linear sequence of amino acids bounded by a polypeptide bond
what are residues
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
why is proline known as a helix breaker
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
describe tertiary structure
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
describe quarternary structure
the assembly of two or more tertiary structures producing a complete functional protein
what is familiar parkinson's disease
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.
what is sickle cell anemia
caused by single point mutation, when glutamic acid (polar) is converted to valine (nonpolar) produces a sickle shaped hemoglobin structure
amino acid, residues, primary, secondary, tertiary and quarternary structure