pH-Dependent Conformational Changes in Proteins and Their Effect on Experimental pKas: The Case of Nitrophorin 4
Figure 2
Time evolution of relevant parameters when closed NP4 is placed at a solvent pH of 7.5.
Top: Running average of distance Asp30-Leu130; Middle: Running average of distance Asp35-Asp129; Bottom: Asp30 microscopic pKa. The average values of these distances in the stable simulations of the closed (red) and the open (blue) structures are also shown.