Interaction of Lysine-Alanine-Alanine tripeptide with a fragment of DNA: An empirical potential study

✍ Scribed by Pavel Hobza; Dana Nachtigallová; Zdeněk Havlas; Petr Maloň; Jaroslav Šponar

• Book ID: 102878469
• Publisher: John Wiley and Sons
• Year: 1991
• Tongue: English
• Weight: 609 KB
• Volume: 12
• Category: Article
• ISSN: 0192-8651
• DOI: 10.1002/jcc.540120103

✦ Synopsis

Interaction of a rigid fragment of B-DNA (polyanionic as well as screened by Na+ cations) with the flexible tripeptide Lys-Ala-Ala (in both L and D configurations) were investigated with the aid of an empirical potential. The potential consists of intramolecular (MM2 potential) and intermolecular (pair potential described in reference 1) parts; hence total energy is formed by intra-and intermolecular components. The results demonstrate that intramolecular relaxation of the peptide results in a considerable decrease in total energy. While energies of DNA complexes with L-Lys-L-Ala-L-Ala were comparable to those with D-Lys-D-Ala-D-Ala the respective geometries exhibit considerable differences.