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Volumn 41, Issue 50, 2002, Pages 14944-14950

Conformation transition in silk protein films monitored by time-resolved fourier transform infrared spectroscopy: Effect of potassium ions on Nephila spidroin films

Author keywords

[No Author keywords available]

Indexed keywords

ABSORPTION; CONFORMATIONS; FOURIER TRANSFORM INFRARED SPECTROSCOPY; HYDROGEN BONDS; MACROMOLECULES; POTASSIUM; PROTEINS;

EID: 2242434437     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi026550m     Document Type: Article
Times cited : (102)

References (46)
  • 2
    • 0035967162 scopus 로고    scopus 로고
    • Liquid crystalline spinning of spider silk
    • Vollrath, F., and Knight, D. P. (2001) Liquid crystalline spinning of spider silk, Nature 410, 541-548.
    • (2001) Nature , vol.410 , pp. 541-548
    • Vollrath, F.1    Knight, D.P.2
  • 3
    • 0031082016 scopus 로고    scopus 로고
    • Natural silks: Archetypal supramolecular assembly of polymer fibres
    • Viney, C. (1997) Natural silks: Archetypal supramolecular assembly of polymer fibres, Supramol. Sci. 4, 75-81.
    • (1997) Supramol. Sci. , vol.4 , pp. 75-81
    • Viney, C.1
  • 4
    • 0033531474 scopus 로고    scopus 로고
    • Liquid crystals and flow elongation in a spider's silk production line
    • Knight, D. P., and Vollrath, F. (1999) Liquid crystals and flow elongation in a spider's silk production line, Proc. R. Soc. London, Ser. B 266, 519-523.
    • (1999) Proc. R. Soc. London, Ser. B , vol.266 , pp. 519-523
    • Knight, D.P.1    Vollrath, F.2
  • 5
    • 0000035952 scopus 로고
    • Liquid crystallinity of natural silk secretions
    • Kerkam, K., Viney, C., Kaplan, D., and Lombardi, S. (1991) Liquid crystallinity of natural silk secretions, Nature 349, 596-598.
    • (1991) Nature , vol.349 , pp. 596-598
    • Kerkam, K.1    Viney, C.2    Kaplan, D.3    Lombardi, S.4
  • 6
    • 0030196210 scopus 로고    scopus 로고
    • Evidence of a cholesteric liquid crystalline phase in natural silk spinning processes
    • Willcox, P. J., Gido. S. P., Muller, W., and Kaplan, D. L. (1996) Evidence of a cholesteric liquid crystalline phase in natural silk spinning processes, Macromolecules 29, 5106-5110.
    • (1996) Macromolecules , vol.29 , pp. 5106-5110
    • Willcox, P.J.1    Gido, S.P.2    Muller, W.3    Kaplan, D.L.4
  • 7
    • 0034643851 scopus 로고    scopus 로고
    • Beta transition and stress-induced phase separation in the spinning of spider dragline silk
    • Knight, D. P., Knight, M. M., and Vollrath, F. (2000) Beta transition and stress-induced phase separation in the spinning of spider dragline silk, Int. J. Biol. Macromol. 27, 205-210.
    • (2000) Int. J. Biol. Macromol. , vol.27 , pp. 205-210
    • Knight, D.P.1    Knight, M.M.2    Vollrath, F.3
  • 9
    • 0030574944 scopus 로고    scopus 로고
    • Local structure in spider dragline silk investigated by two- dimensional spin-diffusion nuclear magnetic resonance
    • Kummerlen, J., vanBeek, J. D., Vollrath, F., Meier, B. H. (1996) Local structure in spider dragline silk investigated by two- dimensional spin-diffusion nuclear magnetic resonance, Macro- molecules 29, 2920-2928.
    • (1996) Macro-molecules , vol.29 , pp. 2920-2928
    • Kummerlen, J.1    VanBeek, J.D.2    Vollrath, F.3    Meier, B.H.4
  • 11
    • 0025648652 scopus 로고
    • 2O) solutions. 2. Amide absorption-bands of polypeptides and fibrous proteins in alpha-coil, beta-coil, and random coil conformations
    • 2O) solutions. 2. Amide absorption-bands of polypeptides and fibrous proteins in alpha-coil, beta-coil, and random coil conformations, Biopolymers 30, 1259-1271.
    • (1990) Biopolymers , vol.30 , pp. 1259-1271
    • Venyaminov, S.Y.1    Kalnin, N.N.2
  • 12
    • 0035660088 scopus 로고    scopus 로고
    • The natural silk spinning process - A nucleation-dependent aggregation mechanism
    • Li, G. Y., Zhou, P., Shao, Z. Z., Xie, X., Chen, X., Wang, H. H., Chunyu, L. J., and Yu, T. Y. (2001) The natural silk spinning process - A nucleation-dependent aggregation mechanism, Eur. J. Biochem. 268, 6600-6606.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 6600-6606
    • Li, G.Y.1    Zhou, P.2    Shao, Z.Z.3    Xie, X.4    Chen, X.5    Wang, H.H.6    Chunyu, L.J.7    Yu, T.Y.8
  • 13
    • 0034890493 scopus 로고    scopus 로고
    • Comparison of the spinning of Selachian egg case ply sheets and orb web spider dragline filaments
    • Knight, D. P., and Vollrath, F. (2001) Comparison of the spinning of Selachian egg case ply sheets and orb web spider dragline filaments, Biomacromolecules 2, 323-334.
    • (2001) Biomacromolecules , vol.2 , pp. 323-334
    • Knight, D.P.1    Vollrath, F.2
  • 14
    • 0035970494 scopus 로고    scopus 로고
    • Multiaxial anisotropy of spider (Araneus diadematus) cocoon silk fibres
    • Barghout, J. Y. J., Czernuszka, J. T., and Viney, C. (2001) Multiaxial anisotropy of spider (Araneus diadematus) cocoon silk fibres, Polymer 42, 5797-5800.
    • (2001) Polymer , vol.42 , pp. 5797-5800
    • Barghout, J.Y.J.1    Czernuszka, J.T.2    Viney, C.3
  • 15
    • 0034978997 scopus 로고    scopus 로고
    • Changes in element composition along the spinning duct in a Nephila spider
    • Knight, D. P., and Vollrath, F. (2001) Changes in element composition along the spinning duct in a Nephila spider, Naturwissenschaften 88, 179-182.
    • (2001) Naturwissenschaften , vol.88 , pp. 179-182
    • Knight, D.P.1    Vollrath, F.2
  • 16
    • 0036059262 scopus 로고    scopus 로고
    • Rheological characterization of Nephila spidroin solution
    • Chen, X., Knight, D. P., and Vollrath, F. (2002) Rheological characterization of Nephila spidroin solution, Biomacromolecules 3, 644-648.
    • (2002) Biomacromolecules , vol.3 , pp. 644-648
    • Chen, X.1    Knight, D.P.2    Vollrath, F.3
  • 17
    • 0012037069 scopus 로고
    • Infrared spectra and structure of the proteins of the silk glands
    • Lenormant, H. (1955) Infrared spectra and structure of the proteins of the silk glands, Trans. Faraday Soc. 52, 549-553.
    • (1955) Trans. Faraday Soc. , vol.52 , pp. 549-553
    • Lenormant, H.1
  • 18
    • 0033136870 scopus 로고    scopus 로고
    • Analysis of spider silk in native and supercontracted states using Raman spectroscopy
    • Shao, Z., Vollrath, F., Sirichaisit, J., and Young, R. J. (1999) Analysis of spider silk in native and supercontracted states using Raman spectroscopy, Polymer 40, 2493-2500.
    • (1999) Polymer , vol.40 , pp. 2493-2500
    • Shao, Z.1    Vollrath, F.2    Sirichaisit, J.3    Young, R.J.4
  • 19
    • 0032913539 scopus 로고    scopus 로고
    • The effect of solvents on spider silk studied by mechanical testing and single-fibre Raman spectroscopy
    • Shao. Z. Z., Young, R. J., and Vollrath, F. (1999) The effect of solvents on spider silk studied by mechanical testing and single-fibre Raman spectroscopy, Int. J. Biol. Macromol. 24, 295-300.
    • (1999) Int. J. Biol. Macromol. , vol.24 , pp. 295-300
    • Shao, Z.Z.1    Young, R.J.2    Vollrath, F.3
  • 20
    • 0031259192 scopus 로고    scopus 로고
    • Conformation transition of silk fibroin induced by blending chitosan
    • Chen, X., Li, W. J., and Yu, T. Y. (1997) Conformation transition of silk fibroin induced by blending chitosan, J. Polym. Sci., Part B: Polym. Phys. 35, 2293-2296.
    • (1997) J. Polym. Sci., Part B: Polym. Phys. , vol.35 , pp. 2293-2296
    • Chen, X.1    Li, W.J.2    Yu, T.Y.3
  • 21
    • 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. Z., Marinkovic, N. S., Miller, L. M., Zhou, P., and Chance, M. R. (2001) Conformation transition kinetics of regenerated Bombyx mori silk fibroin membrane monitored by time-resolved FTIR spectroscopy, Biophys. Chem. 89, 25-34.
    • (2001) Biophys. Chem. , vol.89 , pp. 25-34
    • Chen, X.1    Shao, Z.Z.2    Marinkovic, N.S.3    Miller, L.M.4    Zhou, P.5    Chance, M.R.6
  • 22
    • 0029731419 scopus 로고    scopus 로고
    • Refolding of thermally and urea-denatured ribonuclease a monitored by time-resolved FTIR spectroscopy
    • Reinstadler, D., Fabian, H., Backmann, J., and Naumann, D. (1996) Refolding of thermally and urea-denatured ribonuclease a monitored by time-resolved FTIR spectroscopy, Biochemistry 35, 15822-15830.
    • (1996) Biochemistry , vol.35 , pp. 15822-15830
    • Reinstadler, D.1    Fabian, H.2    Backmann, J.3    Naumann, D.4
  • 24
    • 0030817794 scopus 로고    scopus 로고
    • Fast events in protein folding: Relaxation dynamics and structure of the 1 form of apomyoglobin
    • Gilmanshin, R., Williams, S., Callender, R. H., Woodruff, W. H., and Dyer, R. B. (1997) Fast events in protein folding: Relaxation dynamics and structure of the 1 form of apomyoglobin, Biochemistry 36, 15006-15012.
    • (1997) Biochemistry , vol.36 , pp. 15006-15012
    • Gilmanshin, R.1    Williams, S.2    Callender, R.H.3    Woodruff, W.H.4    Dyer, R.B.5
  • 25
    • 0001957057 scopus 로고
    • Composition of the hemolymph of the tarantula eurypelma-californicum
    • Schartau, W., and Leidescher, T. (1983) Composition of the hemolymph of the tarantula eurypelma-californicum, J. Comput. Physiol. 152, 73-77.
    • (1983) J. Comput. Physiol , vol.152 , pp. 73-77
    • Schartau, W.1    Leidescher, T.2
  • 26
    • 0018442937 scopus 로고
    • Physical properties and structure of silk. VI. Conformational changes in silk fibroin induced by immersion in water at 2 and 130 °C
    • Magoshi, J., Mizuide, M., Magoshi, Y., Takahashi, K., Kubo, M., and Nakamura, S. (1979) Physical properties and structure of silk. VI. Conformational changes in silk fibroin induced by immersion in water at 2 and 130 °C, J. Polym. Sci., Polym. Phys. Ed. 17, 515-520.
    • (1979) J. Polym. Sci., Polym. Phys. Ed. , vol.17 , pp. 515-520
    • Magoshi, J.1    Mizuide, M.2    Magoshi, Y.3    Takahashi, K.4    Kubo, M.5    Nakamura, S.6
  • 27
    • 0000951118 scopus 로고
    • Conformation characterization of Bombyx-mori silk fibroin in the solid-state by high-frequency C-13 cross polarization magic angle spinning NMR, X-ray-diffraction, and infrared-spectroscopy
    • Asakura, T., Kuzuhara, A., Tabeta, R., and Saito, H. (1985) Conformation characterization of Bombyx-mori silk fibroin in the solid-state by high-frequency C-13 cross polarization magic angle spinning NMR, X-ray-diffraction, and infrared-spectroscopy, Macromolecules 18, 1841-1845.
    • (1985) Macromolecules , vol.18 , pp. 1841-1845
    • Asakura, T.1    Kuzuhara, A.2    Tabeta, R.3    Saito, H.4
  • 28
    • 0041539677 scopus 로고
    • Silk fibroin/cellulose blend films-preparation, structure, and physical-properties
    • Freddi, G., Romano, M., Massafra, M. R., and Tsukada, M. (1995) Silk fibroin/cellulose blend films-preparation, structure, and physical-properties, J. Appl. Polym. Sci. 56, 1537-1545.
    • (1995) J. Appl. Polym. Sci. , vol.56 , pp. 1537-1545
    • Freddi, G.1    Romano, M.2    Massafra, M.R.3    Tsukada, M.4
  • 29
    • 0022691315 scopus 로고
    • Examination of the secondary structure of protein by deconvolved FTIR spectra
    • Byler, D. M., and Susi, H. (1986) Examination of the secondary structure of protein by deconvolved FTIR spectra, Biopolymers 25, 469-487.
    • (1986) Biopolymers , vol.25 , pp. 469-487
    • Byler, D.M.1    Susi, H.2
  • 30
    • 0023837785 scopus 로고
    • New insight into protein secondary structure from resolution-enhanced infrared-spectra
    • Surewicz, W. K., and Mantsch, H. H. (1988) New insight into protein secondary structure from resolution-enhanced infrared-spectra, Biochim. Biophys. Acta 952, 115-130.
    • (1988) Biochim. Biophys. Acta , vol.952 , pp. 115-130
    • Surewicz, W.K.1    Mantsch, H.H.2
  • 31
    • 0025357111 scopus 로고
    • Protein secondary structures in water from 2nd-derivative amide-1 infrared-spectra
    • Dong, A., Huang. P., and Caughey, W. S. (1990) Protein secondary structures in water from 2nd-derivative amide-1 infrared-spectra, Biochemistry 29, 3303-3308.
    • (1990) Biochemistry , vol.29 , pp. 3303-3308
    • Dong, A.1    Huang, P.2    Caughey, W.S.3
  • 32
    • 0035063476 scopus 로고    scopus 로고
    • New Fourier transform infrared based computational method for peptide secondary structure determination. 1. Description of method
    • Simonetti, M., and Di Bello, C. (2001) New Fourier transform infrared based computational method for peptide secondary structure determination. 1. Description of method, Biopolymers 62, 95-108.
    • (2001) Biopolymers , vol.62 , pp. 95-108
    • Simonetti, M.1    Di Bello, C.2
  • 33
    • 0025701223 scopus 로고
    • The structure of Bombyxmori silk fibroin membrane swollen by water studied with ESR, C-13-NMR, and FT-IR spectroscopies
    • Yoshimizu, H., and Asakura, T. (1990) The structure of Bombyxmori silk fibroin membrane swollen by water studied with ESR, C-13-NMR, and FT-IR spectroscopies, J. Appl. Polym. Sci. 40, 1745-1756.
    • (1990) J. Appl. Polym. Sci. , vol.40 , pp. 1745-1756
    • Yoshimizu, H.1    Asakura, T.2
  • 34
    • 0001102860 scopus 로고
    • Quantitative structural-analysis and physical-properties of silk fibroin hydrogels
    • Ayub, Z. H., Arai, M., and Hirabayashi, K. (1994) Quantitative structural-analysis and physical-properties of silk fibroin hydrogels, Polymer 35, 2197-2200.
    • (1994) Polymer , vol.35 , pp. 2197-2200
    • Ayub, Z.H.1    Arai, M.2    Hirabayashi, K.3
  • 35
    • 0031119134 scopus 로고    scopus 로고
    • Structure and molecular conformation of tussah silk fibroin films: Effect of heat treatment
    • Freddi, G., Monti. P., Nagura, M., Gotoh, Y., and Tsukada, M. (1997) Structure and molecular conformation of tussah silk fibroin films: Effect of heat treatment, J. Polym. Sci., Part B: Polym. Phys. 35, 841-847.
    • (1997) J. Polym. Sci., Part B: Polym. Phys. , vol.35 , pp. 841-847
    • Freddi, G.1    Monti, P.2    Nagura, M.3    Gotoh, Y.4    Tsukada, M.5
  • 36
    • 0034076545 scopus 로고    scopus 로고
    • Do parallel beta-helix proteins have a unique Fourier transform infrared spectrum
    • Khurana, R., and Fink, A. L. (2000) Do parallel beta-helix proteins have a unique Fourier transform infrared spectrum. Biophys. J. 78, 994-1000.
    • (2000) Biophys. J. , vol.78 , pp. 994-1000
    • Khurana, R.1    Fink, A.L.2
  • 37
    • 0035856681 scopus 로고    scopus 로고
    • Influence of casting temperature on the near-surface structure and wettability of cast silk fibroin films
    • Tretinnikov, O. N., and Tamada, Y. (2001) Influence of casting temperature on the near-surface structure and wettability of cast silk fibroin films, Langmuir 17, 7406-7413.
    • (2001) Langmuir , vol.17 , pp. 7406-7413
    • Tretinnikov, O.N.1    Tamada, Y.2
  • 38
    • 0032166681 scopus 로고    scopus 로고
    • Artificial spinning of spider silk
    • Seidel, A., Liivak, O., and Jelinski, L. W. (1998) Artificial spinning of spider silk, Macromolecules 31, 6733-6736.
    • (1998) Macromolecules , vol.31 , pp. 6733-6736
    • Seidel, A.1    Liivak, O.2    Jelinski, L.W.3
  • 39
    • 0035895432 scopus 로고    scopus 로고
    • A repeated beta-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
    • Asakura, T., Ashida, J., Yamane, T., Kameda, T., Nakazawa, Y., Ohgo, K., and Komatsu, K. (2001) A repeated beta-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, 291-305.
    • (2001) J. Mol. Biol. , vol.306 , pp. 291-305
    • Asakura, T.1    Ashida, J.2    Yamane, T.3    Kameda, T.4    Nakazawa, Y.5    Ohgo, K.6    Komatsu, K.7
  • 40
    • 0002158739 scopus 로고
    • Silk-biology, structure, properties, and genetics
    • Kaplan, D., Adams, W. W., Farmer, B., and Viney, C. (1994) Silk-biology, structure, properties, and genetics, ACS Symp. Ser. 544, 2-16.
    • (1994) ACS Symp. Ser. , vol.544 , pp. 2-16
    • Kaplan, D.1    Adams, W.W.2    Farmer, B.3    Viney, C.4
  • 41
    • 0000826425 scopus 로고
    • Mechanism of fiber formation of silkworm
    • Magoshi, J., Magoshi, Y., and Nakamura S. (1994) Mechanism of fiber formation of silkworm, ACS Symp. Ser. 544, 292-310.
    • (1994) ACS Symp. Ser. , vol.544 , pp. 292-310
    • Magoshi, J.1    Magoshi, Y.2    Nakamura, S.3
  • 42
    • 0031269978 scopus 로고    scopus 로고
    • Conformation of the polyalanine repeats in minor ampullate gland silk of spider Nephila clavipes
    • Liivak, O., Flores, A., Lewis, R., and Jelinski, L. W. (1997) Conformation of the polyalanine repeats in minor ampullate gland silk of spider Nephila clavipes, Macromolecules 30, 7127-7130.
    • (1997) Macromolecules , vol.30 , pp. 7127-7130
    • Liivak, O.1    Flores, A.2    Lewis, R.3    Jelinski, L.W.4
  • 43
    • 0000471787 scopus 로고    scopus 로고
    • Studies on chitosan-fibroin blend membranes (1)-Structure of the blend membrane and the improvement of the water adsorption and the mechanical property of fibroin
    • Chen, X., Li, W. J., Zhong, W., Lu, Y. H., and Yu, T. Y. (1998) Studies on chitosan-fibroin blend membranes (1)-Structure of the blend membrane and the improvement of the water adsorption and the mechanical property of fibroin, Chem. J. Chin. Univ. 19, 300-304.
    • (1998) Chem. J. Chin. Univ. , vol.19 , pp. 300-304
    • Chen, X.1    Li, W.J.2    Zhong, W.3    Lu, Y.H.4    Yu, T.Y.5
  • 44
    • 0024303806 scopus 로고
    • Fourier transform Raman studies of secondary structure in synthetic polypeptides
    • Delvin, A., Ober, C. K., and Bluhm, T. L. (1989) Fourier transform Raman studies of secondary structure in synthetic polypeptides, Macromolecules 22, 500-502.
    • (1989) Macromolecules , vol.22 , pp. 500-502
    • Delvin, A.1    Ober, C.K.2    Bluhm, T.L.3
  • 45
    • 0000188841 scopus 로고
    • Dynamics of conformational transitions in polymers
    • Helfand, E. (1984) Dynamics of conformational transitions in polymers, Science 226, 647-650.
    • (1984) Science , vol.226 , pp. 647-650
    • Helfand, E.1


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