ISSN:
1573-3904
Keywords:
Hepatitis A
;
Circular dichroism
;
Conformational analysis
;
Molecular mechanics
;
Liposomes
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
Abstract A conformational analysis of the fragment 110–121 of VP3 coating protein of the hepatitis A virus was carried out using circular dichroism spectroscopy and computational studies. The latter studies indicate the tendency of the peptide to adopt hairpin-type structures. Circular dichroism experiments indicate that, in spite of the fact that the isolated peptide exhibits no structure under different experimental conditions, negatively charged liposomes induce a secondary structure that agrees with the results of the computational study.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1023/A:1008817514647
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