Abstract:
:Epitopic peptides representing the C-terminal (HA1) region of cleaved hemagglutinin of influenza virus from different serotypes were synthesized. Circular dichroism and Fourier-transform infrared spectroscopic data showed that peptides HS2 and HS3 have a predominantly alpha-helical conformation in trifluoroethanol. Recently a component band appearing between 1640 and 1635 cm-1 in the amide I region of the Fourier-transform infrared spectra of polypeptides has been correlated with strongly H-bonded beta-turns (Ref. 8). Using this assignment, HS1 was found to contain less alpha-helix but have tendency to adopt beta-turn(s). Interestingly, fragment HS2 with the highest alpha-helix content proved to be the poorest T-cell epitope among serotypes HS1-HS3.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Holly S,Majer Z,Tóth GK,Váradi G,Rajnavölgyi E,Laczkó I,Hollósi Mdoi
10.1006/bbrc.1993.1759subject
Has Abstractpub_date
1993-06-30 00:00:00pages
1247-54issue
3eissn
0006-291Xissn
1090-2104pii
S0006-291X(83)71759-6journal_volume
193pub_type
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