amino acid

linear sequence of amino acids bounded by a polypeptide bond

amino acids that no longer posses ionizable amino or carboxyl groups

• the three dimensional arrangement of proteins as a result of folding. Bound by a hydrogen bond.
• two types of structure: a-helix, b-sheet

its small structure does not allow for h-bonding.

spiral arrangement with 3.6 amino acids residues per turn and R side chains extending outward

flat, extended arrangement either parallel or antiparallel

• the entire conformation of a complete polypeptide chain
• conformation is driven by hydrophobic effect where hydrophobic residues tend to be inside and hydrophillic residues tend to be outside

the assembly of two or more tertiary structures producing a complete functional protein

when there is a lack of alpha synuclein (protein) production which is necessary for the release of neurotransmitters in the synaptic vesicles in the brain.

caused by single point mutation, when glutamic acid (polar) is converted to valine (nonpolar) produces a sickle shaped hemoglobin structure