Figure 8
From: Dynamic electrophoretic fingerprinting of the HIV-1 envelope glycoprotein
Electrostatic surface potential calculations on differing conformational states of trimeric influenza HA protein. (A) The amino acid type (left panels) and electrostatic surface potential (right panels) of 3 HA protein forms – native protein conformation, low pH triggered conformation after being reneutralized, and low pH conformation (PDB codes 3QQB, 3QQE and 3QQO respectively) all shown under pH 5.5 conditions. (B) Electrostatic surface potential charge asymmetry (A) over a range of pH/pλ shows the relative degree of protonation for each HA structure. (C) Differences in charge asymmetry (ΔA) between HA conformations are focused around pH 5.5.