Dielectric Constant and Solvent Effect Investigafion on Listeria monoeytogenes In1B-13- sheet Conformation: an Al. initio-NMR study

Abstract

IniB-the main external virulence factor of the bacterium Listeria monueytogenes- contains seven parallelB-strands at its concave face with a patches of five exposed aromatic amino acids as a hot spot for host receptor<br />(Met) binding. For better understanding of energetic and physicochemical pmpendes, (u)folding transition,<br />binding affinity and makmetic shielding censors of JAB-CRP-II-sheet ab hullo computer-aided methods have<br />been performed at the Hartree-Fork level. These calculations are based on the influence of solvent polarity as<br />well as hydrogen bond donor and acceptor strensth of it with respect to the self-consistent reaction field<br />(SCRF) method using Onsager model. The optimized molecule with 6-316(4) basis yet in the as phase<br />was used as initial input for subsequent liFiSCRT calculations implementing 6-310(d,p) atomic basis set CO<br />simulate the solscnt effect. To gain further insight to solvent effects on aromatic amino acids IIN and 1.0<br />atoms engaged in hydrogen bonding with receptor, NMR studies have been carried out on the basis of gaugeincluding<br />atomic orbital (GIAO) method at HF/6-3ICi (d,p) level of theory HE' calculations obtained with a<br />good agreement by the presented experimental data and predict the most molecule instability in the solvents<br />by low dielectric constants like THE and existence of a cooperaivi among 0-strands. physicochemically<br />There are various potential of hydrogen bond donors and acceptors among this unique, packed and exposed<br />linearly arrangement of aromatic amino acids that have made it an ideal part for drug design.