Live Poster Session: Zoom Link
Thursday, July 30th 1:15-2:30pm EDT
Abstract: Protein dimerization has been shown to play an integral role in many biological functions, from regulation of cellular mechanisms to forming important enzymatic structures. The enzyme LigAB is a homodimer of heterodimers of which the active site is located at the heterodimeric interface. In previous mutagenesis experiments, it was observed that certain mutations of the Phe103α residue, notably alanine and serine, prevented LigAB from co-purifying as a heterodimer. This finding indicated the potential to disrupt stability at the dimeric interface in the absence of a large, non-polar residue at this particular position. Because the dimeric interface is also the site of catalysis, altered stability of mutants could also affect their enzymatic activity. Using the GROMACS molecular dynamics package, the relative stability of the dimer interface was determined for various mutants. Fluctuation values were mapped and compared to corresponding values in wild type, looking specifically at residues known to occupy the active site and allosteric pockets. By comparing these values and additional binding free energy calculations to experimental data, more information about the stability of the dimer interface can be elucidated, specifically which residues or interactions might be crucial for co-purification of the dimer.
KLuo_Summer2020_Poster-Kate-LuoLive Poster Session: Zoom Link
Thursday, July 30th 1:15-2:30pm EDT