One of these proteins has an unusual N-terminal ADP/ATP binding pocket that is targeted by geldanamycin. Another class of these proteins binds RpL23, contains a PPIase (“P-P-I-ace”) “head” domain, and are called trigger factors. GrpE (“grip-E”) and J-domain proteins augment the ATPase activity of some of these proteins. One of these proteins dissociates from ATF6, PERK, and IRE1 in a response pathway that usually triggers ERAD (“E-rad”). That one of these proteins is BiP. The eukaryotic TRiC and the prokaryotic GroEL-GroES (“grow-E-L-grow-E-S”) complexes comprise the HSP60 family of these proteins, which are upregulated in response to heat shock. These proteins facilitate hydrophobic collapse, which allows their “clients” to achieve proper tertiary structures. For 10 points, name these proteins that mediate folding of peptides. ■END■
ANSWER: molecular chaperones [accept chaperonins or Cpns or Cpn60; accept heat shock proteins or HSPs or HSP40 or HSP60 or HSP70 or HSP90 until “HSP60” is read; accept binding immunoglobulin protein or BiP until read; prompt on heat shock proteins after “HSP60 is read]
<UCF A, Biology>
= Average correct buzz position