Masking of some charged groups in a protein with beta-structure.
Reactivity of amino groups, phenoxy groups of tyrosine residues and some other charged groups of Tricoplusia ni granulosis virus granulin, which had rigid subunit structure abundant in beta-configuration, was investigated. It was found that there were nonreactive alpha-amino, phenoxy and some other groups in the native protein, and that they became reactive after an alkaline treatment which brought about conformational change of the protein to a random structure. The possibility of the contribution of the beta-structure for the masking of these residues is discussed.[1]References
- Masking of some charged groups in a protein with beta-structure. Egawa, K. Jpn. J. Exp. Med. (1975) [Pubmed]
Annotations and hyperlinks in this abstract are from individual authors of WikiGenes or automatically generated by the WikiGenes Data Mining Engine. The abstract is from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.About WikiGenesOpen Access LicencePrivacy PolicyTerms of Useapsburg