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1
A conformational study of a glutamine- and proline-rich cereal seed protein, C hordein.
Biochem J. 1985 Mar 1;226(2):557-62. doi: 10.1042/bj2260557.
3
Identification of a novel beta-turn-rich repeat motif in the D hordeins of barley.
Biochim Biophys Acta. 1992 Jul 31;1122(2):118-22. doi: 10.1016/0167-4838(92)90313-3.
4
Antioxidant capacities of fractionated barley hordein hydrolysates in relation to peptide structures.
Mol Nutr Food Res. 2013 Mar;57(3):493-503. doi: 10.1002/mnfr.201200252. Epub 2013 Jan 14.
5
Temperature-dependent binding of monoclonal antibodies to C hordein.
Biochim Biophys Acta. 2002 Jan 31;1594(1):17-26. doi: 10.1016/s0167-4838(01)00269-2.
6
Secondary structure prediction of seed storage proteins.
Int J Pept Protein Res. 1983 Oct;22(4):456-63. doi: 10.1111/j.1399-3011.1983.tb02115.x.
7
Targeted modification of storage protein content resulting in improved amino acid composition of barley grain.
Transgenic Res. 2016 Feb;25(1):19-31. doi: 10.1007/s11248-015-9911-7. Epub 2015 Oct 27.
10
13C-n.m.r. study of C hordein.
Biochem J. 1985 Dec 1;232(2):617-20. doi: 10.1042/bj2320617.

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2
Gliadins from wheat grain: an overview, from primary structure to nanostructures of aggregates.
Biophys Rev. 2018 Apr;10(2):435-443. doi: 10.1007/s12551-017-0367-2. Epub 2017 Dec 4.
5
The structure and function of proline-rich regions in proteins.
Biochem J. 1994 Jan 15;297 ( Pt 2)(Pt 2):249-60. doi: 10.1042/bj2970249.
6
A new Escherichia coli cell division gene, ftsK.
J Bacteriol. 1995 Nov;177(21):6211-22. doi: 10.1128/jb.177.21.6211-6222.1995.
7
13C-n.m.r. study of C hordein.
Biochem J. 1985 Dec 1;232(2):617-20. doi: 10.1042/bj2320617.
8
The structure of a high-Mr subunit of durum-wheat (Triticum durum) gluten.
Biochem J. 1987 Oct 1;247(1):215-21. doi: 10.1042/bj2470215.
10
The prolamin storage proteins of cereal seeds: structure and evolution.
Biochem J. 1990 Apr 1;267(1):1-12. doi: 10.1042/bj2670001.

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2
Characterization of soluble peptides of elastin by physical techniques.
Methods Enzymol. 1982;82 Pt A:673-716. doi: 10.1016/0076-6879(82)82096-x.
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Reverse turns in peptides and proteins.
CRC Crit Rev Biochem. 1980;8(4):315-99. doi: 10.3109/10409238009105470.
4
Conformation of model, alanine and proline containing tetrapeptides in water. Comparison of 13C-n.m.r. and CD results.
Int J Pept Protein Res. 1983 Mar;21(3):301-6. doi: 10.1111/j.1399-3011.1983.tb03108.x.
5
Conformational study of the salivary proline-rich polypeptides.
Int J Pept Protein Res. 1983 Mar;21(3):281-7. doi: 10.1111/j.1399-3011.1983.tb03105.x.
6
Conformational study of the basic proline-rich polypeptides from human parotid saliva.
Int J Pept Protein Res. 1984 Feb;23(2):158-65. doi: 10.1111/j.1399-3011.1984.tb02706.x.
9
Computed circular dichroism spectra for the evaluation of protein conformation.
Biochemistry. 1969 Oct;8(10):4108-16. doi: 10.1021/bi00838a031.

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