Specific interactions of Cu2+ ions with fragments of envelope protein of hepatitis B virus.
Potentionmetric and spectroscopic (EPR, CD and absorption spectra) data have shown that a fragment of envelope proteins of the hepatitis B virus could be very specific bind molecules for Cu2+ ions using arginine lateral NH2 donor sites. The presence of Pro and Asp residues makes Arg binding not only very specific, but also very efficient.
Chruściński
L
L
LC. Faculty of Process and Environmental Engineering, Technical University of Lódź, Poland.
Dyba
M
M
Jezowska-Bojczuk
M
M
Henryk-Kozłowski
Kupryszewski
G
G
Maćkiewicz
Z
Z
Majewska
A
A
D000595:Amino Acid Sequence; D001665:Binding Sites; D002942:Circular Dichroism; D003300:Copper / Q000737:chemistry / Q000378:metabolism*; D004578:Electron Spin Resonance Spectroscopy; D006515:Hepatitis B virus / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008024:Ligands; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D011199:Potentiometry; D011485:Protein Binding; D013053:Spectrophotometry; D014759:Viral Envelope Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
D008024:Ligands; D010446:Peptide Fragments; D014759:Viral Envelope Proteins; D003300:Copper