BIOLOGY 2B03 Lecture Notes - Lecture 2: Autoantibody, Prostate Cancer, Phosphoinositide 3-Kinase
4 May 2017
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Hydrophobic aggregates - you want a chaperone that fixes this - Need to give enough time for the protein to fold and be synthesized. Heat shock - discovered when cells were heated. Thought proteins just responded to heat - not the case. Also a similar one in the er - bip - grp78. Functions as a major quality control factory within the er. They all bind to the r group in the amino acids that are hydrophobic and prevent it from folding with a neighbouring molecule (forming aggregates). Chaperones prevent intermolecular interactions - binding prematurely to other proteins. Bip and hsp70 bind to the hydrophobic r goup of amino acids and prevent them from binding to other proteins prematurely - ensures that proper folding in proteins take place and no aggregates form. Nucleotide binding domain has atp - used to lock in the protein - with a co- chaperone. Needs hsp40/dnaj - factor to assist in binding.
