- 1) Wolf, W.J., Soybean proteins: Their functional, chemical, and physical properties. J. Agric. Food Chem., 18, 969-976 (1970).
- 2) Kinsella, J.E., Functional properties of soy proteins. J. Am. Oil Chem. Soc., 56, 242-258 (1979).
- 3) Sebastiani, F.L., Farrell, L.B., Schuler, M.A., and Beachy, R.N., Complete sequence of a cDNA of α subunit of soybean β-conglycinin. Plant Mol. Biol., 15, 197-201 (1990).
- 4) Koshiyama, I., Comparision of acid-induced conformation changes between 7S and 11S globulin in soybean seeds. J. Sci. Food Agric., 23, 853-859 (1972).
- 5) Koshiyama, I., Some aspects of subunit structure of a 7S protein in soybean globulins. Agric. Biol. Chem., 35, 385-392 (1971).
- 6) Ishino, K. and Kudo S., Gelation phenomena induced by alkali-alcohol treatment of 7S and 11S components in soybean globulins. Agric. Biol. Chem., 41, 1347-1352 (1977).
- 7) Ishino, K. and Kudo S., Conformational transition of alkali-denatured soybean 7S and 11S globulins by ethanol. Agric. Biol. Chem., 44, 537-543 (1980).
- 8) Morita, S., Fukase, M., Yamaguchi, M., Fukuda, Y., and Morita, Y., Purification, characterization, and crystallization of single molecular species of β-conglycinin from soybean seeds. Biosci. Biotechnol. Biochem., 60, 866-873 (1996).
- 9) Ko, T.-P., Ng, J.D., and McPherson, A., The three-dimensional structure of canavalin from jack bean (Canavalia ensiformis). Plant Physiol., 101, 729-744 (1993).
- 10) Lawrence, M.C., Suzuki, E., Varghese, J.N., Davis, P.C., Van Donkelaar, A., Tulloch, P.A., and Colman, P.M., The three-dimensional structure of the seed storage protein phaseolin at 3 Å resolution. EMBO J., 9, 9-15 (1990).
- 11) Lawrence, M.C., Izard, T., Beauchat, M., Blagrove, R.J., and Colman, P.M., Structure of phaseolin at 2.2 Å resolution. Implications for a common vicilin/legumin structure and the genetic engineering of seed storage proteins. J. Mol. Biol., 238, 748-776 (1994).
- 12) Utsumi, S., Matsumura, Y. and Mori, T., Structure-function relationships of soy proteins. In “Food Proteins and Their Applications”, eds. Damodaran, S. and Paraf, A., Marcel Dekker, New York, pp. 257-291 (1997).
- 13) Maruyama, N., Katsube, T., Wada, Y., Oh, M.H., Barba De La Rosa, A.P., Okuda, E., Nakagawa, S., and Utsumi, S., The roles of the N-linked glycans and extention regions of soybean β-conglycinin in folding, assembly and structural features. Eur. J. Biochem., 258, 854-862 (1997).
- 14) Yang, J.T., Wu, C.-S., and Martinez, H.M., Calculation of protein comformation from circular dichroism. Methods in Enzymol., 130, 208-269 (1986).
- 15) Zirwer, D., Gast, K., Plietz, P., Schlesier, B., and Schwenke, K.D., Dynamic light scattering studies of globulins from plant seeds. Die Nahrung, 30, 251-255 (1986).
- 16) Alexandrescu, A.T., Ng, Y.-L., and Dobson, C.M., Characterization of trifluoroethanol-induced partially folded state of α-lactalbumin. J. Mol. Biol., 235, 587-599 (1994).
- 17) Christensen, H. and Pain, R.H., Molten globule intermediates and protein folding. Eur. Biophys. J., 19, 221-229 (1991).
- 18) Semisotnov, G.V., Rodionova, N.A., Razgulyaev, O.I., Uversky, V.N., Gripas’, A.F., and Gilmanshin, R.I., Study of the “Molten globule” intermediate state in protein folding by a hydrophobic fluorescent probe. Biopolymers, 31, 119-128 (1991).
- 19) Kamatari, Y.O., Konno, T., Kataoka, M., and Akasaka, K., The methanol-induced transition and the expanded helical conformation in hen lysozyme. Protein Sci., 7, 681-688 (1998).
- 20) Nagano, T., Akasaka, T., and Nishinari, K., Study on the heat-induced conformational changes of β-conglycinin by FTIR and CD analysis. Food Hydrocoll., 9, 83-89 (1995).
- 21) Byler, D.M. and Susi, H., Examination of the secondary structure of proteins by deconvolved FTIR spectra. Biopolymers, 25, 469-487 (1986).
- 22) Surewicz, W.K. and Mantsch, H.H., New insight into protein secondary structure from resolution-enhanced infrared spectra. Biochem. Biophys. Acta, 952, 115-130 (1988).
- 23) Byler, D.M. and Purcell, J.M., FTIR examination of thermal denaturation and gel-formation in whey proteins. Proc. SPIE, Int. Opt. Engl. Soc. (Fourier-Transform Spectroscopy), 1145, 415-417 (1989).
- 24) Jackson, M. and Mantsh, H.H., Halogenated alcohols as solvents for proteins: FTIR spectroscopic studies. Biochem. Biophys. Acta, 1118, 139-143 (1992).
- 25) Hirota, N., Mizuno, K., and Goto, Y., Cooperative α-helix formation of β-lactoglobulin and melittin induced by hexafluoroisopropanol. Protein Sci., 6, 416-421 (1997).
- 26) Doyle, J.J., Schuler, M.A., Godette, W.D., Zenger, V., Beachy, R.N., and Slightom, J.L., The glycosylated seed strage proteins of Glycine max and Phaseolus vulgaris. J. Biol. Chem., 261, 9228-9238 (1986).
- 27) Blout, E.R., De Loze, C., Bloom, S.M., and Fasman, G.D., The dependence of the conformations of synthetic polypeptides on amino acid composition. J. Am. Chem. Soc., 82, 3787-2789 (1960).
- 28) Holzwarth, G. and Doty, P., The ultraviolet circular dichroism of polypeptides. J. Am. Chem. Soc., 87, 218-228 (1965).
- 29) Garnier, J., Osguthorpe, D.J., and Roboson, B., Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. J. Mol. Biol., 120, 97-120 (1978).
Full access
Conformational Change in a Single Molecular Species, β3, of β-Conglycinin in Acidic Ethanol Solution
Reprints and Corporate Permissions
Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?
To request a reprint or corporate permissions for this article, please click on the relevant link below:
Academic Permissions
Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?
Obtain permissions instantly via Rightslink by clicking on the button below:
If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.
Related research
People also read lists articles that other readers of this article have read.
Recommended articles lists articles that we recommend and is powered by our AI driven recommendation engine.
Cited by lists all citing articles based on Crossref citations.
Articles with the Crossref icon will open in a new tab.