BIOLOGY 2B03 Lecture Notes - Lecture 2: Endoplasmic Reticulum, Protein Folding, Hsp70
13 Oct 2018
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3 ways for protein folding: most protein will fold rapidly into native configuration. Incomplete folding receive assistant from chaperone proteins. Chaperon: monomeric molecular chaperons, binds to hydrophobic amino acid r groups. Prevent from folding prematurely and from aggregating with other hydrophobic residues. Examples (heat shock protein hsp) refold protein at a faster rate when temperature are raised: hsp 70 in cytosol and mitochondria, bip in endoplasmic reticulum, dnak in bacteria cells. Hsp 70 contains 2 domains: nucleotide binding domain (blue, substrate-binding domain (orange) Atp hydrolysis to adp, allow the protein to fold. Chaperonin: multimeric chaperonin complex; large, macromolecular complexes containing different proteins. Form a chamber or a barrel [a region where an unfolded protein can move into and fold in isolation without interference] Example: tcip in cytosol, groel in bacteria or chloroplast, hsp 60 in mitochondria. 2 large subunits (groel) that are joined by their base. Top of each chamber are capped by groes.
