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Analysis of the differential conformational behavior of two antigens of the hepatitis A virus through molecular dynamics and physicochemical measurements
|Authors:||Cantó, Josep; Haro Villar, Isabel; Alsina, M. Asunción; Pérez, Juan J.|
|Keywords:||Hepatitis A virus|
|Publisher:||American Chemical Society|
|Citation:||Journal of Physical Chemistry B - Condensed Phase 107(27): 6603-6608 (2003)|
|Abstract:||The surface activity of peptides with proven antigenic activity toward the hepatitis A virus (HAV), [Glu114]VP3(110−121) and [Lys113]VP3(110−121), analogues of the VP3(110−121) antigen of HAV with sequence FWRGDLVFDFQV, was deduced from compression isotherm experiments. The results showed that the lysine analogue exhibits a surface area about three times smaller than that of the glutamic acid analogue. To understand whether this observed differential conformational behavior of the two peptide analogues is a characteristic feature of the peptide sequences, we carried out 10 ns molecular dynamics simulations of the two analogues in water. The results of this study confirm a differential conformational behavior of the two peptides and provide support to the hypothesis of this observed behavior as the reason for the different surface areas obtained from compression isotherm experiments.|
|Description:||6 pages, 7 figures, 2 tables.-- Printed version published Jul 10, 2003.|
|Publisher version (URL):||http://dx.doi.org/10.1021/jp022556+|
|Appears in Collections:||(IQAC) Artículos|
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