Abstract
We here report the results of MD simulations for several systems including a model peptide which has two tandem repeats of the characteristic 11-mer motif found in group 3 late embryogenesis abundant (G3LEA) proteins and its partner protein (lysozyme and HybD) in aqueous solution. And for comparison, we performed MD simulations for a control peptide which has the same amino acid composition as that of the G3LEA model but a scrambled sequence. As a result, the G3LEA model was found to spontaneously approach its partner and form the association complex. According to detailed analysis, the acidic residues (Glu and Asp) and basic residues (Lys) in the G3LEA model contribute to binding to lysozyme and HybD, respectively. Similar results were obtained for the control peptide.
