Structure characterization of the central repetitive domain of high molecular weight gluten proteins. II. Characterization in solution and in the dry state

Protein Science

Volumn 6, Issue 3, 1997, Pages 649-656

  Van Dijk, Alard A ^a,c   De Boef, Esther ^b   Bekkers, August ^b   Van Wijk, Lourens L ^a   Van Swieten, Eric ^a   Hamer, Rob J ^b   Robillard, George T ^a  

^a UNIVERSITY OF GRONINGEN   (Netherlands)

^b TNO   (Netherlands)

^c Gist Brocades NV   (Netherlands)

Author keywords

elastic properties; repetitive proteins; structural characterization; wheat gluten proteins

Indexed keywords

GLUTEN;

ARTICLE; DATA ANALYSIS; HYDROGEN BOND; MOLECULAR CLONING; MOLECULAR WEIGHT; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN STRUCTURE; STRUCTURE ACTIVITY RELATION;

TRITICUM AESTIVUM;

EID: 0030972492     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560060314     Document Type: Article

References (27)

1. Anderson OD, Greene FC. 1989. The characterization and comparative analysis of high-molecular-weight glutenin genes from genomes A and B of a hexaploid bread wheat. Theor Appl Genet 77:689-700.
2. Anderson OD, Greene FC, Yip RE, Halford NG, Shewry PR, Malpica-Romero JM. 1989. Nucleotide sequence of two high-molecular-weight glutenin genes from the D-genome of a hexaploid bread wheat, Triticum aestivum L. cv. Cheyenne. Nucleic Acids Res 17:461-462.
3. r subunit of wheat glutenin and comparison with elastin. J Cereal Sci 19:115-121.
4. Doyen C, Anglade P, Lauriere M. 1994. Characterization of the high molecular weight glutenin subunit 20 from wheat, isolated by preparative blotting. In: Wheat kernel proteins: molecular and functional aspects. Viterbo, Italy: Universita degli Studi della Tuscia. pp 221-223.
5. r subunit of durum-wheat (Triticum durum) gluten. Biochem J 247:215-221.
6. Goldsbrough AP, Bulleid NJ, Freedman RB, Flavell RB. 1989. Conformational differences between two wheat (Triticum aestivum) high molecular weight glutenin subunits are due to a short region containing six amino acids differences. Biochem J 263:837-842.
7. Hickman DR, Roepstorff P, Clarke AR, Tatham AS, Shewry PR. 1994. Physicochemical characterisation of high molecular weight subunits of wheat glutenin. In: Wheat kernel proteins: molecular and functional aspects. Viterbo, Italy: Universita degli Studi della Tuscia. pp 75-80.
8. Hollósi M, Majer Zs, Rónai AZ, Magyar A, Medzihradsky K, Holly S, Perczel A, Fasman GD. 1994. CD and fourier transform IR spectroscopic studies of peptides. II. Detection of β-turns in linear peptides. Biopolymers 34:177-185.
9. Holton TA, Graham MW. 1991. A simple and efficient method for direct cloning of PCR products using ddT-tailed vectors. Nucleic Acids Res 19:1156.
10. Hou G, Yamamoto H, Ng PKW. 1996. Relationships of quantity of gliadin subgroups of selected US soft wheat flours to rheological and baking properties. Cereal Chem 75:352-357.
11. Khelifi D, Branlard G. 1990. A new two-step electrophoresis method for analysing gliadin polypeptides and high and low molecular weight subunits of glutenin of wheat. J Cereal Sci 13:41-47.
12. Laemmli UK. 1970. Cleavage of structural proteins during the assembly of bacteriophage T4. Nature 227:680-685.
13. Miles MJ, Carr HJ, McMaster TC, I'Anson KJ, Belton PS, Moms VJ, Field JM, Shewry PR, Tatham AS. 1991. Scanning tunneling microscopy of a wheat seed storage protein reveals details of an unusual supersecondary structure. Proc Natl Acad Sci USA 88:68-71.
14. Perczel A, Hollósi M. 1996. Turns. In: Fasman GD, ed. Circular dichroism and the conformational analysis of biomolecules. New York: Plenum Press. pp 285-380.
15. Pézolet M, Bonenfant S, Dousseau F, Popineau Y. 1992. Conformation of wheat gluten proteins. Comparison between the functional and solution states as determined by infrared spectroscopy. FEBS Lett 299:247-250.
16. Sambrook J, Fritsch EF, Maniatis T. 1989. Molecular cloning, 2nd ed. Cold Spring Harbor, New York: Cold Spring Harbor Laboratory Press.
17. Sharp PM, Li WH. 1987. The codon adaptation index as a measure of directional synonymous codon usage bias, and its potential applications. Nucleic Acids Res 15:1281-1295.
18. Shewry PR, Field JM, Faulks AJ, Parmar S, Miflin BJ, Dietler MD, Lew EJL, Kasarda DD. 1984. The purification and N-terminal amino acid sequence analysis of the high molecular weight gluten polypeptides of wheat. Biochim Biophys Acta 788:23-34.
19. Shewry PR, Halford NG, Tatham AS. 1992. High molecular weight subunits of wheat glutenin. J Cereal Sci 15:105-120.
20. Shewry PR, Miles MJ, Tatham AS. 1994. The prolamin storage proteins of wheat and related cereals. Prog Biophys Mol Biol 61:31-59.
21. Tatham AS, Hickman DR, Shewry PR. 1993. High molecular weight subunits: A reassessment. In: Gluten proteins. Detmold, Germany: Association of Cereal Science. pp 38-46.
22. Tatham AS, Shewry PR, Miflin BJ. 1984. Wheat gluten elasticity: A similar molecular basis to elastin? FEBS Lett 177:205-208.
23. Urry DW. 1993. Molecular machines: How motion and other functions of living organisms can result from reversible chemical changes. Angew Chem Int Ed Engl 32:819-841.
24. van Dijk AA, van Wijk LL, van Vliet A, Haris P, van Swieten E, Tesser GI, Robillard GT. 1997. Structure characterization of the central repetitive domain of high molecular weight gluten proteins. I. Model studies using cyclic and linear peptides. Protein Sci 6:637-648.
25. Wilmot CM, Thornton JM. 1988. Analysis and prediction of the different types of β-turn in proteins. J Mol Biol 203:221-232.
26. Woody RW. 1974. Studies of theoretical circular dichroism of polypeptides: Contributions of β turns. In: Blout ER, Bovey FA, Goodman M, Latan N, eds. Peptides, polypeptides and proteins. New York: John Wiley & Sons Inc. pp 338-350.
27. Woody RW. 1996. Theory of circular dichroism of proteins. In: Fasman GD, ed. Circular dichroism and the conformational analysis of biomolecules. New York: Plenum Press. pp 25-68.