Question

3. The important function of molecular chaperones to A. move proteins from endoplasmic reticulum to the Golgi apparatus B. fold proteins into a native conformation C. add cofactors, coenzymes or prosthetic groups to proteins as they are synthesized D. assemble protein subunits into a quaternary structure E. transport proteins to either the plasma membrane or release them from cells to the extracellular space 4. Protein folding to a native conformation is highly dependent upon all of the following, except: A. the rotation about the peptide bond. D. the polar character of sequences of amino acids. B. The relative size of amino acid R-groups E. the rotation about the Ca-N bond. C. rotation about the Ca-C bond in the backbone.

Answer 1

3, option b- to fold proteins into a native confirmation.

Molecul chaperones are protein families which assist the proteins to fold in its correct native configuration and also unfold the proteins during any translocation. It prevents protein aggregation and aids in producing functional and productive proteins. Wherever in the cell, protein folding is required, different classes of chaperone proteins act there.

4, option-a rotation of the peptide bond

Rotation around the peptide bond is not possible due to its partial dounble bond strcture. Peptide bonds are resonance structures which has restricted rotation.

All the other options provided are factors that influence protein configuration. The bond between C alpha- C and C alpha-N are possible and the rotation angles are known by phi and psi greek letters respectively.

The side chain R group is very important because different amino acids have different side chains ranging from so simple in glycine whereas branched chain amino acid in valine, leucine,etc

Hydrophobicity is also another factor which determines the folding

Mostly hydrophobic are placed inside and hydrophilic outside.