three-dimensional structure in solution of barwin, a protein from barley seed
In molecular biology, the barwin domain is a protein domain found in barwin, a basic protein isolated from aqueous extracts of barley seeds. Barwin is 125 amino acids in length, and contains six cysteine residues that combine to form three disulphide bridges. Comparative analysis shows the sequence of barwin to be highly similar to a 122 amino acid stretch in the C-terminal of the products of two wound-induced genes (win1 and win2) from potato, the product of the hevein gene of rubber trees, and pathogenesis-related protein 4 from tobacco. The high levels of similarity to these proteins, and their ability to bind saccharides, suggest that the barwin domain may be involved in a common defence mechanism in plants.
- Svensson B, Svendsen I, Hojrup P, Roepstorff P, Ludvigsen S, Poulsen FM (September 1992). "Primary structure of barwin: a barley seed protein closely related to the C-terminal domain of proteins encoded by wound-induced plant genes". Biochemistry. 31 (37): 8767–70. PMID 1390663. doi:10.1021/bi00152a012.
- Ludvigsen S, Poulsen FM (September 1992). "Secondary structure in solution of barwin from barley seed using 1H nuclear magnetic resonance spectroscopy". Biochemistry. 31 (37): 8771–82. PMID 1390664. doi:10.1021/bi00152a013.