurements. Biophys. J. 76:409-413.
    • (1999) Biophys. J. , vol.76 , pp. 409-413
    • Bouchiat, C.1    Wang, M.D.2    Allemand, J.F.3    Strick, T.4    Block, S.M.5    Croquette, V.6
  • 21
    • 0036385794 scopus 로고    scopus 로고
    • The backbone conformational entropy of protein folding: Experimental measures from atomic force microscopy
    • Thompson, J. B., H. G. Hansma, P. K. Hansma, and K. W. Plaxco. 2002. The backbone conformational entropy of protein folding: experimental measures from atomic force microscopy. J. Mol. Biol. 322:645-652.
    • (2002) J. Mol. Biol. , vol.322 , pp. 645-652
    • Thompson, J.B.1    Hansma, H.G.2    Hansma, P.K.3    Plaxco, K.W.4
  • 22
    • 0033582763 scopus 로고    scopus 로고
    • Single molecule force spectroscopy of spectrin repeats: Low unfolding forces in helix bundles
    • Rief, M., J. Pascual, M. Saraste, and H. E. Gaub. 1999. Single molecule force spectroscopy of spectrin repeats: low unfolding forces in helix bundles. J. Mol. Biol. 286:553-561.
    • (1999) J. Mol. Biol. , vol.286 , pp. 553-561
    • Rief, M.1    Pascual, J.2    Saraste, M.3    Gaub, H.E.4
  • 26
    • 3142719907 scopus 로고    scopus 로고
    • Investigation of polyelectrolyte desorption by single molecule force spectroscopy
    • Friedsam, C., M. Seitz, and H. E. Gaub. 2004. Investigation of polyelectrolyte desorption by single molecule force spectroscopy. J. Phys. Condens. Matter. 16:S2369-S2382.
    • (2004) J. Phys. Condens. Matter. , vol.16
    • Friedsam, C.1    Seitz, M.2    Gaub, H.E.3
  • 28
    • 0036198476 scopus 로고    scopus 로고
    • Unzipping DNA with optical tweezers: High sequence sensitivity and force flips
    • Bockelmann, U., P. Thomen, B. Essevaz-Roulet, V. Viasnoff, and F. Heslot. 2002. Unzipping DNA with optical tweezers: high sequence sensitivity and force flips. Biophys. J. 82:1537-1553.
    • (2002) Biophys. J. , vol.82 , pp. 1537-1553
    • Bockelmann, U.1    Thomen, P.2    Essevaz-Roulet, B.3    Viasnoff, V.4    Heslot, F.5
  • 29
    • 0034238118 scopus 로고    scopus 로고
    • Pulling pinned polymers and unzipping DNA
    • Lubensky, D. K., and D. R. Nelson. 2000. Pulling pinned polymers and unzipping DNA. Phys. Rev. Lett. 85:1572-1575.
    • (2000) Phys. Rev. Lett. , vol.85 , pp. 1572-1575
    • Lubensky, D.K.1    Nelson, D.R.2
  • 31
    • 0141774751 scopus 로고    scopus 로고
    • Characterization and optimization of the detection sensitivity of an atomic force microscope for small cantilevers
    • Schaffer, T. E., and P. K. Hansma. 1998. Characterization and optimization of the detection sensitivity of an atomic force microscope for small cantilevers. J. Appl. Phys. 84:4661-4666.
    • (1998) J. Appl. Phys. , vol.84 , pp. 4661-4666
    • Schaffer, T.E.1    Hansma, P.K.2
  • 35
    • 0036932510 scopus 로고    scopus 로고
    • Stability of bacteriorhodopsin alpha-helices and loops analyzed by single-molecule force spectroscopy
    • Muller, D. J., M. Kessler, F. Oesterhelt, C. Moller, D. Oesterhelt, and H. Gaub. 2002. Stability of bacteriorhodopsin alpha-helices and loops analyzed by single-molecule force spectroscopy. Biophys. J. 83:3578-3588.
    • (2002) Biophys. J. , vol.83 , pp. 3578-3588
    • Muller, D.J.1    Kessler, M.2    Oesterhelt, F.3    Moller, C.4    Oesterhelt, D.5    Gaub, H.6
  • 36
    • 2542585476 scopus 로고    scopus 로고
    • Shape insensitive optimal adhesion of nanoscale fibrillar structures
    • Gao, H. J., and H. M. Yao. 2004. Shape insensitive optimal adhesion of nanoscale fibrillar structures. Proc. Natl. Acad. Sci. USA. 101:7851-7856.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 7851-7856
    • Gao, H.J.1    Yao, H.M.2
  • 37
    • 0036022290 scopus 로고    scopus 로고
    • A molecular, morphometric and mechanical comparison of the structural elements of byssus from Mytilus edulis and Mytilus galloprovincialis
    • Lucas, J. M., E. Vaccaro, and J. H. Waite. 2002. A molecular, morphometric and mechanical comparison of the structural elements of byssus from Mytilus edulis and Mytilus galloprovincialis. J. Exp. Biol. 205:1807-1817.
    • (2002) J. Exp. Biol. , vol.205 , pp. 1807-1817
    • Lucas, J.M.1    Vaccaro, E.2    Waite, J.H.3
  • 38
    • 2942707997 scopus 로고    scopus 로고
    • Exploring molecular and mechanical gradients in structural bioscaffolds
    • Waite, J. H., H. C. Lichtenegger, G. D. Stucky, and P. Hansma. 2004. Exploring molecular and mechanical gradients in structural bioscaffolds. Biochemistry. 43:7653-7662.
    • (2004) Biochemistry , vol.43 , pp. 7653-7662
    • Waite, J.H.1    Lichtenegger, H.C.2    Stucky, G.D.3    Hansma, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.