protein structure and folding

what are the parts of an amino acid?

central carbon, amino group, carboxyl group, R group

primary structure

covalent peptide bonds

secondary structure

hydrogen bonds form shapes (alpha helix, beta pleated sheets)

tertiary structure

attractions between secondary structure

quaternary structure

exists in proteins with more than one amino acid chain

hydropathy plot

analyzes protein structure based on hydro-affinity

protein domains

tertiary structures in a protein that have specific structural or functional features

how does the protein folding environment in vivo differ from protein folding in vitro?

there are crowded conditions, degradation signals, higher temperatures, and simultaneous translation and folding

protein chaperones

aid in folding, unfolding, and transport of proteins, not necessary for folding

what are the main protein chaperones?

heat shock proteins

how does HSP70 compare to HSP60

70 is more common, 60 exist mainly in mitochondria

HSP70

stabilizes translating proteins, transport proteins, and fold and unfold proteins

where do chaperone proteins bind?

hydrophobic regions, prevents hydrophobic amino acids from binding before they are properly folded

HSP40

identifies proteins needing assistance from HSP70