Folding Overview required for a protein to achieve a proper tertiary protein structure involves heat shock proteins (Hsp) essential for normal protein folding some function as chaperones and some function as chaperonins the more mutated a protein, the more help it needs from chaperones if a protein is not folding properly, a chaperone may send it directly for degradation clinical relevance cystic fibrosis login to view 12 more bullets Chaperones types Hsp70 login to view 4 more bullets Hsp90 login to view 4 more bullets Chaperonins group 1 Hsp60 login to view 5 more bullets group 2 TRiC/CCT login to view 3 more bullets Degradation Ubiquitination cell's mechanism to mark a protein for destruction mechanism several copies of ubiquitin added to a misfolded/unneeded protein polyubiquitinated protein enters the proteasome protein hydrolyzed into peptide fragments Defects in destruction of misfolded proteins inability to send degraded proteins to proteasome results in accumulation in ER examples α1-antitrypsin (AAT) deficiency login to view 11 more bullets