抄録
Raman spectra have been measured of a nonapeptide which has an amino acid sequence identical to that of the C-terminal region of the major coat protein subunit of Filamentous bacteriophage Pf3. The peptide shows a strong tendency to form a β-sheet structure in aqueous solution. The β-sheet formation is significantly promoted by complexation with single-stranded DNA but not with double-stranded DNA. It is suggested that the C-terminal region of the Pf3 coat protein binds to the single-stranded DNA genome in the virion with a β-sheet conformation, in sharp contrast with the α-helical binding in other filamentous bacteriophages.
本文言語 | English |
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ページ(範囲) | 181-184 |
ページ数 | 4 |
ジャーナル | FEBS Letters |
巻 | 307 |
号 | 2 |
DOI | |
出版ステータス | Published - 1992 7月 28 |
外部発表 | はい |
ASJC Scopus subject areas
- 生物理学
- 構造生物学
- 生化学
- 分子生物学
- 遺伝学
- 細胞生物学