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BIOC212 Mid Term Review.doc

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Anatomy & Cell Biology
ANAT 261
Jason Young

Midterm ReviewReview QuestionsProtein Folding Review QuestionsA mutation in a cytosolic protein from F to C results in a protein that does not fold correctly Why decrease hydrophobicity results in core of protein not established and thus destabilized structureNo sulphide bond formation in cytosol reducingLoss of F disrupts binding of proteins with partner and thus disrupts quaternary structure Less suitable substrate for chaperonesF is key binding residue for hydrophobic ligand thats required for foldingProtein able to form nonspecific interactions between the C and cellular components These impede proper foldingDifferentiate between the 3 chaperone families all are ATP dependent use to control substrate binding and releaseATPbound states bind substrate for Hsp70 but not Hsp60 or 90All target hydrophobic residuesOnly Hsp70s require cochaperonesTargets Hsp70versatile short stretches and unfolded proteins Hsp90 proteins closer to native state Hsp60 can only target small proteins usually nearer to the native stateUses Hsp70 used to fold newly synthesized proteins and proteins being translocated to the ER and
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