See if you can tell why each amino acid has been sorted in that way. For these amino acids, the deprotonated forms predominate at physiological pH (about 7).Ĭlick on the Protein 1 icon at left to see a chart of all the amino acids, classified according to the chemistry of their side chains. Their side chains have carboxylic acid groups whose pKa's are low enough to lose protons, becoming negatively charged in the process.Ĭlick on the structures below to switch between their protonated and deprotonated forms. These are aspartic acid or aspartate (Asp) and glutamic acid or glutamate (Glu). A hydrocarbon chain or a similar nonpolar region of a large molecule is incapable of forming hydrogen bonds with water. Some argue that the hydrophobic interaction is mostly an entropic effect originating from the disruption of highly dynamic hydrogen bonds between molecules of liquid water by the nonpolar solute. For these amino acids, the protonated forms predominate at physiological pH (about 7). The origin of the hydrophobic effect is not fully understood. Their pKa's are high enough that they tend to bind protons, gaining a positive charge in the process.Ĭlick on the structures below to switch between their protonated and deprotonated forms. Their side chains contain nitrogen and resemble ammonia, which is a base. These are arginine (Arg), lysine (Lys), and histidine (His). There are three amino acids that have basic
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