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Isolation and amino acid sequence of two new PR-4 proteins from wheat.
- Source :
-
Journal of protein chemistry [J Protein Chem] 2001 May; Vol. 20 (4), pp. 327-35. - Publication Year :
- 2001
-
Abstract
- We have purified and characterized two new pathogenesis-related (PR) proteins from wheat belonging to the PR-4 family. We named the proteins wheatwin3 and wheatwin4 in analogy with the previously characterized wheatwin1 and wheatwin2. Their isoelectric points were 7.1 and 8.4, respectively. We determined the complete amino acid sequence of both proteins by a rapid approach based on the knowledge of the primary structures of the homologous wheatwin1 and wheatwin2. Wheatwin3 differs from wheatwin1 in one substitution at position 88, while wheatwin4 differs from wheatwin2 in one substitution at position 78. The secondary structure and solvent accessibility of these residues were determined on the three-dimensional model of wheatwinl. Residue 88 was very accessible and was located in a flexible region. Preliminary results indicate that, like wheatwin1 and wheatwin2, wheatwin3 and wheatwin4 have antifungal activity.
- Subjects :
- Alkylation
Amino Acid Sequence
Antifungal Agents isolation & purification
Immunoblotting
Models, Molecular
Molecular Sequence Data
Peptide Fragments chemistry
Peptides chemistry
Peptides pharmacology
Plant Proteins chemistry
Sequence Analysis
Trypsin metabolism
Antifungal Agents chemistry
Plant Proteins isolation & purification
Triticum chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 0277-8033
- Volume :
- 20
- Issue :
- 4
- Database :
- MEDLINE
- Journal :
- Journal of protein chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 11594467
- Full Text :
- https://doi.org/10.1023/a:1010905802749