Studies on an Antifungal Protein and a Chromatographically and Structurally Related Protein Isolated from the Culture Broth of Bacillus amyloliquefaciens
An antifungal protein with multiple stable biological activities unaffected by chemical modification of tyrosine and tryptophan, and a protein with N-terminal sequence and molecular mass resemblance to the antifungal protein but no identifiable activities were isolated from culture broth of Bacillus amyloliquefaciens. The findings are analogous to previous reports on thaumatin and thaumatin-like proteins.
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Document Type: Research Article
Publication date: November 1, 2009
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- Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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