Effect of selected Hofmeister anions on the secondary structure and dynamics of wheat prolamins in gluten

Cereal Chemistry

Volumn 80, Issue 5, 2003, Pages 596-600

  Wellner, Nikolaus ^a   Bianchini, David ^a   Mills, E N Clare ^a   Belton, Peter S ^b  

^a NORWICH RESEARCH PARK   (United Kingdom)

^b UNIVERSITY OF EAST ANGLIA   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

BROMINE COMPOUNDS; IODINE COMPOUNDS; IONS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; SODIUM CHLORIDE;

CHAOTROPIC ANIONS; HELIX STRUCTURES; HOFMEISTER; NMR-SPECTROSCOPY; SECONDARY DYNAMICS; SECONDARY STRUCTURES; SPECTRA'S; STRUCTURE AND DYNAMICS; STRUCTURE CHARACTERISTIC; Β-SHEET STRUCTURE;

SODIUM IODIDE;

ANION; GLUTEN; PROLAMIN; SODIUM BROMIDE; SODIUM CHLORIDE;

ARTICLE; BETA SHEET; FOURIER TRANSFORMATION; INFRARED SPECTROSCOPY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN SECONDARY STRUCTURE; WHEAT;

TRITICUM AESTIVUM;

EID: 0141568214     PISSN: 00090352     EISSN: None     Source Type: Journal    
DOI: 10.1094/CCHEM.2003.80.5.596     Document Type: Article

References (24)

1. Belton, P. S. 1999. On the elasticity of wheat gluten. J. Cereal Sci. 29:103-107.
2. r subunit of wheat glutenin and comparison with elastin. J. Cereal Sci. 19:115-121.
3. Belton, P. S., Colquhoun, I. J., Grant, A., Wellner, N., Field, J. M., Shewry, P. R., and Tatham, A. S. 1995. FTIR and NMR studies on the hydration of a high-M(r) M(d subunit of glutenin. Int. J. Biol. Macromol. 17:74-80.
4. Butow, B. J., Gras, P. W., Haraszi, R., and Bekes, F. 2002. Effects of different salts on mixing and extension parameters on a diverse group of wheat cultivars using 2-g mixograph and extensigraph methods. Cereal Chem. 79:826-833.
5. Byler, D. M., and Susi, H. 1986. Examination of the secondary structure of proteins by deconvoluted FTIR spectra. Biopolymers 25:469-487.
6. Cacace, M. G., Landau, E. M., and Ramsden, J. J. 1997. The Hofmeister series: Salt and solvent effects on interfacial phenomena. Q. Rev. Biophys. 30:241-277.
7. r subunit of durum wheat (Triticium durum) gluten. Biochem. J. 247:215-221.
8. Gilbert, S. M., Wellner, N., Belton, P. S., Greenfield, J. A., Siligardi, G., Shewry, P. R., and Tatham, A. S. 2000. Expression and characterisation of a highly repetitive peptide derived from a wheat seed storage protein. Biochim. Biophys. Acta Protein Struc. Molecular Enzymol. 1479:135-146.
9. Grant, A., Belton, P. S., Colquhoun, I. J., Parker, M. L., Plijter, J. J., Shewry, P. R., Tatham, A. S., and Wellner, N. 1999. Effects of temperature on sorption of water by wheat gluten determined using deuterium nuclear magnetic resonance. Cereal Chem. 76:219-226.
10. He, H., Roach, R. R., and Hoseney, R. C. 1992. Effect of nonchaotropic salts on flour bread-making properties. Cereal Chem. 69:366-371.
11. Kim, H. R., and Bushuk, W. 1995. Salt sensitivity of acetic acid-extractable proteins of wheat flour. J. Cereal Sci. 21:241-250.
12. Kinsella, J. E., and Hale, M. L. 1984. Hydrophobic associations and gluten consistency: Effects of specific anions. J. Agric. Food. Chem. 32:1054-1056.
13. Larsson, H. 2002. Effect of pH and sodium chloride on wheat flour dough properties: Ultracentrifugation and rheological measurements. Cereal Chem. 79:544-545.
14. Parchment, O., Shewry, P. R., Tatham, A. S., and Osguthorpe, D. J. 2001. Molecular modeling of unusual spiral structure in elastomeric wheal seed protein. Cereal Chem. 78:658-662.
15. Pézolet, M., Bonenfant, S., Dousseau, F., and Popineau, Y. 1992. Conformation of wheat gluten proteins-Comparison between functional and solution states as determined by infrared spectroscopy. FEBS Lett. 299:247-250.
16. Preston, K. R. 1989. Effects of neutral salts of the lyotropic series on the physical dough properties of a Canadian red spring wheat flour. Cereal Chem. 66:144-148.
17. Sakurai, K., Oobatake, M., and Goto, Y. 2001. Salt-dependent monomer-dimer equilibrium of bovine β-lactoglobulin at pH 3. Prot. Sci. 10:2325-2335.
18. Shewry, P. R., Miles, M. J., and Tatham, A. S. 1994. The prolamin storage proteins of wheat and related cereals. Prog. Biophys. Molec. Biol. 61:37-59.
19. Singh, H., and MacRitchie, F. 2001. Application of polymer science to properties of gluten. J. Cereal Sci. 33:231-243.
20. Tatham, A. S., Miflin, B. J., and Shewry, P. R. 1985. The β-turn conformation in wheat glutenin proteins: Relationship to gluten elasticity. Cereal Chem. 62:405-412.
21. Tatham, A. S., Field, J. M., Smith, S. J., and Shewry, P. R. 1987. The conformations of wheat gluten proteins. 2. Aggregated gliadins and low molecular weight subunits of glutenin. J. Cereal Sci. 5:203-214.
22. VanDijk, A. A., VanWijk, L. L., VanVliet, A., Haris, P., VanSwieten, E., Tesser, G. I., and Robillard, G. T. 1997. Structure characterization of the central repetitive domain of high molecular weight gluten proteins. 1. Model studies using cyclic and linear peptides. Prot. Sci. 6:637-648.
23. 2O) solutions. 1. Spectral parameters of amino acid residue absorption bands. Biopolymers 30:1243-1257.
24. Wellner, N., Belton, P. S., and Tatham, A. S. 1996. Fourier transform IR spectroscopic study of hydration-induced structure changes in the solid state of ω-gliadins. Biochem. J. 319:741-747.