Conformational and functional properties of peptides covering the intersubunit region of influenza virus hemagglutinin.
The functionally active part of influenza virus hemagglutinin was investigated through the synthesis of a series of peptides representing different parts of the intersubunit region. Secondary structure prediction, circular dichroism and Fourier transform infrared spectroscopic studies were undertaken to investigate the secondary structure of these peptides. The peptide fragments were found to adopt multiple conformations, depending on their concentration in solution, the presence of the non-ionic detergent octyl-beta-D-glucoside and the polarity of the solvent. The results of biological studies with these peptide fragments are discussed in relation to their conformation, as inferred from the spectroscopic analysis.
Hollósi
M
M
Department of Organic Chemistry, Eötvös University, Budapest, Hungary.
Ismail
A A
AA
Mantsch
H H
HH
Penke
B
B
Varadi
I G
IG
Toth
G K
GK
Laczkó
I
I
Kurucz
I
I
Nagy
Z
Z
Fasman
G D
GD
D000595:Amino Acid Sequence; D002942:Circular Dichroism; D005583:Fourier Analysis; D019267:Hemagglutinin Glycoproteins, Influenza Virus; D006389:Hemagglutinins, Viral / Q000737:chemistry* / Q000235:genetics; D008969:Molecular Sequence Data; D011487:Protein Conformation; D012996:Solutions; D013055:Spectrophotometry, Infrared; D014270:Trifluoroethanol; D014759:Viral Envelope Proteins / Q000737:chemistry* / Q000235:genetics
D019267:Hemagglutinin Glycoproteins, Influenza Virus; D006389:Hemagglutinins, Viral; D012996:Solutions; D014759:Viral Envelope Proteins; D014270:Trifluoroethanol