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By definition, an amino acid bares an amine group on one face and an acidic group on another face. Imagining the central carbon with four equally spaced groups around it, separated by a bond angle of 109.5 degrees, the other two faces are a single proton (hydrogen) and a variable position.
The amine group can be protonated at low pH and the carboxylic acid group can be deprotonated at neutral and high pH. Biochemists typically draw amino acids in Zwitterionic form with an overall zero charge balanced between the positive amino and the negative acid groups.
Amino acids are generally divided up by their characteristics: Nonpolar, Polar, Acidic, Basic. The forces governing the folding of proteins and interactions between these single units and the microscopic biological machinery that synthesizes them can be predicted by considering these four cardinal characteristics of these molecules.
One of the reasons we need to consume plants (and other kingdoms of life) is that we need to assimilate amino acids that we do not make ourselves. Amino acid biosynthesis is a pathway often targeted by synthetic pesticides because it is non-toxic to humans. The ratios of these molecules in living systems can become disrupted by chemical or environmental stress. We can observe this phenomena using Nuclear Magnetic Resonance (NMR).
Sources:
Larsen, P. ELEMENTARY BIOCHEMISTRY (BCH 100), Spring 2007, University of California Riverside. Lecture 3: Amino acids, Peptides. Notes from Friday, April 6, 2007.
M. K. Campbell & S. Farrell. BIOCHEMISTRY, 5th edition, Thomson Brooks/Cole Publishers.
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