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1What is a molecular chaperone?- large and diverse group of proteins that assist the folding/unfolding and the assembly/disassembly of other macromolecular structures
-They are not permanent components of the folded structures.
2What leads to complex folding pathways?Inappropriate amino acid interactions that are irreversible (especially hydrophobic). Complex folding pathway.
Slow kinetic factors (proline isomerization).
Peptidyl-Prolyl Isomerase. Take to long!
Some proteins need covalent modifications to fold: Glycosylation, disulphide bonds etc. Help direct them to the correct folding pathway
During folding some residues may make stable interactions that are not part of the native structure. They might be said to have complex folding pathways that can lead to stable energetic minima for particular non-native states. Often these interactions are hydrophobic in nature. These must be avoided or disrupted once formed. Chaperones do both these functions.
Slow kinetic factors may limit the speed and success of folding. Chaperones can speed these slow processes.
Some protein need covalent modification to go on to fold correctly. Glycosylation of polyepetides in the ER is an example of this. Without these modifications direction down the correct folding pathway fails to occur.
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