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Volumn , Issue , 2009, Pages 144-178

Types, structure and mechanical properties of silk

Author keywords

Bombyx mori silk; Mechanical properties; Microstructure; Regenerated silk; Spider silk

Indexed keywords

ANIMALS; FIBERS; FOURIER TRANSFORM INFRARED SPECTROSCOPY; MECHANICAL PROPERTIES; MICROSTRUCTURE; X RAY DIFFRACTION;

EID: 84941264892     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1533/9781845696801.1.144     Document Type: Chapter
Times cited : (18)

References (105)
  • 2
    • 4544336281 scopus 로고    scopus 로고
    • Structure and structural changes of the silk fibroin from Samia cynthia ricini using nuclear magnetic resonance spectroscopy
    • Asakura T., Nakazawa Y. Structure and structural changes of the silk fibroin from Samia cynthia ricini using nuclear magnetic resonance spectroscopy. Macromolecular Bioscience 2004, 4:175-185.
    • (2004) Macromolecular Bioscience , vol.4 , pp. 175-185
    • Asakura, T.1    Nakazawa, Y.2
  • 3
    • 0031080850 scopus 로고    scopus 로고
    • NMR study of silk I structure of Bombyx mori silk fibroin with 15N- and 13C-NMR chemical shift contour plots
    • Asakura T., Demura M., Date T., Miyashita N., Ogawa K., Williamson M.P. NMR study of silk I structure of Bombyx mori silk fibroin with 15N- and 13C-NMR chemical shift contour plots. Biopolymers 1997, 41:193-203.
    • (1997) Biopolymers , vol.41 , pp. 193-203
    • Asakura, T.1    Demura, M.2    Date, T.3    Miyashita, N.4    Ogawa, K.5    Williamson, M.P.6
  • 4
    • 0035895432 scopus 로고    scopus 로고
    • A repeated b-turn structure in poly(ala-gly) as a model for silk I of Bombyx mori silk fibroin studied with two-dimensional spindiffusion NMR under off magic angle spinning and rotational echo double resonance
    • Asakura T., Ashida J., Yamane T., Kameda T., Nakasawa Y., Ohgo K., Komatsu K. A repeated b-turn structure in poly(ala-gly) as a model for silk I of Bombyx mori silk fibroin studied with two-dimensional spindiffusion NMR under off magic angle spinning and rotational echo double resonance. Journal of Molecular Biology 2001, 306:291-305.
    • (2001) Journal of Molecular Biology , vol.306 , pp. 291-305
    • Asakura, T.1    Ashida, J.2    Yamane, T.3    Kameda, T.4    Nakasawa, Y.5    Ohgo, K.6    Komatsu, K.7
  • 5
    • 24944514627 scopus 로고    scopus 로고
    • Refinement of repeated β-turn structure for silk I conformation of Bombyx mori silk fibroin using 13C solid-state NMR and X-ray diffraction methods
    • Asakura T., Ohgo K., Komatsu K., Kanenari M., Okuyama K. Refinement of repeated β-turn structure for silk I conformation of Bombyx mori silk fibroin using 13C solid-state NMR and X-ray diffraction methods. Macromolecules 2005, 38:7397-7403.
    • (2005) Macromolecules , vol.38 , pp. 7397-7403
    • Asakura, T.1    Ohgo, K.2    Komatsu, K.3    Kanenari, M.4    Okuyama, K.5
  • 6
    • 33947178954 scopus 로고    scopus 로고
    • Structure of the spinning apparatus of a wild Silkworm Samia cythia ricini and molecular dynamics calculation on the structural change of the silk fibroin
    • Asakura T., Yao J., Yang M., Zhu Z., Hirose H. Structure of the spinning apparatus of a wild Silkworm Samia cythia ricini and molecular dynamics calculation on the structural change of the silk fibroin. Polymer 2007, 48:2064-2070.
    • (2007) Polymer , vol.48 , pp. 2064-2070
    • Asakura, T.1    Yao, J.2    Yang, M.3    Zhu, Z.4    Hirose, H.5
  • 7
    • 84857654932 scopus 로고
    • The further application of the intra-articular silk ligament in the flail joints of poliomyelitis paralysis
    • Bartow B. The further application of the intra-articular silk ligament in the flail joints of poliomyelitis paralysis. Journal of Bone and Joint Surgery 1916, 2(14):217-220.
    • (1916) Journal of Bone and Joint Surgery , vol.2 , Issue.14 , pp. 217-220
    • Bartow, B.1
  • 9
    • 33749169644 scopus 로고    scopus 로고
    • Unraveling the mechanical properties of composite silk threads spun by cribellate orb-weaving spiders
    • Blackledge T.A., Hayashi C.Y. Unraveling the mechanical properties of composite silk threads spun by cribellate orb-weaving spiders. Journal of Experimental Biology 2006, 209:3131-3140.
    • (2006) Journal of Experimental Biology , vol.209 , pp. 3131-3140
    • Blackledge, T.A.1    Hayashi, C.Y.2
  • 10
    • 0035977675 scopus 로고    scopus 로고
    • Conformation transition kinetics of regenerated Bombyx mori silk fibroin membrane monitored by time-resolved FTIR spectroscopy
    • Chen X., Shao Z., Marinkovic N.S., Miller L.M., Zhou P., Chance M.R. Conformation transition kinetics of regenerated Bombyx mori silk fibroin membrane monitored by time-resolved FTIR spectroscopy. Biophysical Chemistry 2001, 89:25-34.
    • (2001) Biophysical Chemistry , vol.89 , pp. 25-34
    • Chen, X.1    Shao, Z.2    Marinkovic, N.S.3    Miller, L.M.4    Zhou, P.5    Chance, M.R.6
  • 11
    • 0036669933 scopus 로고    scopus 로고
    • Analysis of strain and stress in ceramic, polymer and metal matrix composites by Raman spectroscopy
    • Colomban P. Analysis of strain and stress in ceramic, polymer and metal matrix composites by Raman spectroscopy. Advanced Engineering Materials 2002, 4:535-542.
    • (2002) Advanced Engineering Materials , vol.4 , pp. 535-542
    • Colomban, P.1
  • 12
    • 56749101661 scopus 로고    scopus 로고
    • Raman and IR micro-analysis of high performance polymer fibres tested in traction and compression
    • Colomban P., Gouadec G. Raman and IR micro-analysis of high performance polymer fibres tested in traction and compression. Composites Science and Technology 2007, 69(1):10-16.
    • (2007) Composites Science and Technology , vol.69 , Issue.1 , pp. 10-16
    • Colomban, P.1    Gouadec, G.2
  • 13
    • 33747162702 scopus 로고    scopus 로고
    • Micro-Raman study of the fatigue and fracture behaviour of single PA 66 Fibres. Comparison with single PET and PP fibres
    • Colomban P., Herrera Ramirez J M, Paquin R., Marcellan A., Bunsell A.R. Micro-Raman study of the fatigue and fracture behaviour of single PA 66 Fibres. Comparison with single PET and PP fibres. Engineering Fracture Mechanisms 2006, 73:2463-2475.
    • (2006) Engineering Fracture Mechanisms , vol.73 , pp. 2463-2475
    • Colomban, P.1    Herrera, R.J.M.2    Paquin, R.3    Marcellan, A.4    Bunsell, A.R.5
  • 14
    • 57149100176 scopus 로고    scopus 로고
    • Nanomechanics of single silkworm and spider fibres: a Raman and micromechanical in situ study of the conformation change with stress
    • Colomban P., Dinh H.M., Riand J., Prinsloo L.C., Mauchamp B. Nanomechanics of single silkworm and spider fibres: a Raman and micromechanical in situ study of the conformation change with stress. Journal of Raman Spectroscopy 2008, 39(12):1749-1764.
    • (2008) Journal of Raman Spectroscopy , vol.39 , Issue.12 , pp. 1749-1764
    • Colomban, P.1    Dinh, H.M.2    Riand, J.3    Prinsloo, L.C.4    Mauchamp, B.5
  • 15
    • 0030940619 scopus 로고    scopus 로고
    • Evolution of arthropod silks
    • Craig C.L. Evolution of arthropod silks. Annual Review of Entomology 1997, 42:231-267.
    • (1997) Annual Review of Entomology , vol.42 , pp. 231-267
    • Craig, C.L.1
  • 18
    • 0032542564 scopus 로고    scopus 로고
    • Structure of Bombyx mori silk fibroin based on solid-state NMR: orientational constraints and fiber diffraction unit cell parameters
    • Demura M., Minami M., Asakura T., Cross T.A. Structure of Bombyx mori silk fibroin based on solid-state NMR: orientational constraints and fiber diffraction unit cell parameters. Journal of the American Chemical Society 1998, 120:1300-1308.
    • (1998) Journal of the American Chemical Society , vol.120 , pp. 1300-1308
    • Demura, M.1    Minami, M.2    Asakura, T.3    Cross, T.A.4
  • 19
    • 0001263217 scopus 로고
    • The physical properties of spider's silk and their role in the design of orb-webs
    • Denny M. The physical properties of spider's silk and their role in the design of orb-webs. Experimental Biology 1976, 65:483-506.
    • (1976) Experimental Biology , vol.65 , pp. 483-506
    • Denny, M.1
  • 20
    • 2542535248 scopus 로고    scopus 로고
    • Structural conformation of spidroin in solution: a synchrotron radiation circular dichroism study
    • Dicko C., Knight D., Kenney J.M., Vollrath F. Structural conformation of spidroin in solution: a synchrotron radiation circular dichroism study. Biomacromolecules 2004, 5:758-767.
    • (2004) Biomacromolecules , vol.5 , pp. 758-767
    • Dicko, C.1    Knight, D.2    Kenney, J.M.3    Vollrath, F.4
  • 22
    • 28844434957 scopus 로고    scopus 로고
    • Thermally induced α-helix to β-sheet transition in regenerated silk fibers and films
    • Drummy L.F., Phillips D.M., Stone M.O., Farmer B.L., Naik R.R. Thermally induced α-helix to β-sheet transition in regenerated silk fibers and films. Biomacromolecules 2005, 6:3328-3333.
    • (2005) Biomacromolecules , vol.6 , pp. 3328-3333
    • Drummy, L.F.1    Phillips, D.M.2    Stone, M.O.3    Farmer, B.L.4    Naik, R.R.5
  • 23
  • 24
    • 0042317003 scopus 로고    scopus 로고
    • Correlation between fibroin amino acid sequence and physical silk properties
    • Fedič R., Zčurovec M., Sehnal F. Correlation between fibroin amino acid sequence and physical silk properties. Journal of Biological Chemistry 2003, 278:35255-35264.
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 35255-35264
    • Fedič, R.1    Zčurovec, M.2    Sehnal, F.3
  • 26
    • 0031148815 scopus 로고    scopus 로고
    • Structure and organization of the Bombyx mori sericin 1 gene and of the sericins 1 deduced from the sequence of the ser 1BcDNA
    • Garel A., Deleage G., Prudhomme J.-C. Structure and organization of the Bombyx mori sericin 1 gene and of the sericins 1 deduced from the sequence of the ser 1BcDNA. Insect Biochemistry and Molecular Biology 1997, 27(5):469-477.
    • (1997) Insect Biochemistry and Molecular Biology , vol.27 , Issue.5 , pp. 469-477
    • Garel, A.1    Deleage, G.2    Prudhomme, J.-C.3
  • 29
    • 33947331746 scopus 로고    scopus 로고
    • Raman study of nano-materials: how spectra related to disorder, particle size and mechanical properties
    • Gouadec G., Colomban P. Raman study of nano-materials: how spectra related to disorder, particle size and mechanical properties. Progress in Crystal Growth & Characterization Materials 2007, 53:1-56.
    • (2007) Progress in Crystal Growth & Characterization Materials , vol.53 , pp. 1-56
    • Gouadec, G.1    Colomban, P.2
  • 31
    • 0001062986 scopus 로고
    • Infrared and Raman study of polyaniline. Part II: influence of orthosubstituents on hydrogen bonding and UV/Vis-near IR electron charge transfer
    • Gruger A., Novak A., Regis A., Colomban P. Infrared and Raman study of polyaniline. Part II: influence of orthosubstituents on hydrogen bonding and UV/Vis-near IR electron charge transfer. Journal of Molecular Structure 1995, 328:153-167.
    • (1995) Journal of Molecular Structure , vol.328 , pp. 153-167
    • Gruger, A.1    Novak, A.2    Regis, A.3    Colomban, P.4
  • 33
    • 0038517813 scopus 로고    scopus 로고
    • Dissolution of Bombyx mori silk fibroin in the calcium nitrate tetrahydrate-methanol system and aspects of wet spinning of fibroin solution
    • Ha S.-W., Park Y.H., Hudson S.M. Dissolution of Bombyx mori silk fibroin in the calcium nitrate tetrahydrate-methanol system and aspects of wet spinning of fibroin solution. Biomacromolecules 2003, 4:488-496.
    • (2003) Biomacromolecules , vol.4 , pp. 488-496
    • Ha, S.-W.1    Park, Y.H.2    Hudson, S.M.3
  • 34
    • 25844452749 scopus 로고    scopus 로고
    • Structural study of irregular amino acid sequences in the heavy chain Bombyx mori silk fibroin
    • Ha S.-W., Gracz H.S., Tonelli A.E., Hudson S.M. Structural study of irregular amino acid sequences in the heavy chain Bombyx mori silk fibroin. Biomacromolecules 2005, 6:2563-2569.
    • (2005) Biomacromolecules , vol.6 , pp. 2563-2569
    • Ha, S.-W.1    Gracz, H.S.2    Tonelli, A.E.3    Hudson, S.M.4
  • 35
    • 0032963575 scopus 로고    scopus 로고
    • Hypotheses that correlate the sequence, structure, and mechanical properties of spider silk proteins
    • Hayashi C.H., Shipley N.H., Lewis R.V. Hypotheses that correlate the sequence, structure, and mechanical properties of spider silk proteins. International Journal of Biological Macromolecules 1999, 24:271-275.
    • (1999) International Journal of Biological Macromolecules , vol.24 , pp. 271-275
    • Hayashi, C.H.1    Shipley, N.H.2    Lewis, R.V.3
  • 36
    • 4944247871 scopus 로고    scopus 로고
    • Spider flagelliform silk: lessons in protein design, gene structure, and molecular evolution
    • Hayashi C.Y., Blackledge T.A., Lewis R.V. Spider flagelliform silk: lessons in protein design, gene structure, and molecular evolution. Molecular Biology and Evolution 2004, 21(10):1950-1959.
    • (2004) Molecular Biology and Evolution , vol.21 , Issue.10 , pp. 1950-1959
    • Hayashi, C.Y.1    Blackledge, T.A.2    Lewis, R.V.3
  • 37
    • 11244317632 scopus 로고    scopus 로고
    • Micro-Raman study of the fatigue fracture and tensile behaviour of polyamide (PA 66) fibres
    • Herrera Ramirez J M, Colomban P., Bunsell A. Micro-Raman study of the fatigue fracture and tensile behaviour of polyamide (PA 66) fibres. Journal of Raman Spectroscopy 2004, 35:1063-1072.
    • (2004) Journal of Raman Spectroscopy , vol.35 , pp. 1063-1072
    • Herrera, R.J.M.1    Colomban, P.2    Bunsell, A.3
  • 38
    • 33751511523 scopus 로고    scopus 로고
    • Microstructural mechanisms governing the fatigue failure of polyamide 66 fibres
    • Herrera Ramirez J M, Bunsell A.R., Colomban P. Microstructural mechanisms governing the fatigue failure of polyamide 66 fibres. Journal of Materials Science 2006, 41:7261-7271.
    • (2006) Journal of Materials Science , vol.41 , pp. 7261-7271
    • Herrera, R.J.M.1    Bunsell, A.R.2    Colomban, P.3
  • 40
    • 33748778466 scopus 로고    scopus 로고
    • Determining beta-sheet crystallinity in fibrous proteins by thermal analysis and infrared spectroscopy
    • Hu X., Kaplan D., Cebe P. Determining beta-sheet crystallinity in fibrous proteins by thermal analysis and infrared spectroscopy. Macromolecules 2006, 39:6161-6170.
    • (2006) Macromolecules , vol.39 , pp. 6161-6170
    • Hu, X.1    Kaplan, D.2    Cebe, P.3
  • 41
    • 0009715073 scopus 로고
    • The physico-chemical properties of silk fibers and the fiber spinning process
    • Iizuka E. The physico-chemical properties of silk fibers and the fiber spinning process. Experimentia 1983, 39(5):449-454.
    • (1983) Experimentia , vol.39 , Issue.5 , pp. 449-454
    • Iizuka, E.1
  • 42
    • 0034704173 scopus 로고    scopus 로고
    • Silk fibroin of Bombyx mori is secreted, assembling a high molecular mass elementary unit consisting of H-chain, L-chain, and P25, with a 6:6:1 molar ratio
    • Inoue S., Tanaka K., Arisaka F., Kiura S., Ohtomo K., Mizuno S. Silk fibroin of Bombyx mori is secreted, assembling a high molecular mass elementary unit consisting of H-chain, L-chain, and P25, with a 6:6:1 molar ratio. Journal of Biological Chemistry 2000, 275(51):40517-40528.
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.51 , pp. 40517-40528
    • Inoue, S.1    Tanaka, K.2    Arisaka, F.3    Kiura, S.4    Ohtomo, K.5    Mizuno, S.6
  • 44
    • 29444456462 scopus 로고    scopus 로고
    • Tensile behavior and morphology of differently degummed silkworm (Bombyx mori) cocoon fibres
    • Jiang P., Liu H., Wang C., Wu L., Huang J., Guo C. Tensile behavior and morphology of differently degummed silkworm (Bombyx mori) cocoon fibres. Materials Letters 2006, 60:919-925.
    • (2006) Materials Letters , vol.60 , pp. 919-925
    • Jiang, P.1    Liu, H.2    Wang, C.3    Wu, L.4    Huang, J.5    Guo, C.6
  • 45
    • 0037025129 scopus 로고    scopus 로고
    • Determination of intermolecular distance for a model peptide of Bombyx mori silk fibroin, GAGAG, with rotational echo double resonance
    • Kameda T., Nakazawa Y., Kazuhara J., Yamane T., Asakura T. Determination of intermolecular distance for a model peptide of Bombyx mori silk fibroin, GAGAG, with rotational echo double resonance. Biopolymers 2002, 64:80-85.
    • (2002) Biopolymers , vol.64 , pp. 80-85
    • Kameda, T.1    Nakazawa, Y.2    Kazuhara, J.3    Yamane, T.4    Asakura, T.5
  • 47
  • 48
    • 34548052022 scopus 로고    scopus 로고
    • Nanofibrous membrane of wool keratose/ silk fibroin blend for heavy metal ion adsorption
    • Ki C.S., Gang E.H., Um I.C., Park Y.H. Nanofibrous membrane of wool keratose/ silk fibroin blend for heavy metal ion adsorption. Journal of Membrane Science 2007, 302:20-26.
    • (2007) Journal of Membrane Science , vol.302 , pp. 20-26
    • Ki, C.S.1    Gang, E.H.2    Um, I.C.3    Park, Y.H.4
  • 49
  • 51
    • 0033110632 scopus 로고    scopus 로고
    • Cocoon spinning behavior in the silkworm, Bombyx mori: comparison of three strains constructing different cocoons in shape
    • Kiyosawa M., Ito E., Shirai K., Kanekatsu R., Miura M., Kiguchi K. Cocoon spinning behavior in the silkworm, Bombyx mori: comparison of three strains constructing different cocoons in shape. Zoological Science 1999, 16:215-223.
    • (1999) Zoological Science , vol.16 , pp. 215-223
    • Kiyosawa, M.1    Ito, E.2    Shirai, K.3    Kanekatsu, R.4    Miura, M.5    Kiguchi, K.6
  • 52
    • 84858795988 scopus 로고    scopus 로고
    • Engineering properties of spider silk fibers
    • Kluwer Academic Publisher, Dordrect, Wallensberger, N. Weston (Eds.)
    • Ko J. Engineering properties of spider silk fibers. Natural Fibres, Plastics and Composites 2004, Kluwer Academic Publisher, Dordrect, (ISBN 1-4020-7643-6). Wallensberger, N. Weston (Eds.).
    • (2004) Natural Fibres, Plastics and Composites
    • Ko, J.1
  • 54
    • 34548216437 scopus 로고    scopus 로고
    • Conformation of spider silk proteins in situ in the intact major ampullate gland and in solution
    • Lefèvre T., Leclerc J., Rioux-Dube J.F., et al. Conformation of spider silk proteins in situ in the intact major ampullate gland and in solution. Biomacromolecules 2007, 8(8):2342-2344.
    • (2007) Biomacromolecules , vol.8 , Issue.8 , pp. 2342-2344
    • Lefèvre, T.1    Leclerc, J.2    Rioux-Dube, J.F.3
  • 55
    • 34147152672 scopus 로고    scopus 로고
    • Protein secondary structure and orientation in silk as revealed by raman spectromicroscopy
    • Lefèvre T., Rousseau M.-E., Pézolet M. Protein secondary structure and orientation in silk as revealed by raman spectromicroscopy. Biophysical Journal BioFAST 2007, 92:2885-2895.
    • (2007) Biophysical Journal BioFAST , vol.92 , pp. 2885-2895
    • Lefèvre, T.1    Rousseau, M.-E.2    Pézolet, M.3
  • 58
    • 0018401676 scopus 로고
    • The chemical structure and the crystalline structures of Bombyx mori silk fibroin
    • Lotz B., Cesari C. The chemical structure and the crystalline structures of Bombyx mori silk fibroin. Biochimie 1979, 61:205-214.
    • (1979) Biochimie , vol.61 , pp. 205-214
    • Lotz, B.1    Cesari, C.2
  • 60
    • 33846882627 scopus 로고    scopus 로고
    • Attachment and growth of human bone marrow derived mesenchymal stem cells on regenerated Antheraea pernyi silk fibroin films
    • Luan X.-Y., Wang Y., Duan X., Duan Q.-Y., Li M.-Z., Lu S.-Z., Zhang H.-X., Zhang X.-G. Attachment and growth of human bone marrow derived mesenchymal stem cells on regenerated Antheraea pernyi silk fibroin films. Biomedical Materials 2006, 1:181-187.
    • (2006) Biomedical Materials , vol.1 , pp. 181-187
    • Luan, X.-Y.1    Wang, Y.2    Duan, X.3    Duan, Q.-Y.4    Li, M.-Z.5    Lu, S.-Z.6    Zhang, H.-X.7    Zhang, X.-G.8
  • 63
    • 2342521978 scopus 로고    scopus 로고
    • (Nano)structure, internal stress and in situ fracture behaviour of polyamide fibres
    • Marcellan A., Colomban P., Bunsell A. (Nano)structure, internal stress and in situ fracture behaviour of polyamide fibres. Journal of Raman Spectroscopy 2004, 35:308-315.
    • (2004) Journal of Raman Spectroscopy , vol.35 , pp. 308-315
    • Marcellan, A.1    Colomban, P.2    Bunsell, A.3
  • 69
    • 0345688114 scopus 로고    scopus 로고
    • Electrospinning of silk fibroin nanofibers and its effect on the adhesion and spreading of normal human keratinocytes and fibroblasts in vitro
    • Min B.-M., Lee G., Kim S.H., Nam Y.S., Lee T.S., Park W.H. Electrospinning of silk fibroin nanofibers and its effect on the adhesion and spreading of normal human keratinocytes and fibroblasts in vitro. Biomaterials 2004, 25:1289-1297.
    • (2004) Biomaterials , vol.25 , pp. 1289-1297
    • Min, B.-M.1    Lee, G.2    Kim, S.H.3    Nam, Y.S.4    Lee, T.S.5    Park, W.H.6
  • 70
    • 0028340069 scopus 로고
    • Highly repetitive structure and its organization of the silk fibroin gene
    • Mita K., Ichimura S., James T.C. Highly repetitive structure and its organization of the silk fibroin gene. Journal of Molecular Evolution 1994, 38:583-592.
    • (1994) Journal of Molecular Evolution , vol.38 , pp. 583-592
    • Mita, K.1    Ichimura, S.2    James, T.C.3
  • 71
    • 85043728630 scopus 로고    scopus 로고
    • Raman spectroscopic characterization of Bombyx mori silk fibroRaman spectrum of silk I
    • Monti P., Taddei P., Freddi G., Asakura T., Tsukada M. Raman spectroscopic characterization of Bombyx mori silk fibroRaman spectrum of silk I. Journal of Raman Spectroscopy 2001, 32(2):103-107.
    • (2001) Journal of Raman Spectroscopy , vol.32 , Issue.2 , pp. 103-107
    • Monti, P.1    Taddei, P.2    Freddi, G.3    Asakura, T.4    Tsukada, M.5
  • 72
    • 0000778524 scopus 로고    scopus 로고
    • A 13C NMR study on the structural change of silk fibroin from Samia cynthia ricini
    • Nakazawa Y., Nakai T., Kameda T., Asakura T. A 13C NMR study on the structural change of silk fibroin from Samia cynthia ricini. Chemical Physics Letters 1999, 311:362-366.
    • (1999) Chemical Physics Letters , vol.311 , pp. 362-366
    • Nakazawa, Y.1    Nakai, T.2    Kameda, T.3    Asakura, T.4
  • 73
  • 74
    • 34248197448 scopus 로고    scopus 로고
    • Nanomechanics of single keratin fibres: a Raman study of the a helix-b sheet transition and water effect
    • Paquin R., Colomban P. Nanomechanics of single keratin fibres: a Raman study of the a helix-b sheet transition and water effect. Journal of Raman Spectroscopy 2007, 38:504-514.
    • (2007) Journal of Raman Spectroscopy , vol.38 , pp. 504-514
    • Paquin, R.1    Colomban, P.2
  • 78
    • 0038662300 scopus 로고    scopus 로고
    • Mechanical properties of silkworm silk in liquid media
    • Pérez-Rigueiro J., Viney C., Llorca J., Elices M. Mechanical properties of silkworm silk in liquid media. Polymer 2000, 41:8433-8439.
    • (2000) Polymer , vol.41 , pp. 8433-8439
    • Pérez-Rigueiro, J.1    Viney, C.2    Llorca, J.3    Elices, M.4
  • 80
    • 34547663037 scopus 로고    scopus 로고
    • Similarities and differences in the supramolecular organization of silkworm and spider silk
    • Pérez-Rigueiro J., Elices M., Plaza G.R., Guinea G.V. Similarities and differences in the supramolecular organization of silkworm and spider silk. Macromolecules 2007, 40:5360-5365.
    • (2007) Macromolecules , vol.40 , pp. 5360-5365
    • Pérez-Rigueiro, J.1    Elices, M.2    Plaza, G.R.3    Guinea, G.V.4
  • 82
    • 3042781559 scopus 로고    scopus 로고
    • Structural evolution of regenerated silk fibroin under shear: combined wide- and small-angle X-ray scattering experiments using synchrotron radiation
    • Rössle M., Panine P., Urban V.S., Riekel C. Structural evolution of regenerated silk fibroin under shear: combined wide- and small-angle X-ray scattering experiments using synchrotron radiation. Biopolymers 2004, 74:316-327.
    • (2004) Biopolymers , vol.74 , pp. 316-327
    • Rössle, M.1    Panine, P.2    Urban, V.S.3    Riekel, C.4
  • 83
    • 9744223571 scopus 로고    scopus 로고
    • Study of protein conformation and orientation in silkworm and spider silk fibers using Raman microspectroscopy
    • Rousseau M.-E., Lefèvre T., Beaulieu L., et al. Study of protein conformation and orientation in silkworm and spider silk fibers using Raman microspectroscopy. Biomacromolecules 2004, 5(6):2247-2257.
    • (2004) Biomacromolecules , vol.5 , Issue.6 , pp. 2247-2257
    • Rousseau, M.-E.1    Lefèvre, T.2    Beaulieu, L.3
  • 84
    • 33749539341 scopus 로고    scopus 로고
    • Characterization by Raman microspectroscopy of the strain-induced conformational transition in fibroin fibres from the silkworm Samia cynthia ricini
    • Rousseau M.-E., Beaulieu L., Lefèvre T., et al. Characterization by Raman microspectroscopy of the strain-induced conformational transition in fibroin fibres from the silkworm Samia cynthia ricini. Biomacromolecules 2006, 7(9):2512-2521.
    • (2006) Biomacromolecules , vol.7 , Issue.9 , pp. 2512-2521
    • Rousseau, M.-E.1    Beaulieu, L.2    Lefèvre, T.3
  • 86
    • 2642557196 scopus 로고    scopus 로고
    • The construction of silk fibre core in Lepidoptera
    • Sehnal F., Žurovec M. The construction of silk fibre core in Lepidoptera. Biomacromolecules 2004, 5:666-674.
    • (2004) Biomacromolecules , vol.5 , pp. 666-674
    • Sehnal, F.1    Žurovec, M.2
  • 87
    • 0037102416 scopus 로고    scopus 로고
    • Surprising strength of silkworm silk
    • Shao Z., Vollrath F. Surprising strength of silkworm silk. Nature 2002, 418:741.
    • (2002) Nature , vol.418 , pp. 741
    • Shao, Z.1    Vollrath, F.2
  • 88
    • 0000624264 scopus 로고
    • Chemical composition and biosynthesis of silk proteins
    • Shimura K. Chemical composition and biosynthesis of silk proteins. Experimentia 1983, 39(5):455-461.
    • (1983) Experimentia , vol.39 , Issue.5 , pp. 455-461
    • Shimura, K.1
  • 89
    • 0034142611 scopus 로고    scopus 로고
    • Molecular deformation in spider dragline silk subjected to stress
    • Sirichaisit J., Young R.J., Vollrath F. Molecular deformation in spider dragline silk subjected to stress. Polymer 2000, 41(3):1223-1227.
    • (2000) Polymer , vol.41 , Issue.3 , pp. 1223-1227
    • Sirichaisit, J.1    Young, R.J.2    Vollrath, F.3
  • 90
    • 0037734260 scopus 로고    scopus 로고
    • Analysis of structure/property relationships in silkworm (Bombyx mori) and spider dragline (Nephila edulis) silks using Raman spectroscopy
    • Sirichaisit J., Brookes V.L., Young R.J., et al. Analysis of structure/property relationships in silkworm (Bombyx mori) and spider dragline (Nephila edulis) silks using Raman spectroscopy. Biomacromolecules 2003, 4(2):387-394.
    • (2003) Biomacromolecules , vol.4 , Issue.2 , pp. 387-394
    • Sirichaisit, J.1    Brookes, V.L.2    Young, R.J.3
  • 91
    • 23944483501 scopus 로고    scopus 로고
    • Vibrational infrared conformational studies of model peptides representing the semicrystalline domains of Bombyx mori silk fibroin
    • Taddei P., Monti P. Vibrational infrared conformational studies of model peptides representing the semicrystalline domains of Bombyx mori silk fibroin. Biopolymers 2005, 78:249-258.
    • (2005) Biopolymers , vol.78 , pp. 249-258
    • Taddei, P.1    Monti, P.2
  • 92
    • 34748822259 scopus 로고    scopus 로고
    • Identification and characterization of a novel sericin gene expressed in the anterior middle gland of the silkworm Bombyx mori
    • Takasu Y., Yamada H., Tamura T., Sezutsu H., Mita K., Tsubouchi K. Identification and characterization of a novel sericin gene expressed in the anterior middle gland of the silkworm Bombyx mori. Insect Biochemistry and Molecular Biology 2007, 37(11):1234-1240.
    • (2007) Insect Biochemistry and Molecular Biology , vol.37 , Issue.11 , pp. 1234-1240
    • Takasu, Y.1    Yamada, H.2    Tamura, T.3    Sezutsu, H.4    Mita, K.5    Tsubouchi, K.6
  • 93
    • 0028765923 scopus 로고
    • Molecular modeling of spider silk elasticity
    • Termonia Y. Molecular modeling of spider silk elasticity. Macromolecules 1994, 27:7378-7381.
    • (1994) Macromolecules , vol.27 , pp. 7378-7381
    • Termonia, Y.1
  • 94
    • 9744275950 scopus 로고    scopus 로고
    • Nanoscale self-assembly of multiblock copolymer chains into rods
    • Termonia Y. Nanoscale self-assembly of multiblock copolymer chains into rods. Biomacromolecules 2004, 5:2404-2407.
    • (2004) Biomacromolecules , vol.5 , pp. 2404-2407
    • Termonia, Y.1
  • 96
    • 0035967162 scopus 로고    scopus 로고
    • Liquid crystal silk spinning in nature
    • Vollrath F., Knight D.P. Liquid crystal silk spinning in nature. Nature 2001, 410:541-548.
    • (2001) Nature , vol.410 , pp. 541-548
    • Vollrath, F.1    Knight, D.P.2
  • 97
    • 33745685415 scopus 로고    scopus 로고
    • Spider silk as archetypal protein elastomer
    • Vollrath F., Porter D. Spider silk as archetypal protein elastomer. Soft Matter 2006, 2:377-385.
    • (2006) Soft Matter , vol.2 , pp. 377-385
    • Vollrath, F.1    Porter, D.2
  • 99
    • 0034023387 scopus 로고    scopus 로고
    • Conformational transitions in model silk peptides
    • Wilson D., Valluzzi R., Kaplan D. Conformational transitions in model silk peptides. Biophysical Journal 2000, 78:2690-2701.
    • (2000) Biophysical Journal , vol.78 , pp. 2690-2701
    • Wilson, D.1    Valluzzi, R.2    Kaplan, D.3
  • 101
    • 35348975160 scopus 로고    scopus 로고
    • Development and evaluation of silk fibroin-based nerve grafts used for peripheral nerve regeneration
    • Yang Y., Ding F., Wu J., Hu W., Liu W., Liu J., Gu X. Development and evaluation of silk fibroin-based nerve grafts used for peripheral nerve regeneration. Biomaterials 2007, 28:5526-5535.
    • (2007) Biomaterials , vol.28 , pp. 5526-5535
    • Yang, Y.1    Ding, F.2    Wu, J.3    Hu, W.4    Liu, W.5    Liu, J.6    Gu, X.7
  • 104
    • 0242710694 scopus 로고    scopus 로고
    • The 62-kb upstream region of Bombyx mori fibroin heavy chain gene is clustered of repetitive elements and candidate matrix association regions
    • Zhou L., Chen X., Shao Z., Zhou P., Knight D.P., Vollrath F. The 62-kb upstream region of Bombyx mori fibroin heavy chain gene is clustered of repetitive elements and candidate matrix association regions. FEBS Letters 2003, 554:337-341.
    • (2003) FEBS Letters , vol.554 , pp. 337-341
    • Zhou, L.1    Chen, X.2    Shao, Z.3    Zhou, P.4    Knight, D.P.5    Vollrath, F.6
  • 105
    • 0037151068 scopus 로고    scopus 로고
    • Unique molecular architeture of silk fibroin in the waxmoth Galleria mellonella
    • Žurovec M., Sehnal F. Unique molecular architeture of silk fibroin in the waxmoth Galleria mellonella. Journal of Biological Chemistry 2002, 277(25):22639-22647.
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.25 , pp. 22639-22647
    • Žurovec, M.1    Sehnal, F.2


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