Raman spectroscopic study on the conformation of a peptide fragment representing the DNA‐binding domain of filamentous virus Pf3 coat protein

FEBS Letters

Harada, Issei¹  Miura, Takashi¹  Takeuchi, Hideo¹ 

[1] Pharmaceutical Institute, Tohoku University, Aobayama, Sendai 980, Japan

关键词: Filamentous virus;    Coat protein;    Secondary structure;    DNA—protein interaction;    Raman spectroscopy;   

DOI  :  10.1016/0014-5793(92)80763-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown