amino acids/peptide bonds

proteins

linear polymers of amino acids joined by peptide bonds; function determined by structure

types of protein structure

primary, secondary, tertiary, quaternary

amino acids

building blocks that make up protein sequence; vary by size, shape, chemical bonding/reactivity, charge, polarity

nonpolar amino acids

glycine, alanine, valine, leucine, isoleucine, methionine, proline

aromatic amino acids

tryptophan, phenylalanine, tyrosine

polar uncharged amino acids

serine, threonine, cysteine, asparagine, glutamine

acidic amino acids

aspartate, glutamate (negatively charged)

basic amino acids

histidine, lysine, arginine (positively charged)

peptide bonds

bonds between alpha-carboxyl carbon and the next alpha-amine nitrogen; have double-bond character due to resonance delocalization