Experimental studies of ionic interactions near a hydrophobic surface in an aqueous environment
Tuesday, May 12, 2015 - 08:00
in Physics & Chemistry
(Phys.org)—The way a protein folds in aqueous solutions is largely determined by hydrophobic effects with the hydrophobic portions of the protein residing within the protein core or within the active site. Oftentimes, ionic interactions will occur in the hydrophobic active site. In theory, an ion pair will form a stronger interaction the closer the ions are to a hydrophobic surface, which is attributed to how the ions and the hydrophobic surface interact with the bulk water.