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Volumn 170, Issue 2, 2010, Pages 413-419

The role of salt and shear on the storage and assembly of spider silk proteins

Author keywords

Protein assembly; Salt; Shear; Spider silk

Indexed keywords

NANOPARTICLE; PROTEIN; RECOMBINANT PROTEIN; SODIUM CHLORIDE; SPIDER SILK PROTEIN; UNCLASSIFIED DRUG;

EID: 77951974343     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2009.12.027     Document Type: Article
Times cited : (75)

References (65)
  • 1
    • 0028161607 scopus 로고
    • Design-features of the orb web of the spider, Araneus diadematus
    • Aprhisiart A., Vollrath F. Design-features of the orb web of the spider, Araneus diadematus. Behavioral Ecology 1994, 5:280-287.
    • (1994) Behavioral Ecology , vol.5 , pp. 280-287
    • Aprhisiart, A.1    Vollrath, F.2
  • 2
    • 0029792830 scopus 로고    scopus 로고
    • How Hofmeister ion interactions affect protein stability
    • Baldwin R.L. How Hofmeister ion interactions affect protein stability. Biophysical Journal 1996, 71:2056-2063.
    • (1996) Biophysical Journal , vol.71 , pp. 2056-2063
    • Baldwin, R.L.1
  • 3
    • 67649171018 scopus 로고    scopus 로고
    • Shear-induced deformation of bovine insulin in couette flow
    • Bekard I.B., Dunstan D.E. Shear-induced deformation of bovine insulin in couette flow. Journal of Physical Chemistry B 2009, 113:8453-8457.
    • (2009) Journal of Physical Chemistry B , vol.113 , pp. 8453-8457
    • Bekard, I.B.1    Dunstan, D.E.2
  • 4
    • 0345118157 scopus 로고    scopus 로고
    • Mapping domain structures in silks from insects and spiders related to protein assembly
    • Bini E., Knight D.P., Kaplan D.L. Mapping domain structures in silks from insects and spiders related to protein assembly. Journal of Molecular Biology 2004, 335:27-40.
    • (2004) Journal of Molecular Biology , vol.335 , pp. 27-40
    • Bini, E.1    Knight, D.P.2    Kaplan, D.L.3
  • 5
    • 54449096188 scopus 로고    scopus 로고
    • Attenuated total reflection infrared spectroscopy: an efficient technique to quantitatively determine the orientation and conformation of proteins in single silk fibers
    • Boulet-Audet M., Lefevre T., Buffeteau T., Pezolet M. Attenuated total reflection infrared spectroscopy: an efficient technique to quantitatively determine the orientation and conformation of proteins in single silk fibers. Applied Spectroscopy 2008, 62:956-962.
    • (2008) Applied Spectroscopy , vol.62 , pp. 956-962
    • Boulet-Audet, M.1    Lefevre, T.2    Buffeteau, T.3    Pezolet, M.4
  • 6
    • 0036908603 scopus 로고    scopus 로고
    • Ultrastructure of the major ampullate gland of the black widow spider, Latrodectus hesperus
    • Casem M.L., Tran L.P.P., Moore A.M.F. Ultrastructure of the major ampullate gland of the black widow spider, Latrodectus hesperus. Tissue & Cell 2002, 34:427-436.
    • (2002) Tissue & Cell , vol.34 , pp. 427-436
    • Casem, M.L.1    Tran, L.P.P.2    Moore, A.M.F.3
  • 10
    • 40449126548 scopus 로고    scopus 로고
    • Hydrophobic and Hofmeister effects on the adhesion of spider silk proteins onto solid substrates: an AFM-based single-molecule study
    • Geisler M., Pirzer T., Ackerschott C., Lud S., Garrido J., Scheibel T., Hugel T. Hydrophobic and Hofmeister effects on the adhesion of spider silk proteins onto solid substrates: an AFM-based single-molecule study. Langmuir 2008, 24:1350-1355.
    • (2008) Langmuir , vol.24 , pp. 1350-1355
    • Geisler, M.1    Pirzer, T.2    Ackerschott, C.3    Lud, S.4    Garrido, J.5    Scheibel, T.6    Hugel, T.7
  • 13
    • 0029925013 scopus 로고    scopus 로고
    • Silk properties determined by gland-specific expression of a spider fibroin gene family
    • Guerette P.A., Ginzinger D.G., Weber B.H.F., Gosline J.M. Silk properties determined by gland-specific expression of a spider fibroin gene family. Science 1996, 272:112-115.
    • (1996) Science , vol.272 , pp. 112-115
    • Guerette, P.A.1    Ginzinger, D.G.2    Weber, B.H.F.3    Gosline, J.M.4
  • 19
    • 50949110817 scopus 로고    scopus 로고
    • Polymeric materials based on silk proteins
    • Hardy J.G., Romer L.M., Scheibel T.R. Polymeric materials based on silk proteins. Polymer 2008, 49:4309-4327.
    • (2008) Polymer , vol.49 , pp. 4309-4327
    • Hardy, J.G.1    Romer, L.M.2    Scheibel, T.R.3
  • 20
    • 40849102539 scopus 로고    scopus 로고
    • Structural properties of recombinant nonrepetitive and repetitive parts of major ampullate spidroin 1 from Euprosthenops australis: implications for fiber formation
    • Hedhammar M., Rising A., Grip S., Martinez A.S., Nordling K., Casals C., Stark M., Johansson J. Structural properties of recombinant nonrepetitive and repetitive parts of major ampullate spidroin 1 from Euprosthenops australis: implications for fiber formation. Biochemistry 2008, 47:3407-3417.
    • (2008) Biochemistry , vol.47 , pp. 3407-3417
    • Hedhammar, M.1    Rising, A.2    Grip, S.3    Martinez, A.S.4    Nordling, K.5    Casals, C.6    Stark, M.7    Johansson, J.8
  • 25
    • 33746562390 scopus 로고    scopus 로고
    • Characterization and expression of a cDNA encoding a tubuliform silk protein of the golden web spider Nephila antipodiana
    • Huang W., Lin Z., Sin Y.M., Li D., Gong Z., Yang D. Characterization and expression of a cDNA encoding a tubuliform silk protein of the golden web spider Nephila antipodiana. Biochimie 2006, 88:849-858.
    • (2006) Biochimie , vol.88 , pp. 849-858
    • Huang, W.1    Lin, Z.2    Sin, Y.M.3    Li, D.4    Gong, Z.5    Yang, D.6
  • 27
    • 6344228390 scopus 로고    scopus 로고
    • Primary structure elements of spider dragline silks and their contribution to protein solubility
    • Huemmerich D., Helsen C.W., Quedzuweit S., Oschmann J., Rudolph R., Scheibel T. Primary structure elements of spider dragline silks and their contribution to protein solubility. Biochemistry 2004, 43:13604-13612.
    • (2004) Biochemistry , vol.43 , pp. 13604-13612
    • Huemmerich, D.1    Helsen, C.W.2    Quedzuweit, S.3    Oschmann, J.4    Rudolph, R.5    Scheibel, T.6
  • 28
    • 34948902334 scopus 로고    scopus 로고
    • A model for the structure of the C-terminal domain of dragline spider silk and the role of its conserved cysteine
    • Ittah S., Michaeli A., Goldblum A., Gat U. A model for the structure of the C-terminal domain of dragline spider silk and the role of its conserved cysteine. Biomacromolecules 2007, 8:2768-2773.
    • (2007) Biomacromolecules , vol.8 , pp. 2768-2773
    • Ittah, S.1    Michaeli, A.2    Goldblum, A.3    Gat, U.4
  • 29
    • 33745633089 scopus 로고    scopus 로고
    • An essential role for the C-terminal domain of a dragline spider silk protein in directing fiber formation
    • Ittah S., Cohen S., Garty S., Cohn D., Gat U. An essential role for the C-terminal domain of a dragline spider silk protein in directing fiber formation. Biomacromolecules 2006, 7:1790-1795.
    • (2006) Biomacromolecules , vol.7 , pp. 1790-1795
    • Ittah, S.1    Cohen, S.2    Garty, S.3    Cohn, D.4    Gat, U.5
  • 30
    • 0042364941 scopus 로고    scopus 로고
    • Mechanism of silk processing in insects and spiders
    • Jin H.J., Kaplan D.L. Mechanism of silk processing in insects and spiders. Nature 2003, 424:1057-1061.
    • (2003) Nature , vol.424 , pp. 1057-1061
    • Jin, H.J.1    Kaplan, D.L.2
  • 31
    • 0035903262 scopus 로고    scopus 로고
    • Elucidating changes in interfacial water structure upon protein adsorption
    • Kim J., Cremer P.S. Elucidating changes in interfacial water structure upon protein adsorption. ChemPhysChem 2001, 2:543-546.
    • (2001) ChemPhysChem , vol.2 , pp. 543-546
    • Kim, J.1    Cremer, P.S.2
  • 32
    • 0034978997 scopus 로고    scopus 로고
    • Changes in element composition along the spinning duct in a Nephila spider
    • Knight D.P., Vollrath F. Changes in element composition along the spinning duct in a Nephila spider. Naturwissenschaften 2001, 88:179-182.
    • (2001) Naturwissenschaften , vol.88 , pp. 179-182
    • Knight, D.P.1    Vollrath, F.2
  • 34
  • 35
    • 34147152672 scopus 로고    scopus 로고
    • Protein secondary structure and orientation in silk as revealed by Raman spectromicroscopy
    • Lefevre T., Rousseau M.E., Pezolet M. Protein secondary structure and orientation in silk as revealed by Raman spectromicroscopy. Biophysical Journal 2007, 92:2885-2895.
    • (2007) Biophysical Journal , vol.92 , pp. 2885-2895
    • Lefevre, T.1    Rousseau, M.E.2    Pezolet, M.3
  • 36
    • 52649170349 scopus 로고    scopus 로고
    • Conformational and orientational transformation of silk proteins in the major ampullate gland of Nephila clavipes spiders
    • Lefevre T., Boudreault S., Cloutier C., Pezolet M. Conformational and orientational transformation of silk proteins in the major ampullate gland of Nephila clavipes spiders. Biomacromolecules 2008, 9:2399-2407.
    • (2008) Biomacromolecules , vol.9 , pp. 2399-2407
    • Lefevre, T.1    Boudreault, S.2    Cloutier, C.3    Pezolet, M.4
  • 40
    • 33749832915 scopus 로고    scopus 로고
    • Spider silk: ancient ideas for new biomaterials
    • Lewis R.V. Spider silk: ancient ideas for new biomaterials. Chemical Reviews 2006, 106:3762-3774.
    • (2006) Chemical Reviews , vol.106 , pp. 3762-3774
    • Lewis, R.V.1
  • 41
    • 0028797409 scopus 로고
    • Structural-engineering of an orb-spiders web
    • Lin L.H., Edmonds D.T., Vollrath F. Structural-engineering of an orb-spiders web. Nature 1995, 373:146-148.
    • (1995) Nature , vol.373 , pp. 146-148
    • Lin, L.H.1    Edmonds, D.T.2    Vollrath, F.3
  • 43
    • 28844433042 scopus 로고    scopus 로고
    • Analysis of the conserved N-terminal domains in major ampullate spider silk proteins
    • Motriuk-Smith D., Smith A., Hayashi C.Y., Lewis R.V. Analysis of the conserved N-terminal domains in major ampullate spider silk proteins. Biomacromolecules 2005, 6:3152-3159.
    • (2005) Biomacromolecules , vol.6 , pp. 3152-3159
    • Motriuk-Smith, D.1    Smith, A.2    Hayashi, C.Y.3    Lewis, R.V.4
  • 44
  • 48
    • 68349139437 scopus 로고    scopus 로고
    • Single molecule force measurements delineate salt, pH and surface effects on biopolymer adhesion
    • Pirzer T., Geisler M., Scheibel T., Hugel T. Single molecule force measurements delineate salt, pH and surface effects on biopolymer adhesion. Physical Biology 2009, 6. 10.1088/1478-3975/6/2/025004.
    • (2009) Physical Biology , vol.6
    • Pirzer, T.1    Geisler, M.2    Scheibel, T.3    Hugel, T.4
  • 50
    • 33846008063 scopus 로고    scopus 로고
    • N-terminal nonrepetitive domain common to dragline, flagelliform, and cylindriform spider silk proteins
    • Rising A., Hjalm G., Engstrom W., Johansson J. N-terminal nonrepetitive domain common to dragline, flagelliform, and cylindriform spider silk proteins. Biomacromolecules 2006, 7:3120-3124.
    • (2006) Biomacromolecules , vol.7 , pp. 3120-3124
    • Rising, A.1    Hjalm, G.2    Engstrom, W.3    Johansson, J.4
  • 52
    • 70350059595 scopus 로고    scopus 로고
    • Conformation and orientation of proteins in various types of silk fibers produced by Nephila clavipes spiders
    • Rousseau M.E., Lefevre T., Pezolet M. Conformation and orientation of proteins in various types of silk fibers produced by Nephila clavipes spiders. Biomacromolecules 2009, 10:2945-2953.
    • (2009) Biomacromolecules , vol.10 , pp. 2945-2953
    • Rousseau, M.E.1    Lefevre, T.2    Pezolet, M.3
  • 53
    • 9744223571 scopus 로고    scopus 로고
    • Study of protein conformation and orientation in silkworm and spider silk fibers using Raman microspectroscopy
    • Rousseau M.E., Lefevre T., Beaulieu L., Asakura T., Pezolet M. Study of protein conformation and orientation in silkworm and spider silk fibers using Raman microspectroscopy. Biomacromolecules 2004, 5:2247-2257.
    • (2004) Biomacromolecules , vol.5 , pp. 2247-2257
    • Rousseau, M.E.1    Lefevre, T.2    Beaulieu, L.3    Asakura, T.4    Pezolet, M.5
  • 54
    • 50949092503 scopus 로고    scopus 로고
    • Folding, self-assembly and conformational switches of proteins
    • Nova Publishers, New York, J.P. Zbilut, T. Scheibel (Eds.)
    • SenGupta S., Scheibel T. Folding, self-assembly and conformational switches of proteins. Protein Folding-Misfolding: Some Current Concepts of Protein Chemistry 2007, Nova Publishers, New York, pp. 1-34. J.P. Zbilut, T. Scheibel (Eds.).
    • (2007) Protein Folding-Misfolding: Some Current Concepts of Protein Chemistry , pp. 1-34
    • SenGupta, S.1    Scheibel, T.2
  • 56
    • 0001113739 scopus 로고
    • Water extraction by the major ampullate duct during silk formation in the spider, Argiope aurantia Lucas
    • Tillinghast E.K., Chase S.F., Townley M.A. Water extraction by the major ampullate duct during silk formation in the spider, Argiope aurantia Lucas. Journal of Insect Physiology 1984, 30:591-596.
    • (1984) Journal of Insect Physiology , vol.30 , pp. 591-596
    • Tillinghast, E.K.1    Chase, S.F.2    Townley, M.A.3
  • 57
    • 70349504671 scopus 로고    scopus 로고
    • Interfacial rheological properties of recombinant spider-silk proteins
    • Vezy C., Hermanson K.D., Scheibel T., Bausch A.R. Interfacial rheological properties of recombinant spider-silk proteins. Biointerphases 2009, 4:43-46.
    • (2009) Biointerphases , vol.4 , pp. 43-46
    • Vezy, C.1    Hermanson, K.D.2    Scheibel, T.3    Bausch, A.R.4
  • 58
    • 0032935646 scopus 로고    scopus 로고
    • Structure and function of the silk production pathway in the spider Nephila edulis
    • Vollrath F., Knight D.P. Structure and function of the silk production pathway in the spider Nephila edulis. International Journal of Biological Macromolecules 1999, 24:243-249.
    • (1999) International Journal of Biological Macromolecules , vol.24 , pp. 243-249
    • Vollrath, F.1    Knight, D.P.2
  • 59
    • 0035967162 scopus 로고    scopus 로고
    • Liquid crystalline spinning of spider silk
    • Vollrath F., Knight D.P. Liquid crystalline spinning of spider silk. Nature 2001, 410:541-548.
    • (2001) Nature , vol.410 , pp. 541-548
    • Vollrath, F.1    Knight, D.P.2
  • 60
    • 84963388465 scopus 로고
    • Mechanical denaturation of high polymers in solutions. 36. Flow-induced crystallization of bombyx-mori l silk fibroin from the aqueous-solution under a steady-state flow
    • Yamaura K., Okumura Y., Matsuzawa S. Mechanical denaturation of high polymers in solutions. 36. Flow-induced crystallization of bombyx-mori l silk fibroin from the aqueous-solution under a steady-state flow. Journal of Macromolecular Science-Physics 1982, B21:49-69.
    • (1982) Journal of Macromolecular Science-Physics , vol.21 B , pp. 49-69
    • Yamaura, K.1    Okumura, Y.2    Matsuzawa, S.3
  • 61
    • 0021851161 scopus 로고
    • Flow-induced crystallization of bombyx-mori l silk fibroin from regenerated aqueous-solution and spinnability of its solution
    • Yamaura K., Okumura Y., Ozaki A., Matsuzawa S. Flow-induced crystallization of bombyx-mori l silk fibroin from regenerated aqueous-solution and spinnability of its solution. Applied Polymer Symposia 1985, 205:220.
    • (1985) Applied Polymer Symposia , vol.205 , pp. 220
    • Yamaura, K.1    Okumura, Y.2    Ozaki, A.3    Matsuzawa, S.4
  • 64
    • 33751408436 scopus 로고    scopus 로고
    • Interactions between macromolecules and ions: the Hofmeister series
    • Zhang Y.J., Cremer P.S. Interactions between macromolecules and ions: the Hofmeister series. Current Opinion in Chemical Biology 2006, 10:658-663.
    • (2006) Current Opinion in Chemical Biology , vol.10 , pp. 658-663
    • Zhang, Y.J.1    Cremer, P.S.2
  • 65
    • 26844452263 scopus 로고    scopus 로고
    • Specific ion effects on the water solubility of macromolecules: PNIPAM and the Hofmeister series
    • Zhang Y.J., Furyk S., Bergbreiter D.E., Cremer P.S. Specific ion effects on the water solubility of macromolecules: PNIPAM and the Hofmeister series. Journal of the American Chemical Society 2005, 127:14505-14510.
    • (2005) Journal of the American Chemical Society , vol.127 , pp. 14505-14510
    • Zhang, Y.J.1    Furyk, S.2    Bergbreiter, D.E.3    Cremer, P.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.