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Volumn 47, Issue 12, 1999, Pages 5093-5099

Identification of microphases in mixed α- and ω-gliadin protein films investigated by atomic force microscopy

Author keywords

AFM; Atomic force microscopy; Gliadin; Phase angle; Protein film

Indexed keywords

GLIADIN;

EID: 0033394598     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf9904057     Document Type: Article
Times cited : (24)

References (27)
  • 1
    • 0001109566 scopus 로고
    • Immunocytochemical localisation of the wheat storage protein triticin in developing endosperm tissue
    • Bechtel, D. B.; Wilson, J. D.; Shewry, P. R. Immunocytochemical localisation of the wheat storage protein triticin in developing endosperm tissue. Cereal Chem. 1991, 68, 573-577.
    • (1991) Cereal Chem. , vol.68 , pp. 573-577
    • Bechtel, D.B.1    Wilson, J.D.2    Shewry, P.R.3
  • 2
    • 0032532286 scopus 로고    scopus 로고
    • TM-AFM threshold analysis of macromolecular orientation: A study of the orientation of IgG and IgE on mica surfaces
    • Bergkvist, M.; Carlsson, J.; Karlsson, T.; Oscarsson, S. TM-AFM threshold analysis of macromolecular orientation: A study of the orientation of IgG and IgE on mica surfaces. J. Colloid Interface Sci. 1998, 206, 475-481.
    • (1998) J. Colloid Interface Sci. , vol.206 , pp. 475-481
    • Bergkvist, M.1    Carlsson, J.2    Karlsson, T.3    Oscarsson, S.4
  • 3
    • 0021176063 scopus 로고
    • The conformational structure of A-gliadin. Intrinsic viscosities under conditions approaching the native state and under denaturing conditions
    • Cole, E. W.; Kasarda, D. D.; Lafiandra, D. The conformational structure of A-gliadin. Intrinsic viscosities under conditions approaching the native state and under denaturing conditions. Biochim. Biophys. Acta 1984, 787, 244-251.
    • (1984) Biochim. Biophys. Acta , vol.787 , pp. 244-251
    • Cole, E.W.1    Kasarda, D.D.2    Lafiandra, D.3
  • 5
    • 17644429283 scopus 로고    scopus 로고
    • Imaging two-dimensional arrays of soluble proteins by atomic force microscopy in contact mode using sharp supertip
    • Furuno, T.; Sasabe, H.; Ikegami, A. Imaging two-dimensional arrays of soluble proteins by atomic force microscopy in contact mode using sharp supertip. Ultramicroscopy 1998, 70, 125-131.
    • (1998) Ultramicroscopy , vol.70 , pp. 125-131
    • Furuno, T.1    Sasabe, H.2    Ikegami, A.3
  • 9
    • 0030859366 scopus 로고    scopus 로고
    • Three-dimensional structure of human fibrinogen under aqueous conditions visualized by atomic force microscopy
    • Marchant, R. E.; Barb, M. D.; Shainoff, J. R.; Eppell, S. J.; Wilson, D. L.; Siedlecki, C. A. Three-dimensional structure of human fibrinogen under aqueous conditions visualized by atomic force microscopy. Thromb. Haemostasis 1997, 77, 1048-1051.
    • (1997) Thromb. Haemostasis , vol.77 , pp. 1048-1051
    • Marchant, R.E.1    Barb, M.D.2    Shainoff, J.R.3    Eppell, S.J.4    Wilson, D.L.5    Siedlecki, C.A.6
  • 10
    • 0029862834 scopus 로고    scopus 로고
    • Direct observation of protein secondary structure in gas vesicles by atomic force microscopy
    • McMaster, T. J.; Miles, M. J.; Walsby, A. E. Direct observation of protein secondary structure in gas vesicles by atomic force microscopy. Biophys. J. 1996, 70, 2432-2436.
    • (1996) Biophys. J. , vol.70 , pp. 2432-2436
    • McMaster, T.J.1    Miles, M.J.2    Walsby, A.E.3
  • 11
    • 0031194365 scopus 로고    scopus 로고
    • Structural changes in native membrane proteins monitored at subnanometer resolution with the atomic force microscope: A review
    • Müller, D. G.; Schoenenberger, C. A.; Schabert, F.; Engel, A. Structural changes in native membrane proteins monitored at subnanometer resolution with the atomic force microscope: A review. Struct. Biol. 1997, 119, 149-157.
    • (1997) Struct. Biol. , vol.119 , pp. 149-157
    • Müller, D.G.1    Schoenenberger, C.A.2    Schabert, F.3    Engel, A.4
  • 12
    • 0041841000 scopus 로고    scopus 로고
    • Mapping flexible protein domains at subnanometer resolution with the atomic force microscope
    • Müller, D. J.; Fotiadas, D.; Engel, A. Mapping flexible protein domains at subnanometer resolution with the atomic force microscope. FEBS Lett. 1998, 430, 105-111.
    • (1998) FEBS Lett. , vol.430 , pp. 105-111
    • Müller, D.J.1    Fotiadas, D.2    Engel, A.3
  • 13
    • 0030397047 scopus 로고    scopus 로고
    • Imaging two-dimensional crystals of catalase by atomic force microscopy
    • Ohnishi, S.; Kara, M.; Furuno, T.; Sasabe, H. Imaging two-dimensional crystals of catalase by atomic force microscopy. Jpn. J. Appl. Phys. 1996, 35, 6233-6238.
    • (1996) Jpn. J. Appl. Phys. , vol.35 , pp. 6233-6238
    • Ohnishi, S.1    Kara, M.2    Furuno, T.3    Sasabe, H.4
  • 14
    • 0032523832 scopus 로고    scopus 로고
    • ATP-induced shape change of nuclear pores visualised with the atomic force microscope
    • Rakowska, A.; Danker, T.; Schneider, S. W.; Oberleithner, H. ATP-induced shape change of nuclear pores visualised with the atomic force microscope. J. Membr. Biol. 1998, 163, 129-136.
    • (1998) J. Membr. Biol. , vol.163 , pp. 129-136
    • Rakowska, A.1    Danker, T.2    Schneider, S.W.3    Oberleithner, H.4
  • 15
    • 0031951980 scopus 로고    scopus 로고
    • Molecular weights of individual proteins correlate with molecular volumes measured by atomic force microscope
    • Schneider, S. W.; Larmer, J.; Henderson, R. M.; Oberleithner, H. Molecular weights of individual proteins correlate with molecular volumes measured by atomic force microscope. Pfluegers Arch. Eur. J. Physiol. 1998, 435, 362-367.
    • (1998) Pfluegers Arch. Eur. J. Physiol. , vol.435 , pp. 362-367
    • Schneider, S.W.1    Larmer, J.2    Henderson, R.M.3    Oberleithner, H.4
  • 16
    • 0025357314 scopus 로고
    • The prolamin storage proteins of cereal seeds: Structure and evolution
    • Shewry, P. R.; Tatham, A. S. The prolamin storage proteins of cereal seeds: structure and evolution. Biochem. J. 1990, 267, 1-12.
    • (1990) Biochem. J. , vol.267 , pp. 1-12
    • Shewry, P.R.1    Tatham, A.S.2
  • 17
    • 0012342479 scopus 로고    scopus 로고
    • Disulphide bonds in wheat gluten proteins
    • Shewry, P. R.; Tatham, A. S. Disulphide bonds in wheat gluten proteins. J. Cereal Sci. 1997, 25, 207-227.
    • (1997) J. Cereal Sci. , vol.25 , pp. 207-227
    • Shewry, P.R.1    Tatham, A.S.2
  • 18
    • 0030924201 scopus 로고    scopus 로고
    • Scanning probe microscopies-applications in cereal science
    • Shewry, P. R.; Miles, M. J.; Thomson, N. H.; Tatham, A. S. Scanning probe microscopies-applications in cereal science. Cereal Chem. 1997, 74 (4), 193-199.
    • (1997) Cereal Chem. , vol.74 , Issue.4 , pp. 193-199
    • Shewry, P.R.1    Miles, M.J.2    Thomson, N.H.3    Tatham, A.S.4
  • 20
    • 0001211660 scopus 로고
    • The conformations of wheat gluten proteins. The secondary structures and thermal stabilities of the α-, β-, γ-and ω-gliadins
    • Tatham, A. S.; Shewry, P. R. The conformations of wheat gluten proteins. The secondary structures and thermal stabilities of the α-, β-, γ-and ω-gliadins. J. Cereal Sci. 1985, 3, 103-113.
    • (1985) J. Cereal Sci. , vol.3 , pp. 103-113
    • Tatham, A.S.1    Shewry, P.R.2
  • 21
    • 0002470531 scopus 로고
    • The S-poor prolamins of wheat, barley and rye
    • Tatham, A. S.; Shewry, P. R. The S-poor prolamins of wheat, barley and rye. J. Cereal Sci. 1995, 22, 1-16.
    • (1995) J. Cereal Sci. , vol.22 , pp. 1-16
    • Tatham, A.S.1    Shewry, P.R.2
  • 22
    • 0024970049 scopus 로고
    • Conformational studies of a synthetic peptide corresponding to the repeat motif of C hordein
    • Tatham, A. S.; Drake, A. F.; Shewry, P. R. Conformational studies of a synthetic peptide corresponding to the repeat motif of C hordein. Biochem. J. 1989, 259, 471-476.
    • (1989) Biochem. J. , vol.259 , pp. 471-476
    • Tatham, A.S.1    Drake, A.F.2    Shewry, P.R.3
  • 23
    • 0032985443 scopus 로고    scopus 로고
    • Small-angle X-ray scattering of wheat seed-storage proteins: α-, γ-and ω-gliadins and the high molecular weight (HMW) subunits of glutenin
    • Thomson, N. H.; Miles, M. J.; Popineau, Y.; Harries, J.; Shewry, P.; Tatham, A. S. Small-angle X-ray scattering of wheat seed-storage proteins: α-, γ-and ω-gliadins and the high molecular weight (HMW) subunits of glutenin. Biochim. Biophys. Acta Protein Struct. Mol. Enzymol. 1999, 1430, 359-366.
    • (1999) Biochim. Biophys. Acta Protein Struct. Mol. Enzymol. , vol.1430 , pp. 359-366
    • Thomson, N.H.1    Miles, M.J.2    Popineau, Y.3    Harries, J.4    Shewry, P.5    Tatham, A.S.6
  • 26
    • 0029952769 scopus 로고    scopus 로고
    • Fourier transform IR spectroscopy of hydration-induced structure changes in the solid state of omega-gliadins
    • Wellner, N.; Belton, P. S.; Tatham, A. S. Fourier transform IR spectroscopy of hydration-induced structure changes in the solid state of omega-gliadins. Biochem. J. 1996, 319, 741-747.
    • (1996) Biochem. J. , vol.319 , pp. 741-747
    • Wellner, N.1    Belton, P.S.2    Tatham, A.S.3
  • 27
    • 0001096080 scopus 로고
    • Starch gel electrophoresis of wheat gluten proteins with concentrated urea
    • Woychik, J. H.; Boundy, J. A.; Dimler, R. J. Starch gel electrophoresis of wheat gluten proteins with concentrated urea. Arch. Biochem. Biophys. 1961, 94, 477-482.
    • (1961) Arch. Biochem. Biophys. , vol.94 , pp. 477-482
    • Woychik, J.H.1    Boundy, J.A.2    Dimler, R.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.