메뉴 건너뛰기




Volumn 69, Issue , 2013, Pages 23-68

Silk structure studied with nuclear magnetic resonance

Author keywords

A. Pernyi; Anaphe; Bombyx mori; NMR; Poly(Ala Gly); Polyalanine; S. c.ricini; Silk fibroin; Spider silk

Indexed keywords

BIOCOMPATIBILITY; BIOPOLYMERS; STRENGTH OF MATERIALS; TOUGHNESS; X RAY DIFFRACTION;

EID: 84875102530     PISSN: 00796565     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pnmrs.2012.08.001     Document Type: Review
Times cited : (95)

References (196)
  • 1
    • 0035895432 scopus 로고    scopus 로고
    • A repeated β-turn structure in poly(Ala-Gly) as a model for silk I of Bombyx mori silk fibroin studied with two-dimensional spin-diffusion NMR under off magic angle spinning and rotational echo double resonance
    • DOI 10.1006/jmbi.2000.4394
    • T. Asakura, J. Ashida, T. Yamane, T. Kameda, Y. Nakazawa, K. Ohgo, and K. Komatsu A repeated β-turn structure in Poly(Ala-Gly) as a model for Silk I of Bombyx mori silk fibroin studied with two-dimensional spin-diffusion NMR under off magic angle spinning and rotational echo double resonance J. Mol. Biol. 306 2001 291 305 (Pubitemid 33032881)
    • (2001) Journal of Molecular Biology , vol.306 , Issue.2 , pp. 291-305
    • Asakura, T.1    Ashida, J.2    Yamane, T.3    Kameda, T.4    Nakazawa, Y.5    Ohgo, K.6    Komatsu, K.7
  • 4
    • 48249154984 scopus 로고    scopus 로고
    • Determining secondary structure in spider dragline silk by carbon-carbon correlation solid-state NMR spectroscopy
    • G.P. Holland, M.S. Creager, J.E. Jenkins, R.V. Lewis, and J.L. Yarger Determining secondary structure in spider dragline silk by carbon-carbon correlation solid-state NMR spectroscopy J. Am. Chem. Soc. 130 2008 9871 9877
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 9871-9877
    • Holland, G.P.1    Creager, M.S.2    Jenkins, J.E.3    Lewis, R.V.4    Yarger, J.L.5
  • 8
    • 28544433674 scopus 로고
    • 13C NMR of Nephila clavipes dragline silk establishes structure and identity of crystalline regions
    • 13C NMR of Nephila clavipes dragline silk establishes structure and identity of crystalline regions Macromolecules 27 1994 5235 5237
    • (1994) Macromolecules , vol.27 , pp. 5235-5237
    • Simmons, A.1    Ray, E.2    Jelinski, L.W.3
  • 9
    • 0025008260 scopus 로고
    • Structure of a protein superfiber: Spider dragline silk
    • M. Xu, and R. Lewis Structure of a protein superfiber: spider dragline silk Proc. Natl. Acad. Sci. USA 87 1990 7120 7124
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 7120-7124
    • Xu, M.1    Lewis, R.2
  • 10
    • 0026657815 scopus 로고
    • Isolation of a clone encoding a second dragline silk fibroin. Nephila clavipes dragline silk is a two-protein fiber
    • M. Hinman, and R.V. Lewis Isolation of a clone encoding a second dragline silk fibroin. Nephila clavipes dragline silk is a two-protein fiber J. Biol. Chem. 267 1992 19320 19324
    • (1992) J. Biol. Chem. , vol.267 , pp. 19320-19324
    • Hinman, M.1    Lewis, R.V.2
  • 11
    • 0031269978 scopus 로고    scopus 로고
    • Conformation of the polyalanine repeats in minor ampullate gland silk of the spider Nephila clavipes
    • O. Liivak, A. Flores, R.V. Lewis, and L.W. Jelinski Conformation of the PLA repeats in minor ampullate gland silk of the spider Nephila clavipes Macromolecules 30 1997 7127 7130 (Pubitemid 127567586)
    • (1997) Macromolecules , vol.30 , Issue.23 , pp. 7127-7130
    • Liivak, O.1    Flores, A.2    Lewis, R.3    Jelinski, L.W.4
  • 13
    • 23044432901 scopus 로고    scopus 로고
    • Araneoid egg case silk: A fibroin with novel ensemble repeat units from the black widow spider, Latrodectus hesperus
    • DOI 10.1021/bi050494i
    • X. Hu, B. Lawrence, K. Kohler, A.M. Falick, A.M.F. Moore, E. McMullen, P.R. Jones, and C. Vierra Araneoid egg case silk: a fibroin with novel ensemble repeat units from the Black Widow Spider, Latrodectus hesperus Biochemistry 44 2005 10020 10027 (Pubitemid 41076797)
    • (2005) Biochemistry , vol.44 , Issue.30 , pp. 10020-10027
    • Hu, X.1    Lawrence, B.2    Kohler, K.3    Falick, A.M.4    Moore, A.M.F.5    McMullen, E.6    Jones, P.R.7    Vierra, C.8
  • 14
    • 2542623618 scopus 로고    scopus 로고
    • Molecular and mechanical properties of major ampullate silk of the black widow spider, Latrodectus hesperus
    • DOI 10.1021/bm0342640
    • B.A. Lawrence, C.A. Vierra, and A.M.F. Moore Molecular and mechanical properties of major ampullate silk of the Black Widow Spider, Latrodectus hesperus Biomacromolecules 5 2004 689 695 (Pubitemid 38702233)
    • (2004) Biomacromolecules , vol.5 , Issue.3 , pp. 689-695
    • Lawrence, B.A.1    Vierra, C.A.2    Moore, A.M.F.3
  • 16
    • 0036678028 scopus 로고    scopus 로고
    • The molecular structure of spider dragline silk: Folding and orientation of the protein backbone
    • J.D. van Beek, S. Hess, F. Vollrath, and B. Meier The molecular structure of spider dragline silk: folding and orientation of the protein backbone Proc. Natl. Acad. Sci. USA 99 2002 10266 10271
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 10266-10271
    • Van Beek, J.D.1    Hess, S.2    Vollrath, F.3    Meier, B.4
  • 17
    • 33744474888 scopus 로고    scopus 로고
    • Orientational order of Australian spider silks as determined by solid-state NMR
    • DOI 10.1002/bip.20471
    • B. Bonev, S. Grieve, M. Herberstein, A. Kishore, A. Watts, and F. Separovic Orientational order of Australian spider silks as determined by solid-state NMR Biopolymers 82 2006 134 143 (Pubitemid 43798161)
    • (2006) Biopolymers , vol.82 , Issue.2 , pp. 134-143
    • Bonev, B.1    Grieve, S.2    Herberstein, M.E.3    Kishore, A.I.4    Watts, A.5    Separovic, F.6
  • 18
    • 1442285968 scopus 로고    scopus 로고
    • Solid-state NMR relaxation studies of Australian spider silks
    • A. Kishore, M. Herberstein, C. Craig, and F. Separovic Solid-state NMR relaxation studies of Australian spider silks Biopolymers 61 2002 287 297
    • (2002) Biopolymers , vol.61 , pp. 287-297
    • Kishore, A.1    Herberstein, M.2    Craig, C.3    Separovic, F.4
  • 19
    • 0020130102 scopus 로고
    • A physico-chemical study of the supercontraction of spider major ampullate silk fibers Text
    • R.W. Work, and N. Morosoff A physico-chemical study of the supercontraction of spider major ampullate silk fibers Text. Res. J. 52 1982 349 356 (Pubitemid 12551402)
    • (1982) Textile Research Journal , vol.52 , Issue.5 , pp. 349-356
    • Work Robert, W.1    Morosoff Nicholas2
  • 21
    • 39749136083 scopus 로고    scopus 로고
    • Solid-state NMR investigation of major and minor ampullate spider silk in the native and hydrated states
    • DOI 10.1021/bm700950u
    • G.P. Holland, J.E. Jenkins, M. Creager, R.V. Lewis, and J.L. Yarger Solid-state NMR investigation of major and minor ampullate spider silks in the native and hydrated states Biomacromolecules 9 2008 651 657 (Pubitemid 351298490)
    • (2008) Biomacromolecules , vol.9 , Issue.2 , pp. 651-657
    • Holland, G.P.1    Jenkins, J.E.2    Creager, M.S.3    Lewis, R.V.4    Yarger, J.L.5
  • 22
    • 73949115562 scopus 로고    scopus 로고
    • Structure and dynamics of aromatic residues in spider silk: 2D carbon correlation NMR of dragline fibers
    • T. Izdebski, P. Akhenblit, J.E. Jenkins, J.L. Yarger, and G.P. Holland Structure and dynamics of aromatic residues in spider silk: 2D carbon correlation NMR of dragline fibers Biomacromolecules 11 2010 168 174
    • (2010) Biomacromolecules , vol.11 , pp. 168-174
    • Izdebski, T.1    Akhenblit, P.2    Jenkins, J.E.3    Yarger, J.L.4    Holland, G.P.5
  • 23
    • 77956330677 scopus 로고    scopus 로고
    • Solid-state NMR evidence for elastin-like β-turn structure in spider dragline silk
    • J.E. Jenkins, M.S. Creager, R.V. Lewis, J.L. Yarger, and G.P. Holland Solid-state NMR evidence for elastin-like β-turn structure in spider dragline silk Chem. Commun. 46 2010 6714 6716
    • (2010) Chem. Commun. , vol.46 , pp. 6714-6716
    • Jenkins, J.E.1    Creager, M.S.2    Lewis, R.V.3    Yarger, J.L.4    Holland, G.P.5
  • 24
    • 33845449514 scopus 로고    scopus 로고
    • 13C polarization transfer under dipolar-assisted rotational resonance in magic-angle-spinning NMR
    • 13C polarization transfer under dipolar-assisted rotational resonance in magic-angle-spinning NMR J. Chem. Phys. 125 2006 214503
    • (2006) J. Chem. Phys. , vol.125 , pp. 214503
    • Ohashi, R.1    Takegoshi, K.2
  • 25
    • 0000953276 scopus 로고    scopus 로고
    • 1H dipolar-assisted rotational resonance in magic-angle spinning NMR
    • DOI 10.1016/S0009-2614(01)00791-6, PII S0009261401007916
    • 1H dipolar-assisted rotational resonance in magic-angle-spinning NMR Chem. Phys. Lett. 344 2001 631 637 (Pubitemid 33628408)
    • (2001) Chemical Physics Letters , vol.344 , Issue.5-6 , pp. 631-637
    • Takegoshi, K.1    Nakamura, S.2    Terao, T.3
  • 26
    • 0037329467 scopus 로고    scopus 로고
    • 13C RF irradiation in nuclear magnetic resonance of rotating solids
    • 13C RF irradiation in nuclear magnetic resonance of rotating solids J. Chem. Phys. 118 2003 2325 2341
    • (2003) J. Chem. Phys. , vol.118 , pp. 2325-2341
    • Takegoshi, K.1    Nakamura, S.2    Terao, T.3
  • 27
    • 73949098417 scopus 로고    scopus 로고
    • Quantitative correlation between the protein primary sequences and secondary structures in spider dragline silks
    • J.E. Jenkins, M.S. Creager, R.V. Lewis, G.P. Holland, and J.L. Yarger Quantitative correlation between the protein primary sequences and secondary structures in spider dragline silks Biomacromolecules 11 2010 192 200
    • (2010) Biomacromolecules , vol.11 , pp. 192-200
    • Jenkins, J.E.1    Creager, M.S.2    Lewis, R.V.3    Holland, G.P.4    Yarger, J.L.5
  • 28
    • 0027115080 scopus 로고
    • Correlation of structure, mobility, and morphological information in heterogeneous polymer materials by two-dimensional wideline-separation NMR spectroscopy
    • K. Schmidt-Rohr, J. Clauss, and H.W. Spiess Correlation of structure, mobility, and morphological information in heterogeneous polymer materials by two-dimensional wideline-separation NMR spectroscopy Macromolecules 25 1992 3273 3277
    • (1992) Macromolecules , vol.25 , pp. 3273-3277
    • Schmidt-Rohr, K.1    Clauss, J.2    Spiess, H.W.3
  • 29
    • 2442454478 scopus 로고    scopus 로고
    • WISE NMR Characterization of Nanoscale Heterogeneity and Mobility in Supercontracted Nephila clavipes Spider Dragline Silk
    • DOI 10.1021/ja031930w
    • G.P. Holland, R.V. Lewis, and J.L. Yarger WISE NMR characterization of nanoscale heterogeneity and mobility in supercontracted Nephila clavipes spider dragline silk J. Am. Chem. Soc. 126 2004 5867 5872 (Pubitemid 38621425)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.18 , pp. 5867-5872
    • Holland, G.P.1    Lewis, R.V.2    Yarger, J.L.3
  • 30
    • 58149103420 scopus 로고    scopus 로고
    • Development of silk-like materials based on Bombyx mori and Nephila clavipes dragline silk fibroins
    • Y. Mingying, J. Kawamura, Z. Zhu, K. Yamauchi, and T. Asakura Development of silk-like materials based on Bombyx mori and Nephila clavipes dragline silk fibroins Polymer 50 2009 117 124
    • (2009) Polymer , vol.50 , pp. 117-124
    • Mingying, Y.1    Kawamura, J.2    Zhu, Z.3    Yamauchi, K.4    Asakura, T.5
  • 32
    • 0002579470 scopus 로고
    • Symmetrized multipulse nuclear-magnetic-resonance experiments solids-measurement of chemical-shift shielding tensor in some compounds
    • P. Mansfield, M.J. Orchard, D.C. Stalker, and K.H.B. Richards Symmetrized multipulse nuclear-magnetic-resonance experiments solids-measurement of chemical-shift shielding tensor in some compounds Phys. Rev. B 7 1973 90 105
    • (1973) Phys. Rev. B , vol.7 , pp. 90-105
    • Mansfield, P.1    Orchard, M.J.2    Stalker, D.C.3    Richards, K.H.B.4
  • 33
    • 36749120596 scopus 로고
    • Analysis of multiple pulse NMR in solids
    • D.P. Burum, and W.K. Rhim Analysis of multiple pulse NMR in solids J. Chem. Phys. 71 1979 944 956
    • (1979) J. Chem. Phys. , vol.71 , pp. 944-956
    • Burum, D.P.1    Rhim, W.K.2
  • 34
    • 0000628777 scopus 로고
    • An improved experiment for heteronuclear-correlation 2D-NMR in solids
    • D.P. Burum, and A. Bielecki An improved experiment for heteronuclear-correlation 2D-NMR in solids J. Magn. Reson. 94 1991 645 652
    • (1991) J. Magn. Reson. , vol.94 , pp. 645-652
    • Burum, D.P.1    Bielecki, A.2
  • 35
    • 0346938543 scopus 로고    scopus 로고
    • 13C NMR Heteronuclear Dipolar-Correlation Spectroscopy of Solids with Frequency-Switched Lee-Goldburg Homonuclear Decoupling
    • B.-J. van Rossum, H. Förster, and H.J.M. de Groot High-field and high-speed CP-MAS 13C NMR heteronuclear dipolar-correlation spectroscopy of solids with frequency-switched Lee-Goldburg homonuclear decoupling J. Magn. Reson. 124 1997 516 519 (Pubitemid 127451823)
    • (1997) Journal of Magnetic Resonance , vol.124 , Issue.2 , pp. 516-519
    • Van Rossum, B.-J.1    Forster, H.2    De Groot, H.J.M.3
  • 37
    • 0037066031 scopus 로고    scopus 로고
    • Proton spectroscopy in solid state nuclear magnetic resonance with windowed phase modualted Lee-Goldburg decoupling sequences
    • E. Vinogradov, P.K. Madhu, and S. Vega Proton spectroscopy in solid state nuclear magnetic resonance with windowed phase modualted Lee-Goldburg decoupling sequences Chem. Phys. Lett. 354 2002 193 202
    • (2002) Chem. Phys. Lett. , vol.354 , pp. 193-202
    • Vinogradov, E.1    Madhu, P.K.2    Vega, S.3
  • 38
    • 55649120023 scopus 로고    scopus 로고
    • Homonuclear dipolar decoupling at magic angle spinning frequencies up to 65 kHz in solid-state nuclear magnetic resonance
    • M. Leskes, S. Steuernagel, D. Schneider, P.K. Madhu, and S. Vega Homonuclear dipolar decoupling at magic angle spinning frequencies up to 65 kHz in solid-state nuclear magnetic resonance Chem. Phys. Lett. 466 2008 95 99
    • (2008) Chem. Phys. Lett. , vol.466 , pp. 95-99
    • Leskes, M.1    Steuernagel, S.2    Schneider, D.3    Madhu, P.K.4    Vega, S.5
  • 39
    • 0001315175 scopus 로고    scopus 로고
    • Homonuclear dipolar decoupling in solid-state NMR using continuous phase modulation
    • D. Sakellariou, A. Lesage, P. Hodgkinson, and L. Emsley Homonuclear dipolar decoupling in solid-state NMR using continuous phase modulation Chem. Phys. Lett. 319 2000 253 260
    • (2000) Chem. Phys. Lett. , vol.319 , pp. 253-260
    • Sakellariou, D.1    Lesage, A.2    Hodgkinson, P.3    Emsley, L.4
  • 40
    • 33745676528 scopus 로고    scopus 로고
    • Investigation of dipolar-mediated water-protein interactions in microcrystalline Crh by solid-state NMR spectroscopy
    • DOI 10.1021/ja060866q
    • A. Lesage, L. Emsley, F. Penin, and A. Böckmann Investigation of dipolar-mediated water-protein interactions in microcrystalline Crh by solid-state NMR spectroscopy J. Am. Chem. Soc. 128 2006 8246 8255 (Pubitemid 43967769)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.25 , pp. 8246-8255
    • Lesage, A.1    Emsley, L.2    Penin, F.3    Bockmann, A.4
  • 42
    • 0037177289 scopus 로고    scopus 로고
    • Structural investigations of solid proteins at natural abundance using 2D multiple-pulse NMR
    • DOI 10.1021/ma012067s
    • J.L. White, and X. Wang Structural investigation of solid proteins at natural abundance using 2D multiple-pulse NMR Macromolecules 35 2002 2633 2639 (Pubitemid 34586595)
    • (2002) Macromolecules , vol.35 , Issue.7 , pp. 2633-2639
    • White, J.L.1    Wang, X.2
  • 46
    • 0032179660 scopus 로고    scopus 로고
    • 1H combined rotation and multiple pulse spectroscopy NMR. 2. Amide proton chemical shift
    • H. Kimura, T. Ozaki, H. Sugisawa, K. Deguchi, and A. Shoji Conformational study of solid polypeptides by H-1 combined rotation and multiple pulse spectroscopy NMR. 2. Amide proton chemical shift Macromolecules 31 1998 7398 7403 (Pubitemid 128563454)
    • (1998) Macromolecules , vol.31 , Issue.21 , pp. 7398-7403
    • Kimura, H.1    Ozaki, T.2    Sugisawa, H.3    Deguchi, K.4    Shoji, A.5
  • 47
    • 0030574944 scopus 로고    scopus 로고
    • Local structure in spider dragline silk investigated by two-dimensional spin-diffusion nuclear magnetic resonance
    • J. Kummerlen, J.D. van Beek, F. Vollrath, and B.H. Meier Local structure in spider dragline silk investigated by two-dimensional spin-diffusion nuclear magnetic resonance Macromolecules 29 1996 2920 2928 (Pubitemid 126554020)
    • (1996) Macromolecules , vol.29 , Issue.8 , pp. 2920-2928
    • Kummerlen, J.1    Van Beek, J.D.2    Vollrath, F.3    Meier, B.H.4
  • 48
    • 0035045539 scopus 로고    scopus 로고
    • 13C cross-polarization/ magic angle spinning NMR
    • DOI 10.1002/1097-0282(20010415)58: 5<521::AID-BIP1027>3.0.CO;2-T
    • 13C cross-polarization/magic angle spinning NMR Biopolymers 58 2001 521 525 (Pubitemid 32303817)
    • (2001) Biopolymers , vol.58 , Issue.5 , pp. 521-525
    • Asakura, T.1    Yamane, T.2    Nakazawa, Y.3    Kameda, T.4    Ando, K.5
  • 49
    • 0037068874 scopus 로고    scopus 로고
    • Determination of the torsion angles of alanine and glycine residues of Bombyx mori silk fibroin and the model peptides in the silk I and silk II forms using 2D spin diffusion solid-state NMR under off magic angle spinning
    • DOI 10.1021/jp020331t
    • J. Ashida, K. Ohgo, and T. Asakura Determination of the torsion angles of alanine and glycine residues of Bombyx mori silk fibroin and the model peptides in the Silk I and Silk II forms using 2D spin diffusion solid-state NMR under off magic angle spinning J. Phys. Chem. B 106 2002 9434 9439 (Pubitemid 35382814)
    • (2002) Journal of Physical Chemistry B , vol.106 , Issue.36 , pp. 9434-9439
    • Ashida, J.1    Ohgo, K.2    Asakura, T.3
  • 51
  • 52
    • 0037377504 scopus 로고    scopus 로고
    • Tightly winding structure of sequential model peptide for repeated helical region in Samia cynthia ricini silk fibroin studied with solid-state NMR
    • DOI 10.1110/ps.0239203
    • Y. Nakazawa, M. Bamba, S. Nishio, and T. Asakura Tightly winding structure of sequential model peptide for repeated helical region in Samia cynthia ricini silk fibroin studied with solid-state NMR Protein Sci. 12 2003 666 671 (Pubitemid 36348452)
    • (2003) Protein Science , vol.12 , Issue.4 , pp. 666-671
    • Nakazawa, Y.1    Bamba, M.2    Nishio, S.3    Asakura, T.4
  • 53
    • 0038451228 scopus 로고    scopus 로고
    • Structure determination of a peptide model of the repeated helical domain in Samia cynthia ricini silk fibroin before spinning by a combination of advanced solid-state NMR methods
    • DOI 10.1021/ja0300721
    • Y. Nakazawa, and T. Asakura Structure determination of a peptide model of the repeated helical domain in Samia cynthia ricini silk fibroin before spinning by a combination of advanced solid-state NMR methods J. Am. Chem. Soc. 125 2003 7230 7237 (Pubitemid 36798970)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.24 , pp. 7230-7237
    • Nakazawa, Y.1    Asakura, T.2
  • 54
    • 2542591611 scopus 로고    scopus 로고
    • Structure of the model peptides of Bombyx mori silk-elastin like protein studied with solid state NMR
    • DOI 10.1021/bm034355x
    • K. Ohgo, T.L. Kurano, K.K. Kumashiro, and T. Asakura Structure of the model peptides of Bombyx mori silk-elastin like protein studied with solid state NMR Biomacromolecules 5 2004 744 750 (Pubitemid 38702241)
    • (2004) Biomacromolecules , vol.5 , Issue.3 , pp. 744-750
    • Ohgo, K.1    Kurano, T.L.2    Kumashiro, K.K.3    Asakura, T.4
  • 55
    • 2542544274 scopus 로고    scopus 로고
    • Structures of Bombyx mori and Samia cynthia ricini silk fibroins studied with solid-state NMR
    • DOI 10.1021/bm034285u
    • J. Yao, Y. Nakazawa, and T. Asakura Structures of Bombyx mori and Samia cynthia ricini silk fibroins studied with solid-state NMR Biomacromolecules 5 2004 680 688 (Pubitemid 38702232)
    • (2004) Biomacromolecules , vol.5 , Issue.3 , pp. 680-688
    • Yao, J.1    Nakazawa, Y.2    Asakura, T.3
  • 56
    • 17444427722 scopus 로고    scopus 로고
    • 13C solid-state NMR study of structural heterogeneity in peptides containing both polyalanine and repeated GGA sequences as a local structural model of nephila clavipes dragline silk (spidroin 1)
    • DOI 10.1021/ma047660z
    • 13C solid-state NMR study of structural heterogeneity in peptides containing both PLA and repeated GGA sequences as a local structural model of Nephila clavipes dragline silk (spidroin 1) Macromolecules 38 2005 3356 3363 (Pubitemid 40541240)
    • (2005) Macromolecules , vol.38 , Issue.8 , pp. 3356-3363
    • Asakura, T.1    Yang, M.2    Kawase, T.3    Nakazawa, Y.4
  • 57
    • 24944514627 scopus 로고    scopus 로고
    • 13C solid-state NMR and X-ray diffraction methods
    • DOI 10.1021/ma050936y
    • T. Asakura, K. Ohgo, K. Komatsu, M. Kanenari, and K. Okuyama Refinement of repeated beta-turn structure for Silk I conformation of Bombyx mori silk fibroin using C-13 solid-state NMR and X-ray diffraction methods Macromolecules 38 2005 7397 7403 (Pubitemid 41305040)
    • (2005) Macromolecules , vol.38 , Issue.17 , pp. 7397-7403
    • Asakura, T.1    Ohgo, K.2    Komatsu, K.3    Kanenari, M.4    Okuyama, K.5
  • 58
    • 33646359182 scopus 로고    scopus 로고
    • 6-Gly derived from a flagelliform silk sequence of Nephila clavipes
    • DOI 10.1021/bm0600522
    • 6-Gly derived from a flagelliform silk sequence of Nephila clavipes Biomacromolecules 7 2006 1210 1214 (Pubitemid 43670808)
    • (2006) Biomacromolecules , vol.7 , Issue.4 , pp. 1210-1214
    • Ohgo, K.1    Kawase, T.2    Ashida, J.3    Asakura, T.4
  • 59
    • 34247862118 scopus 로고    scopus 로고
    • Lamellar structure in poly(Ala-Gly) determined by solid-state NMR and statistical mechanical calculations
    • DOI 10.1021/ja070128h
    • T. Asakura, H. Sato, F. Moro, Y. Nakazawa, and A. Aoki Lamellar structure in Poly(Ala-Gly) determined by solid-state NMR and statistical mechanical calculations J. Am. Chem. Soc. 129 2007 5703 5709 (Pubitemid 46697661)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.17 , pp. 5703-5709
    • Asakura, T.1    Sato, H.2    Moro, F.3    Nakazawa, Y.4    Aoki, A.5
  • 62
    • 0032615011 scopus 로고    scopus 로고
    • Solid-State Dipolar INADEQUATE NMR Spectroscopy with a Large Double-Quantum Spectral Width
    • M. Hong Solid-state dipolar INADEQUATE NMR spectroscopy with a large double-quantum spectral width J. Magn. Reson. 136 1999 86 91 (Pubitemid 129607250)
    • (1999) Journal of Magnetic Resonance , vol.136 , Issue.1 , pp. 86-91
    • Hong, M.1
  • 63
    • 0030883873 scopus 로고    scopus 로고
    • Determination of through-bond carbon-carbon connectivities in solid-state NMR using the INADEAUATE experiment
    • DOI 10.1021/ja971089k
    • A. Lesage, C. Auger, S. Caldarelli, and L. Emsley Determination of through-bond carbon-carbon connectivities in solid-state NMR using the INADEQUATE experiment J. Am. Chem. Soc. 119 1997 7867 7868 (Pubitemid 27376404)
    • (1997) Journal of the American Chemical Society , vol.119 , Issue.33 , pp. 7867-7868
    • Lesage, A.1    Auger, C.2    Caldarelli, S.3    Emsley, L.4
  • 64
    • 0033485482 scopus 로고    scopus 로고
    • Through-bond carbon-Carbon connectivities in disordered solids by NMR
    • A. Lesage, M. Bardet, and L. Emsley Determination of through-bond carbon-carbon connectivities in disordered solids by NMR J. Am. Chem. Soc. 121 1999 10987 10993 (Pubitemid 129541231)
    • (1999) Journal of the American Chemical Society , vol.121 , Issue.47 , pp. 10987-10993
    • Lesage, A.1    Bardet, M.2    Emsley, L.3
  • 65
    • 34548403387 scopus 로고    scopus 로고
    • The refocused INADEQUATE MAS NMR experiment in multiple spin-systems: Interpreting observed correlation peaks and optimising lineshapes
    • DOI 10.1016/j.jmr.2007.05.016, PII S1090780707001589
    • S. Cadars, J. Sein, L. Duma, A. Lesage, T.N. Pham, J.H. Baltisberger, S.P. Brown, and L. Emsley The refocused INADEQUATE MAS NMR experiment in multiple spin-systems: interpreting observed correlation peaks and optimising lineshapes J. Magn. Reson. 188 2007 24 34 (Pubitemid 47369668)
    • (2007) Journal of Magnetic Resonance , vol.188 , Issue.1 , pp. 24-34
    • Cadars, S.1    Sein, J.2    Duma, L.3    Lesage, A.4    Pham, T.N.5    Baltisberger, J.H.6    Brown, S.P.7    Emsley, L.8
  • 66
    • 0000448380 scopus 로고
    • Double-quantum filtering in magic-angle-spinning NMR-spectroscopy-an approach to spectral simplification and molecular-structure determination
    • R. Tycko, and G. Dabbagh Double-quantum filtering in magic-angle-spinning NMR-spectroscopy-an approach to spectral simplification and molecular-structure determination J. Am. Chem. Soc. 113 1991 9444 9448
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 9444-9448
    • Tycko, R.1    Dabbagh, G.2
  • 67
    • 0001537199 scopus 로고
    • An NMR technique for tracing out the carbon skeleton of an organic molecule
    • A. Bax, R. Freeman, and T.A. Frenkiel An NMR technique for tracing out the carbon skeleton of an organic molecule J. Am. Chem. Soc. 103 1981 2102 2104
    • (1981) J. Am. Chem. Soc. , vol.103 , pp. 2102-2104
    • Bax, A.1    Freeman, R.2    Frenkiel, T.A.3
  • 68
    • 49049151387 scopus 로고
    • Assignment of C-13 NMR-spectra via double-quantum coherence
    • A. Bax, R. Freeman, T.A. Frenkiel, and M.H. Levitt Assignment of C-13 NMR-spectra via double-quantum coherence J. Magn. Reson. 43 1981 478 483
    • (1981) J. Magn. Reson. , vol.43 , pp. 478-483
    • Bax, A.1    Freeman, R.2    Frenkiel, T.A.3    Levitt, M.H.4
  • 70
    • 77954656138 scopus 로고    scopus 로고
    • Recent developments in liquid-state INADEQUATE studies
    • A. Webb, Elsevier
    • D. Uhrin Recent developments in liquid-state INADEQUATE studies A. Webb, Annual Reports on NMR Spectroscopy vol. 70 2010 Elsevier 2 34
    • (2010) Annual Reports on NMR Spectroscopy , vol.70 VOL. , pp. 2-34
    • Uhrin, D.1
  • 71
    • 0033485482 scopus 로고    scopus 로고
    • Through-bond carbon-Carbon connectivities in disordered solids by NMR
    • A. Lesage, M. Bardet, and L. Emsley Through-bond carbon-carbon connectivities in disordered solids by NMR J. Am. Chem. Soc. 121 1999 10987 10993 (Pubitemid 129541231)
    • (1999) Journal of the American Chemical Society , vol.121 , Issue.47 , pp. 10987-10993
    • Lesage, A.1    Bardet, M.2    Emsley, L.3
  • 73
    • 0037194998 scopus 로고    scopus 로고
    • 60: Refocused INADEQUATE experiments
    • DOI 10.1021/jp026093j
    • G. Grasso, T.M. de Swiet, and J.J. Titman Electronic structure of the polymer phase of CsC60: refocused INADEQUATE experiments J. Phys. Chem. B 106 2002 8676 8680 (Pubitemid 35382876)
    • (2002) Journal of Physical Chemistry B , vol.106 , Issue.34 , pp. 8676-8680
    • Grasso, G.1    De Swiet, T.M.2    Titman, J.J.3
  • 75
    • 0040729295 scopus 로고
    • Applicability of the C-13 NMR inadequate experiment to lignin, a natural polymer
    • E. Guittet, J.Y. Lallemand, C. Lapierre, and B. Monties Applicability of the C-13 NMR inadequate experiment to lignin, a natural polymer Tetrahedron Lett. 26 1985 2671 2674
    • (1985) Tetrahedron Lett. , vol.26 , pp. 2671-2674
    • Guittet, E.1    Lallemand, J.Y.2    Lapierre, C.3    Monties, B.4
  • 77
    • 0024127905 scopus 로고
    • Pentad assignments of methine carbon resonances in stereoregular ethylene propylene copolymer based on two-dimensional inadequate NMR-spectrum
    • T. Hayashi, Y. Inoue, R. Chujo, and T. Asakura Pentad assignments of methine carbon resonances in stereoregular ethylene propylene copolymer based on two-dimensional inadequate NMR-spectrum Polym. J. 20 1988 895 902
    • (1988) Polym. J. , vol.20 , pp. 895-902
    • Hayashi, T.1    Inoue, Y.2    Chujo, R.3    Asakura, T.4
  • 78
    • 55849111582 scopus 로고    scopus 로고
    • Quantifying the fraction of glycine and alanine in β-sheet and helical structures in spider dragline silk using solid-state NMR
    • G.P. Holland, J.E. Jenkins, M.S. Creager, R.V. Lewis, and J.L. Yarger Quantifying the fraction of glycine and alanine in β-sheet and helical structures in spider dragline silk using solid-state NMR Chem. Commun. 2008 5568 5570
    • (2008) Chem. Commun. , pp. 5568-5570
    • Holland, G.P.1    Jenkins, J.E.2    Creager, M.S.3    Lewis, R.V.4    Yarger, J.L.5
  • 79
    • 0030142818 scopus 로고    scopus 로고
    • A double-quantum solid-state NMR technique for determining torsion angles in polymers
    • K. Schmidt-Rohr A double-quantum solid-state NMR technique for determining torsion angles in polymers Macromolecules 29 1996 3975 3981 (Pubitemid 126520381)
    • (1996) Macromolecules , vol.29 , Issue.11 , pp. 3975-3981
    • Schmidt-Rohr, K.1
  • 80
    • 0032076265 scopus 로고    scopus 로고
    • Elucidation of the chain conformation in a glassy polyester, PET, by two-dimensional NMR
    • DOI 10.1126/science.280.5364.714
    • K. Schmidt-Rohr, W. Hu, and N. Zumbulyadis Elucidation of the chain conformation in a glassy polyester, PET, by two-dimensional NMR Science 280 1998 714 717 (Pubitemid 28243340)
    • (1998) Science , vol.280 , Issue.5364 , pp. 714-717
    • Schmidt-Rohr, K.1    Hu, W.2    Zumbulyadis, N.3
  • 81
    • 0034729680 scopus 로고    scopus 로고
    • Solid-state NMR determination of the secondary structure of Samia cynthia ricini silk
    • DOI 10.1038/35016625
    • J.D. van Beek, L. Beaulieu, H. Schafer, M. Demura, T. Asakura, and B.H. Meier Solid-state NMR determination of the secondary structure of Samia cynthia ricini silk Nature 405 2000 1077 1079 (Pubitemid 30447795)
    • (2000) Nature , vol.405 , Issue.6790 , pp. 1077-1079
    • Van Beek, J.D.1    Beaulleu, L.2    Schafer, H.3    Demura, M.4    Asakura, T.5    Meler, B.H.6
  • 82
    • 28844470727 scopus 로고    scopus 로고
    • A DOQSY approach for the elucidation of torsion angle distributions in biopolymers: Application to silk
    • DOI 10.1016/j.jmr.2005.09.004, PII S1090780705002995
    • J.D. van Beek, and B.H. Meier A DOQSY approach for the elucidation of torsion angle distributions in biopolymers: application to silk J. Magn. Reson. 178 2006 106 120 (Pubitemid 41774017)
    • (2006) Journal of Magnetic Resonance , vol.178 , Issue.1 , pp. 106-120
    • Van Beek, J.D.1    Meier, B.H.2
  • 83
    • 0041708442 scopus 로고    scopus 로고
    • Inverse methods in two-dimensional NMR spectral analysis
    • J.D. van Beek, B.H. Meier, and H. Schafer Inverse methods in two-dimensional NMR spectral analysis J. Magn. Reson. 162 2003 141 157
    • (2003) J. Magn. Reson. , vol.162 , pp. 141-157
    • Van Beek, J.D.1    Meier, B.H.2    Schafer, H.3
  • 84
    • 36449008649 scopus 로고
    • 2-Dimensional nuclear-magnetic-resonance with sample flip for characterizing orientation distributions, and its analogy to X-ray-scattering
    • K. Schmidt-Rohr, M. Hehn, D. Schaefer, and H.W. Spiess 2-Dimensional nuclear-magnetic-resonance with sample flip for characterizing orientation distributions, and its analogy to X-ray-scattering J. Chem. Phys. 97 1992 2247 2262
    • (1992) J. Chem. Phys. , vol.97 , pp. 2247-2262
    • Schmidt-Rohr, K.1    Hehn, M.2    Schaefer, D.3    Spiess, H.W.4
  • 85
    • 2542561209 scopus 로고    scopus 로고
    • A DECODER NMR study of backbone orientation in Nephila clavipes dragline silk under varying strain and draw rate
    • DOI 10.1021/bm0342685
    • P. Eles, and C. Michal A DECODER NMR study of backbone orientation in Nephila clavipes dragline silk under varying strain and draw rate Biomacromolecules 5 2004 661 665 (Pubitemid 38702230)
    • (2004) Biomacromolecules , vol.5 , Issue.3 , pp. 661-665
    • Eles, P.T.1    Michal, C.A.2
  • 86
    • 0037025129 scopus 로고    scopus 로고
    • Determination of intermolecular distance for a model peptide of Bombyx mori silk fibroin, GAGAG, with rotational echo double resonance
    • DOI 10.1002/bip.10132
    • T. Kameda, Y. Nakazawa, J. Kazuhara, T. Yamane, and T. Asakura Determination of intermolecular distance for a model peptide of Bombyx mori silk fibroin, GAGAG, with rotational echo double resonance Biopolymers 64 2002 80 85 (Pubitemid 34712558)
    • (2002) Biopolymers , vol.64 , Issue.2 , pp. 80-85
    • Kameda, T.1    Nakazawa, Y.2    Kazuhara, J.3    Yamane, T.4    Asakura, T.5
  • 87
    • 0041347970 scopus 로고    scopus 로고
    • Structure of Bombyx mori silk fibroin before spinning in silkworm
    • H.N. Cheng, A.D. English (Eds.) Oxford University Press, Washington 2003
    • T. Asakura, J. Ashida, T. Yamane, Structure of Bombyx mori silk fibroin before spinning in silkworm, in: H.N. Cheng, A.D. English (Eds.), ACS Symposium Series, 834, Oxford University Press, Washington 2003, pp. 71-82.
    • ACS Symposium Series , vol.834 , pp. 71-82
    • Asakura, T.1    Ashida, J.2    Yamane, T.3
  • 88
    • 0037487194 scopus 로고    scopus 로고
    • Determination of distance of intra-molecular hydrogen bonding in (Ala-Gly)15 with Silk i form after removal of the effect of MAS frequency in REDOR experiment
    • T. Kameda, C. Zhao, J. Ashida, and T. Asakura Determination of distance of intra-molecular hydrogen bonding in (Ala-Gly)15 with Silk I form after removal of the effect of MAS frequency in REDOR experiment J. Magn. Reson. 160 2003 91 96
    • (2003) J. Magn. Reson. , vol.160 , pp. 91-96
    • Kameda, T.1    Zhao, C.2    Ashida, J.3    Asakura, T.4
  • 91
    • 4544336281 scopus 로고    scopus 로고
    • Structure and structural changes of the silk fibroin from Samia cynthia ricini using nuclear magnetic resonance spectroscopy
    • DOI 10.1002/mabi.200300098, Highlights from the First IUPAC International Conference on Bio-based Polymers (ICBP 2003)
    • T. Asakura, and Y. Nakazawa Structure and structural changes of the silk fibroin from Samia cynthia ricini using nuclear magnetic resonance spectroscopy Macromol. Biosci. 4 2004 175 185 (Pubitemid 39257177)
    • (2004) Macromolecular Bioscience , vol.4 , Issue.3 , pp. 175-185
    • Asakura, T.1    Nakazawa, Y.2
  • 93
    • 77951051647 scopus 로고    scopus 로고
    • 5, studied with solid-state NMR:REDOR
    • 5, studied with solid-state NMR:REDOR Polym. J. 42 2010 354 356
    • (2010) Polym. J. , vol.42 , pp. 354-356
    • Suzuki, Y.1    Asakura, T.2
  • 94
    • 0032134545 scopus 로고    scopus 로고
    • Rotational-echo double-resonance in complex biopolymers: A study of Nephila clavipes dragline silk
    • C.A. Michal, and L.W. Jelinski Rotational-echo double-resonance in complex biopolymers: a study of Nephila clavipes dragline silk J. Biomol. NMR 12 1998 231 241 (Pubitemid 128511288)
    • (1998) Journal of Biomolecular NMR , vol.12 , Issue.2 , pp. 231-241
    • Michal, C.A.1    Jelinski, L.W.2
  • 95
    • 66149149450 scopus 로고    scopus 로고
    • Water permeability of spider dragline silk
    • X. Li, P.T. Eles, and C.A. Michal Water permeability of spider dragline silk Biomacromolecules 10 2009 1270 1275
    • (2009) Biomacromolecules , vol.10 , pp. 1270-1275
    • Li, X.1    Eles, P.T.2    Michal, C.A.3
  • 96
    • 0030449483 scopus 로고    scopus 로고
    • Gradient, high resolution, magic angle sample spinning NMR
    • DOI 10.1021/ja962227t, PII S0002786396022275
    • W.E. Mass, F.H. Laukien, and D.G. Cory Gradient, high resolution, magic angle spinning NMR J. Am. Chem. Soc. 118 1996 13085 13086 (Pubitemid 27055320)
    • (1996) Journal of the American Chemical Society , vol.118 , Issue.51 , pp. 13085-13086
    • Maas, W.E.1    Laukien, F.H.2    Cory, D.G.3
  • 98
    • 37049012852 scopus 로고    scopus 로고
    • Pulsed field gradient magic angle spinning NMR self-diffusion measurements in liquids
    • DOI 10.1016/j.jmr.2007.10.010, PII S109078070700331X
    • S. Viel, F. Ziarelli, G. Pagès, C. Carrara, and S. Caldarelli Pulsed field gradient magic angle spinning NMR self-diffusion measurements in liquids J. Magn. Reson. 190 2008 113 123 (Pubitemid 350245451)
    • (2008) Journal of Magnetic Resonance , vol.190 , Issue.1 , pp. 113-123
    • Viel, S.1    Ziarelli, F.2    Pages, G.3    Carrara, C.4    Caldarelli, S.5
  • 99
    • 84856714098 scopus 로고    scopus 로고
    • High resolution magic angle spinning NMR investigation of silk protein structure within major ampullate glands of orb weaving spiders
    • J.E. Jenkins, G.P. Holland, and J.L. Yarger High resolution magic angle spinning NMR investigation of silk protein structure within major ampullate glands of orb weaving spiders Soft Matter 8 2012 1947 1954
    • (2012) Soft Matter , vol.8 , pp. 1947-1954
    • Jenkins, J.E.1    Holland, G.P.2    Yarger, J.L.3
  • 101
    • 2542626630 scopus 로고    scopus 로고
    • NMR characterization of native liquid spider dragline silk from Nephila edulis
    • DOI 10.1021/bm0343904
    • M. Hronska, J.D. van Beek, P.T.F. Williamson, F. Vollrath, and B.H. Meier NMR characterization of native liquid spider dragline silk from Nephila edulis Biomacromolecules 5 2004 834 839 (Pubitemid 38702253)
    • (2004) Biomacromolecules , vol.5 , Issue.3 , pp. 834-839
    • Hronska, M.1    Van Beek, J.D.2    Williamson, P.T.F.3    Vollrath, F.4    Meier, B.H.5
  • 102
    • 33845560617 scopus 로고
    • Enhancement of nuclear magnetic resonance signals by polarization transfer
    • G.A. Morris, and R. Freeman Enhancement of nuclear magnetic resonance signals by polarization transfer J. Am. Chem. Soc. 101 1979 760 762
    • (1979) J. Am. Chem. Soc. , vol.101 , pp. 760-762
    • Morris, G.A.1    Freeman, R.2
  • 103
    • 0000195671 scopus 로고
    • Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy
    • G. Bodenhausen, and D.J. Ruben Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy Chem. Phys. Lett. 69 1980 185 189
    • (1980) Chem. Phys. Lett. , vol.69 , pp. 185-189
    • Bodenhausen, G.1    Ruben, D.J.2
  • 105
    • 0015223476 scopus 로고
    • The crystal structures of Poly(LAla-Gly-Gly-Gly) II and Poly(LAla-Gly-Gly) II
    • B. Lotz, and H.D. Keith The crystal structures of Poly(LAla-Gly-Gly-Gly) II and Poly(LAla-Gly-Gly) II J. Mol. Biol. 61 1971 195 200
    • (1971) J. Mol. Biol. , vol.61 , pp. 195-200
    • Lotz, B.1    Keith, H.D.2
  • 106
    • 0018401676 scopus 로고
    • The chemical structure and the crystalline structures of Bombyx mori silk fibroin
    • B. Lotz, and F.C. Cesari The chemical structure and the crystalline structures of Bombyx mori silk fibroin Biochimie 61 1979 205 214
    • (1979) Biochimie , vol.61 , pp. 205-214
    • Lotz, B.1    Cesari, F.C.2
  • 107
    • 0026253604 scopus 로고
    • Conformational energy studies of β-sheets of model silk fibroin peptides. I. Sheets of Poly(Ala-Gly) chains
    • A.S. Fossey, G. Nemethy, D.K. Gibson, and A.H. Scheraga Conformational energy studies of β-sheets of model silk fibroin peptides. I. Sheets of Poly(Ala-Gly) chains Biopolymers 31 1991 1529 1541
    • (1991) Biopolymers , vol.31 , pp. 1529-1541
    • Fossey, A.S.1    Nemethy, G.2    Gibson, D.K.3    Scheraga, A.H.4
  • 108
    • 0035888273 scopus 로고    scopus 로고
    • 2-Ser-Gly peptide sequence
    • DOI 10.1002/1097-0282(20011015)59: 5<310::AID-BIP1028>3.0.CO;2-5
    • K. Okuyama, R. Somashekar, K. Noguchi, and S. Ichimura Refined molecular and crystal structure of Silk I based on Ala-Gly and (Ala-Gly)(2)-Ser-Gly peptide sequence Biopolymers 59 2001 310 319 (Pubitemid 32924184)
    • (2001) Biopolymers , vol.59 , Issue.5 , pp. 310-319
    • Okuyama, K.1    Somashekar, R.2    Noguchi, K.3    Ichimura, S.4
  • 109
    • 0037027580 scopus 로고    scopus 로고
    • The structural characteristics of Bombyx mori silk fibroin before spinning as studied with molecular dynamics simulation
    • DOI 10.1021/ma0209390
    • T. Yamane, K. Umemura, and T. Asakura The structural characteristics of Bombyx mori silk fibroin before spinning as studied with molecular dynamics simulation Macromolecules 35 2002 8831 8838 (Pubitemid 35359225)
    • (2002) Macromolecules , vol.35 , Issue.23 , pp. 8831-8838
    • Yamane, T.1    Umemura, K.2    Asakura, T.3
  • 111
    • 0032956173 scopus 로고    scopus 로고
    • Structure refinement and diffuse streak scattering of silk (Bombyx mori)
    • DOI 10.1016/S0141-8130(98)00080-4, PII S0141813098000804
    • Y. Takahashi, M. Gehoh, and K. Yuzuriha Structure refinement and diffuse streak scattering of silk (Bombyx mori) Int. J. Biol. Macromol. 24 1999 127 138 (Pubitemid 29227194)
    • (1999) International Journal of Biological Macromolecules , vol.24 , Issue.2-3 , pp. 127-138
    • Takahashi, Y.1    Gehoh, M.2    Yuzuriha, K.3
  • 112
    • 33947224695 scopus 로고    scopus 로고
    • C-13-O-17 Reapdor NMR as a tool for determining secondary structure in polyamides
    • T. Gullion, K. Yamauchi, M. Okonogi, and T. Asakura C-13-O-17 Reapdor NMR as a tool for determining secondary structure in polyamides Macromolecules 40 2007 1363 1365
    • (2007) Macromolecules , vol.40 , pp. 1363-1365
    • Gullion, T.1    Yamauchi, K.2    Okonogi, M.3    Asakura, T.4
  • 116
    • 0036839389 scopus 로고    scopus 로고
    • 13C CP/MAS NMR study on structural heterogeneity in Bombyx mori silk fiber and their generation by stretching
    • DOI 10.1110/ps.0221702
    • 13C CP/MAS NMR study on structural heterogeneity in Bombyx mori silk fiber and their generation by stretching Protein Sci. 11 2002 2706 2713 (Pubitemid 35191144)
    • (2002) Protein Science , vol.11 , Issue.11 , pp. 2706-2713
    • Asakura, T.1    Yao, J.2
  • 117
    • 0000890258 scopus 로고
    • 13C NMR study of silk fibroin in the solid state by the cross-polarization-magic angle spinning method. Conformational characterization of Silk i and Silk II type forms of Bombyx mori fibroin by the conformation-dependent carbon-13 chemical shifts
    • 13C NMR study of silk fibroin in the solid state by the cross-polarization-magic angle spinning method. Conformational characterization of Silk I and Silk II type forms of Bombyx mori fibroin by the conformation-dependent carbon-13 chemical shifts Macromolecules 17 1984 1405 1412
    • (1984) Macromolecules , vol.17 , pp. 1405-1412
    • Saitô, H.1    Tabeta, R.2    Asakura, T.3    Iwanaga, Y.4    Shoji, A.5    Ozaki, T.6    Ando, I.7
  • 118
    • 0000951118 scopus 로고
    • 13C cross polarization-magic angle spinning NMR, X-ray diffraction, and infrared spectroscopy
    • 13C cross polarization-magic angle spinning NMR, X-ray diffraction, and infrared spectroscopy Macromolecules 18 1985 1841 1845
    • (1985) Macromolecules , vol.18 , pp. 1841-1845
    • Asakura, T.1    Kuzuhara, A.2    Tabeta, R.3    Saito, H.4
  • 120
    • 0141459939 scopus 로고    scopus 로고
    • Molecular dynamics simulation of conformational change of Poly(Ala-Gly) from Silk i to Silk II in relation to fiber formation mechanism of Bombyx mori silk fibroin
    • T. Yamane, K. Umemura, Y. Nakazawa, and T. Asakura Molecular dynamics simulation of conformational change of Poly(Ala-Gly) from Silk I to Silk II in relation to fiber formation mechanism of Bombyx mori silk fibroin Macromolecules 36 2003 6766 6772
    • (2003) Macromolecules , vol.36 , pp. 6766-6772
    • Yamane, T.1    Umemura, K.2    Nakazawa, Y.3    Asakura, T.4
  • 121
    • 33750478307 scopus 로고    scopus 로고
    • Comparing the rheology of native spider and silkworm spinning dope
    • DOI 10.1038/nmat1762, PII NMAT1762
    • C. Holland, A.E. Terry, D. Porter, and F. Vollrath Comparing the rheology of native spider and silkworm spinning dope Nat. Mater. 5 2006 870 874 (Pubitemid 44658571)
    • (2006) Nature Materials , vol.5 , Issue.11 , pp. 870-874
    • Holland, C.1    Terry, A.E.2    Porter, D.3    Vollrath, F.4
  • 122
    • 0036859560 scopus 로고    scopus 로고
    • Rheology and dynamic light scattering of silk fibroin solution extracted from the middle division of Bombyx mori silkworm
    • DOI 10.1021/bm020056g
    • A. Ochi, K.S. Hossain, J. Magoshi, and N. Nemoto Rheology and dynamic light scattering of silk fibroin solution extracted from the middle division of Bombyx mori silkworm Biomacromolecules 3 2002 1187 1196 (Pubitemid 35423018)
    • (2002) Biomacromolecules , vol.3 , Issue.6 , pp. 1187-1196
    • Ochi, A.1    Hossain, K.S.2    Magoshi, J.3    Nemoto, N.4
  • 123
    • 2542643108 scopus 로고    scopus 로고
    • PH induced changes in the rheology of silk fibroin solution from the middle division of Bombyx mori silkworm
    • DOI 10.1021/bm034381v
    • A.E. Terry, D.P. Knight, D. Porter, and F. Vollrath PH induced changes in the rheology of silk fibroin solution from the middle division of Bombyx mori silkworm Biomacromolecules 5 2004 768 772 (Pubitemid 38702244)
    • (2004) Biomacromolecules , vol.5 , Issue.3 , pp. 768-772
    • Terry, A.E.1    Knight, D.P.2    Porter, D.3    Vollrath, F.4
  • 124
    • 84996415347 scopus 로고
    • On the fiber formation of liquid silk in the spinneret
    • K. Kataoka, and I. Uematsu On the fiber formation of liquid silk in the spinneret Koubunshi Ronbunshu 34 1977 457 464
    • (1977) Koubunshi Ronbunshu , vol.34 , pp. 457-464
    • Kataoka, K.1    Uematsu, I.2
  • 125
    • 85024739032 scopus 로고    scopus 로고
    • Fiber formation of silkworm and crystallization of silk
    • J. Magoshi, and Y. Magoshi Fiber formation of silkworm and crystallization of silk Sen-I Gakkaishi 63 2007 244 252
    • (2007) Sen-I Gakkaishi , vol.63 , pp. 244-252
    • Magoshi, J.1    Magoshi, Y.2
  • 127
    • 34249101345 scopus 로고    scopus 로고
    • Natural and unnatural silks
    • DOI 10.1016/j.polymer.2007.04.019, PII S0032386107003989
    • C. Holland, A.E. Terry, D. Porter, and F. Vollrath Natural and unnatural silks Polymer 48 2007 3388 3392 (Pubitemid 46802672)
    • (2007) Polymer , vol.48 , Issue.12 , pp. 3388-3392
    • Holland, C.1    Terry, A.E.2    Porter, D.3    Vollrath, F.4
  • 128
    • 0013914668 scopus 로고
    • Mechanism of fiber formation by the silkworm, Bombyx mori L
    • E. Iizuka Mechanism of fiber formation by the silkworm, Bombyx mori L. Biorheology 3 1966 141 152
    • (1966) Biorheology , vol.3 , pp. 141-152
    • Iizuka, E.1
  • 129
    • 84963388465 scopus 로고
    • Mechanical denaturation of high polymers in solutions. XXXVI. Flow-induced crystallization of Bombyx mori L. silk fibroin from the aqueous solution under a steady-state flow
    • K. Yamaura, Y. Okumura, and S. Matsuzawa Mechanical denaturation of high polymers in solutions. XXXVI. Flow-induced crystallization of Bombyx mori L. silk fibroin from the aqueous solution under a steady-state flow J. Macromol. Sci.-Phys. B21 1982 49 69
    • (1982) J. Macromol. Sci.-Phys. , vol.21 B , pp. 49-69
    • Yamaura, K.1    Okumura, Y.2    Matsuzawa, S.3
  • 130
    • 0009715073 scopus 로고
    • The physico-chemical properties of silk fibers and the fiber spinning process
    • E. Iizuka The physico-chemical properties of silk fibers and the fiber spinning process Experientia 39 1983 449 454
    • (1983) Experientia , vol.39 , pp. 449-454
    • Iizuka, E.1
  • 132
    • 33846427680 scopus 로고    scopus 로고
    • Some observations on the structure and function of the spinning apparatus in the silkworm Bombyx mori
    • DOI 10.1021/bm060874z
    • T. Asakura, K. Umemura, Y. Nakazawa, H. Hirose, J. Higham, and D. Knight Some observations on the structure and function of the spinning apparatus in the silkworm Bombyx mori Biomacromolecules 8 2007 175 181 (Pubitemid 46140489)
    • (2007) Biomacromolecules , vol.8 , Issue.1 , pp. 175-181
    • Asakura, T.1    Umemura, K.2    Nakazawa, Y.3    Hirose, H.4    Higham, J.5    Knight, D.6
  • 133
    • 65249171938 scopus 로고    scopus 로고
    • Rheological properties of native silk fibroins from domestic and wild silkworms, and flow analysis in each spinneret by a finite element method
    • M. Moriya, F. Roschzttrdtz, Y. Nakahara, H. Saito, Y. Masubuchi, and T. Asakura Rheological properties of native silk fibroins from domestic and wild silkworms, and flow analysis in each spinneret by a finite element method Biomacromolecules 10 2009 929 935
    • (2009) Biomacromolecules , vol.10 , pp. 929-935
    • Moriya, M.1    Roschzttrdtz, F.2    Nakahara, Y.3    Saito, H.4    Masubuchi, Y.5    Asakura, T.6
  • 134
    • 39049163300 scopus 로고    scopus 로고
    • Flow analysis of aqueous solution of silk fibroin in the spinneret of Bombyx mori silkworm by combination of viscosity measurement and finite element method calculation
    • M. Moriya, K. Ohgo, Y. Masubuchi, and T. Asakura Flow analysis of aqueous solution of silk fibroin in the spinneret of Bombyx mori silkworm by combination of viscosity measurement and finite element method calculation Polymer 49 2008 952 956
    • (2008) Polymer , vol.49 , pp. 952-956
    • Moriya, M.1    Ohgo, K.2    Masubuchi, Y.3    Asakura, T.4
  • 135
    • 56749164861 scopus 로고    scopus 로고
    • Micro-computerized tomographic observation of the spinning apparatus in Bombyx mori silkworms
    • M. Moriya, K. Ohgo, Y. Masubuchi, D.P. Knight, and T. Asakura Micro-computerized tomographic observation of the spinning apparatus in Bombyx mori silkworms Polymer 49 2008 5665 5669
    • (2008) Polymer , vol.49 , pp. 5665-5669
    • Moriya, M.1    Ohgo, K.2    Masubuchi, Y.3    Knight, D.P.4    Asakura, T.5
  • 137
    • 2542564210 scopus 로고    scopus 로고
    • X-ray evidence for a "super"-secondary structure in silk fibers
    • DOI 10.1021/bm0343085
    • R. Valluzzi, and H.J. Jin X-ray evidence for a super-secondary structure in silk fibers Biomacromolecules 5 2004 696 703 (Pubitemid 38702234)
    • (2004) Biomacromolecules , vol.5 , Issue.3 , pp. 696-703
    • Valluzzi, R.1    Jin, H.-J.2
  • 138
    • 25844435246 scopus 로고    scopus 로고
    • 13C solid-state NMR spectroscopy for a lamella structure in an alanine-glycine copolypeptide: A model for the crystalline domain of Bombyx mori silk fiber
    • DOI 10.1110/ps.051525505
    • 13C solid-state NMR spectroscopy for a lamella structure in an alanine-glycine copolypeptide: a model for the crystalline domain of Bombyx mori silk fiber Protein Sci. 14 2005 2654 2657 (Pubitemid 41395591)
    • (2005) Protein Science , vol.14 , Issue.10 , pp. 2654-2657
    • Asakura, T.1    Nakazawa, Y.2    Ohnishi, E.3    Moro, F.4
  • 141
    • 38849117672 scopus 로고    scopus 로고
    • Synthesis and characterization of silklike materials containing the calcium-binding sequence from Calbindin D9k or the shell nacreous matrix protein MSI60
    • DOI 10.1021/bm700665m
    • M. Yang, T. Muto, D.P. Knight, A.M. Collins, and T. Asakura Synthesis and characterization of silk-like materials containing the calcium-binding sequence from Calbindin D9k or the shell nacreous matrix protein MSI60 Biomacromolecules 9 2008 416 420 (Pubitemid 351201628)
    • (2008) Biomacromolecules , vol.9 , Issue.1 , pp. 416-420
    • Yang, M.1    Muto, T.2    Knight, D.3    Collins, A.M.4    Asakura, T.5
  • 142
    • 79251648023 scopus 로고    scopus 로고
    • Regeneration of the femoral epicondyle on calcium-binding silk scaffolds developed using transgenic silk fibroin produced by transgenic silkworm
    • A. Nagano, Y. Tanioka, N. Sakurai, H. Sezutsu, N. Kuboyama, H. Kiba, Y. Tanimoto,.N. Nishiyama, and T. Asakura Regeneration of the femoral epicondyle on calcium-binding silk scaffolds developed using transgenic silk fibroin produced by transgenic silkworm Acta Biomater. 7 2011 1192 1201
    • (2011) Acta Biomater. , vol.7 , pp. 1192-1201
    • Nagano, A.1    Tanioka, Y.2    Sakurai, N.3    Sezutsu, H.4    Kuboyama, N.5    Kiba, H.6    Tanimoto, Y.7    Nishiyama, N.8    Asakura, T.9
  • 143
    • 84875089369 scopus 로고    scopus 로고
    • K. Yukuhiro, personal communication, 1998.
    • K. Yukuhiro, personal communication, 1998.
  • 144
    • 0031081695 scopus 로고    scopus 로고
    • Preferential codon usage and two types of repetitive motifs in the fibroin gene of the Chinese oak silkworm, Antheraea pernyi
    • K. Yukuhiro, T. Kanda, and T. Tamura Preferential codon usage and two types of repetitive motifs in the fibroin gene of the Chinese oak silkworm, Antheraea pernyi Insect Mol. Biol. 6 1997 89 95 (Pubitemid 27102786)
    • (1997) Insect Molecular Biology , vol.6 , Issue.1 , pp. 89-95
    • Yukuhiro, K.1    Kanda, T.2    Tamura, T.3
  • 145
    • 0033759526 scopus 로고    scopus 로고
    • Dynamic rearrangement within the Antheraea pernyi silk fibroin gene is associated with four types of repetitive units
    • H. Sezutsu, and K. Yukuhiro Dynamic rearrangement within the Antheraea pernyi silk fibroin gene is associated with four types of repetitive units J. Mol. Evol. 51 2000 329 338
    • (2000) J. Mol. Evol. , vol.51 , pp. 329-338
    • Sezutsu, H.1    Yukuhiro, K.2
  • 147
    • 0023984390 scopus 로고
    • 13C NMR analysis of the conformation and the conformational transition of Philosamia cynthia ricini silk fibroin protein on the basis of Bixon-Scheraga-Lifson theory
    • 13C NMR analysis of the conformation and the conformational transition of Philosamia cynthia ricini silk fibroin protein on the basis of Bixon-Scheraga-Lifson theory Macromolecules 21 1988 644 648 (Pubitemid 18618585)
    • (1988) Macromolecules , vol.21 , Issue.3 , pp. 644-648
    • Asakura Tetsuo1    Kashiba Hitoshi2    Yoshimizu Hiroaki3
  • 149
    • 0005123403 scopus 로고    scopus 로고
    • Dynamics of silk fibroin studied with nuclear magnetic resonance spectroscopy
    • A. Webb, I. Ando, Academic Press
    • T. Kameda, and T. Asakura Dynamics of silk fibroin studied with nuclear magnetic resonance spectroscopy A. Webb, I. Ando, Annual Reports on NMR Spectroscopy vol. 46 2002 Academic Press 102 149
    • (2002) Annual Reports on NMR Spectroscopy , vol.46 VOL. , pp. 102-149
    • Kameda, T.1    Asakura, T.2
  • 151
    • 2442716590 scopus 로고    scopus 로고
    • Spectroscopic characterization of heterogeneous structure of Samia cynthia ricini silk fibroin induced by stretching and molecular dynamics simulation
    • M. Yang, J. Yao, M. Sonoyama, and T. Asakura Spectroscopic characterization of heterogeneous structure of Samia cynthia ricini silk fibroin induced by stretching and molecular dynamics simulation Macromolecules 37 2004 3497 3504
    • (2004) Macromolecules , vol.37 , pp. 3497-3504
    • Yang, M.1    Yao, J.2    Sonoyama, M.3    Asakura, T.4
  • 154
    • 0037066217 scopus 로고    scopus 로고
    • 13C CP/MAS NMR study on structure and structural transition of Antheraea pernyi silk fibroin containing poly(L-alanine) and Gly-rich regions
    • DOI 10.1021/ma011999t
    • 13C CP/MAS NMR study on structure and structural transition of Antheraea pernyi silk fibroin containing Poly(l-alanine) and Gly rich regions Macromolecules 35 2002 2393 2400 (Pubitemid 34586227)
    • (2002) Macromolecules , vol.35 , Issue.6 , pp. 2393-2400
    • Nakazawa, Y.1    Asakura, T.2
  • 156
    • 84894141714 scopus 로고
    • Structure and molecular conformation of Tussah silk fibroin films: Effect of methanol
    • M. Tsukada, G. Freddi, P. Monti, and A. Bertoluzza Structure and molecular conformation of Tussah silk fibroin films: effect of methanol J. Polym. Sci.: Polym Phys. Ed. 33 1995 1995 2001
    • (1995) J. Polym. Sci.: Polym Phys. Ed. , vol.33 , pp. 1995-2001
    • Tsukada, M.1    Freddi, G.2    Monti, P.3    Bertoluzza, A.4
  • 157
    • 0001124562 scopus 로고
    • 13C NMR study of the chain dynamics and solution structure of Bombyx mori silk fiboin
    • 13C NMR study of the chain dynamics and solution structure of Bombyx mori silk fiboin Macromolecules 17 1984 1075 1081
    • (1984) Macromolecules , vol.17 , pp. 1075-1081
    • Asakura, T.1    Watanabe, Y.2    Uchida, A.3    Minagawa, H.4
  • 159
    • 65249189859 scopus 로고    scopus 로고
    • Fine-structural characterization of Anaphe cocoon filament
    • H. Akai, and T. Nakashima Fine-structural characterization of Anaphe cocoon filament Int. J. Wild Silkmoth & Silk 4 1999 13 16
    • (1999) Int. J. Wild Silkmoth & Silk , vol.4 , pp. 13-16
    • Akai, H.1    Nakashima, T.2
  • 163
    • 85010247017 scopus 로고
    • Poly-l-alanylglycyl-l-alanylglycyl-l-serylglycine: A model for the crystalline regions of silk fibroin
    • R.D. Fraser, T.P. MacRae, and F.H. Stewart Poly-l-alanylglycyl-l- alanylglycyl-l-serylglycine: a model for the crystalline regions of silk fibroin J. Mol. Biol. 19 1966 580 582
    • (1966) J. Mol. Biol. , vol.19 , pp. 580-582
    • Fraser, R.D.1    Macrae, T.P.2    Stewart, F.H.3
  • 164
    • 33646507289 scopus 로고    scopus 로고
    • Structural analysis of alanine tripeptide with anti-parallel and parallel β-sheet structures in relation to the analysis of mixed β-sheet structures in Samia cynthia ricini silk protein fiber using solid-state NMR spectroscopy
    • T. Asakura, M. Okonogi, Y. Nakazawa, and K. Yamauchi Structural analysis of alanine tripeptide with anti-parallel and parallel β-sheet structures in relation to the analysis of mixed β-sheet structures in Samia cynthia ricini silk protein fiber using solid-state NMR spectroscopy J. Am. Chem. Soc. 128 2006 6231 6238
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 6231-6238
    • Asakura, T.1    Okonogi, M.2    Nakazawa, Y.3    Yamauchi, K.4
  • 166
    • 0001124563 scopus 로고
    • NMR of silk fibroin. 3. Assignment of carbonyl carbon resonances and their dependence on sequence and conformation in Bombyx mori silk fibroin using selective isotropic labeling
    • T. Asakura, Y. Watanabe, and T. Itoh NMR of silk fibroin. 3. Assignment of carbonyl carbon resonances and their dependence on sequence and conformation in Bombyx mori silk fibroin using selective isotropic labeling Macromolecules 17 1984 2421 2426
    • (1984) Macromolecules , vol.17 , pp. 2421-2426
    • Asakura, T.1    Watanabe, Y.2    Itoh, T.3
  • 169
    • 0842286036 scopus 로고    scopus 로고
    • Structural role of tyrosine in Bombyx mori silk fibroin, studied by solid-state NMR and molecular mechanics on a model peptide prepared as silk I and II
    • DOI 10.1002/mrc.1337
    • T. Asakura, K. Suita, T. Kameda, S. Afonin, and A.S. Ulrich Structural role of tyrosine in Bombyx mori silk fibroin, studied by solid-state NMR and molecular mechanics on a model peptide prepared as Silk I and II Magn. Reson. Chem. 42 2004 258 266 (Pubitemid 38178095)
    • (2004) Magnetic Resonance in Chemistry , vol.42 , Issue.2 , pp. 258-266
    • Asakura, T.1    Suita, K.2    Kameda, T.3    Afonin, S.4    Ulrich, A.S.5
  • 170
    • 0022295095 scopus 로고
    • Viscoelastic behaviour and wet supercontraction of major ampullate silk fibres of certain orb-web-building spiders (Araneae)
    • R.W. Work Viscoelastic behaviour and wet supercontraction of major ampullate silk fibres of certain orb-web-building spiders (Araneae) J. Exp. Biol. 118 1985 379 404 (Pubitemid 16149145)
    • (1985) Journal of Experimental Biology , vol.VOL. 118 , pp. 379-404
    • Work, R.W.1
  • 172
    • 72149114322 scopus 로고    scopus 로고
    • Proton-detected heteronuclear single quantum correlation NMR spectroscopy in rigid solids with ultra-fast MAS
    • G.P. Holland, B.R. Cherry, J.E. Jenkins, and J.L. Yarger Proton-detected heteronuclear single quantum correlation NMR spectroscopy in rigid solids with ultra-fast MAS J. Magn. Reson. 202 2010 64 71
    • (2010) J. Magn. Reson. , vol.202 , pp. 64-71
    • Holland, G.P.1    Cherry, B.R.2    Jenkins, J.E.3    Yarger, J.L.4
  • 173
    • 28544441619 scopus 로고    scopus 로고
    • An NMR approach applicable to biomolecular structure characterization
    • DOI 10.1021/ac051061o
    • B.-W. Hu, P. Zhou, I. Noda, and G.-Z. Zhao An NMR approach applicable to biomolecular structure characterization Anal. Chem. 77 2005 7534 7538 (Pubitemid 41746219)
    • (2005) Analytical Chemistry , vol.77 , Issue.23 , pp. 7534-7538
    • Hu, B.-W.1    Zhou, P.2    Noda, I.3    Zhao, G.-Z.4
  • 175
    • 11944263043 scopus 로고
    • Spider silk: The unraveling of a mystery
    • R.V. Lewis Spider silk: the unraveling of a mystery Acc. Chem. Res. 25 1992 298 392
    • (1992) Acc. Chem. Res. , vol.25 , pp. 298-392
    • Lewis, R.V.1
  • 177
    • 45149145322 scopus 로고
    • Rotational-echo double-resonance NMR
    • T. Gullion, and J. Schaefer Rotational-echo double-resonance NMR J. Magn. Reson. 81 1989 196 200
    • (1989) J. Magn. Reson. , vol.81 , pp. 196-200
    • Gullion, T.1    Schaefer, J.2
  • 179
    • 84858862889 scopus 로고    scopus 로고
    • 13C-labeled peptide, (E)8GGLGGQGAG(A)6GGAGQGGYGG as a model for the local structure of Nephila clavipes dragline silk (MaSp1) before and after spinning
    • 13C-labeled peptide, (E)8GGLGGQGAG(A) 6GGAGQGGYGG as a model for the local structure of Nephila clavipes dragline silk (MaSp1) before and after spinning Biopolymers 97 2012 347 354
    • (2012) Biopolymers , vol.97 , pp. 347-354
    • Yazawa, K.1    Yamaguchi, E.2    Knight, D.P.3    Asakura, T.4
  • 180
    • 67650451406 scopus 로고    scopus 로고
    • Structural analysis of the Gly-rich region in spider dragline silk using stable-isotope labeled sequential model peptides and solid-state NMR
    • E. Yamaguchi, K. Yamauchi, T. Gullion, and T. Asakura Structural analysis of the Gly-rich region in spider dragline silk using stable-isotope labeled sequential model peptides and solid-state NMR Chem. Commun. 2009 4176 4178
    • (2009) Chem. Commun. , pp. 4176-4178
    • Yamaguchi, E.1    Yamauchi, K.2    Gullion, T.3    Asakura, T.4
  • 181
    • 0345118157 scopus 로고    scopus 로고
    • Mapping domain structures in silks from insects and spiders related to protein assembly
    • DOI 10.1016/j.jmb.2003.10.043
    • E. Bini, D.P. Knight, and D.L. Kaplan Mapping domain structures in silks from insects and spiders related to protein assembly J. Mol. Biol. 335 2004 27 40 (Pubitemid 37494959)
    • (2004) Journal of Molecular Biology , vol.335 , Issue.1 , pp. 27-40
    • Bini, E.1    Knight, D.P.2    Kaplan, D.L.3
  • 182
    • 0032488823 scopus 로고    scopus 로고
    • Evidence from flagelliform silk cDNA for the structural basis of elasticity and modular nature of spider silks
    • DOI 10.1006/jmbi.1997.1478
    • C.Y. Hayashi, and R.V. Lewis Evidence from flagelliform silk cDNA for the structural basis of elasticity and modular nature of spider silks J. Mol. Biol. 275 1998 773 784 (Pubitemid 28077695)
    • (1998) Journal of Molecular Biology , vol.275 , Issue.5 , pp. 773-784
    • Hayashi, C.Y.1    Lewis, R.V.2
  • 183
    • 0023953406 scopus 로고
    • Entropic elastic processes in protein mechanisms. I. Elastic structure due to an inverse temperature transition and elasticity due to internal chain dynamics
    • D.W. Urry Entropic elastic processes in protein mechanisms. I. Elastic structure due to an inverse temperature transition and elasticity due to internal chain dynamics J. Protein Chem. 7 1988 1 34
    • (1988) J. Protein Chem. , vol.7 , pp. 1-34
    • Urry, D.W.1
  • 184
    • 0038388786 scopus 로고    scopus 로고
    • Physical chemistry of biological free energy transduction as demonstrated by elastic protein-based polymers
    • D.W. Urry Physical chemistry of biological free energy transduction as demonstrated by elastic protein-based polymers J. Phys. Chem. B. 101 1997 11007 11028 (Pubitemid 127627954)
    • (1997) Journal of Physical Chemistry B , vol.101 , Issue.51 , pp. 11007-11028
    • Urry, D.W.1
  • 186
    • 22944435181 scopus 로고    scopus 로고
    • 13C CP/MAS NMR chemical shifts, two-dimensional off magic angle spinning spin-diffusion NMR, rotational echo double resonance, and statistical distribution of torsion angles from protein data bank
    • DOI 10.1021/ma050052e
    • 13C CP/MAS NMR chemical shifts, two-dimensional off magic angle spinning spin-diffusion NMR, rotational echo double resonance, and statistical distribution of torsion angles from Protein Data Bank Macromolecules 38 2005 6038 6047 (Pubitemid 41048618)
    • (2005) Macromolecules , vol.38 , Issue.14 , pp. 6038-6047
    • Ohgo, K.1    Ashida, J.2    Kumashiro, K.K.3    Asakura, T.4
  • 188
    • 0001761987 scopus 로고
    • The structure of the tripeptide l-alanyl-l-alanyl-l-alanine
    • J.K. Fawcett, N. Camerman, and A. Camerman The structure of the tripeptide l-alanyl-l-alanyl-l-alanine Acta Cryst. B31 1975 658 665
    • (1975) Acta Cryst. , vol.31 B , pp. 658-665
    • Fawcett, J.K.1    Camerman, N.2    Camerman, A.3
  • 190
    • 0014220140 scopus 로고
    • Structure of beta-poly-l-alanine: Refined atomic co-ordinates for an anti-parallel beta-pleated sheet
    • S. Arnott, S.D. Dover, and A. Elliott Structure of beta-poly-l-alanine: refined atomic co-ordinates for an anti-parallel beta-pleated sheet J. Mol. Biol. 30 1967 201 208
    • (1967) J. Mol. Biol. , vol.30 , pp. 201-208
    • Arnott, S.1    Dover, S.D.2    Elliott, A.3
  • 191
    • 79953858602 scopus 로고    scopus 로고
    • Silk fiber mechanics from multiscale force distribution analysis
    • M. Cetinkaya, S. Xiao, B. Markert, W. Stacklies, and F. Grater Silk fiber mechanics from multiscale force distribution analysis Biophys. J. 100 2011 1298 1305
    • (2011) Biophys. J. , vol.100 , pp. 1298-1305
    • Cetinkaya, M.1    Xiao, S.2    Markert, B.3    Stacklies, W.4    Grater, F.5
  • 192
    • 77949943700 scopus 로고    scopus 로고
    • Nanoconfinement controls stiffness, strength and mechanical toughness of beta-sheet crystals in silk
    • S. Keten, Z. Xu, B. Ihle, and M.J. Buehler Nanoconfinement controls stiffness, strength and mechanical toughness of beta-sheet crystals in silk Nat. Mater. 9 2010 359 367
    • (2010) Nat. Mater. , vol.9 , pp. 359-367
    • Keten, S.1    Xu, Z.2    Ihle, B.3    Buehler, M.J.4
  • 193
    • 0031172364 scopus 로고    scopus 로고
    • Non-periodic lattice crystals in the hierarchical microstructure of spider (major ampullate) silk
    • B.L. Thiel, K. Guess, and C. Viney Non-periodic lattice crystals in the hierarchical microstructure of spider (major ampullate) silk Biopolymers 41 1997 703 719
    • (1997) Biopolymers , vol.41 , pp. 703-719
    • Thiel, B.L.1    Guess, K.2    Viney, C.3
  • 194
    • 0033377495 scopus 로고    scopus 로고
    • The mechanical design of spider silks: From fibroin sequence to mechanical function
    • J.M. Gosline, P.A. Guerette, C.S. Ortlepp, and K.N. Savage The mechanical design of spider silks: from fibroin sequence to mechanical function J. Exp. Biol. 202 1999 3295 3303 (Pubitemid 30018435)
    • (1999) Journal of Experimental Biology , vol.202 , Issue.23 , pp. 3295-3303
    • Gosline, J.M.1    Guerette, P.A.2    Ortlepp, C.S.3    Savage, K.N.4
  • 196
    • 0030569727 scopus 로고    scopus 로고
    • Molecular orientation and two-component nature of the crystalline fraction of spider dragline silk
    • A.H. Simmons, C.A. Michal, and L.W. Jelinski Molecular orientation and two-component nature of the crystalline fraction of spider dragline silk Science 271 1996 84 87 (Pubitemid 26033282)
    • (1996) Science , vol.271 , Issue.5245 , pp. 84-87
    • Simmons, A.1    Michal, C.A.2    Jelinski, L.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.