6 (5 of 20) The more we learn about protein folding the more we understand that

Question

6 (5 of 20) The more we learn about protein folding the more we understand that the process is the result of the minimization of free energy and the final structure will sit in a thermodynamic well as seen in protein folding funnels. Considering this process which of the following statements is true? O The depth of the well is determined solely by entropic contributions resulting from the formation of the hydrophobic core. O The final native structure represents the absolute lowest free energy value the peptide chain can achieve in all conditions Disulfide bonds are a stabilizing force in all protein structures. O The unfavorable entropic cost of forming the native conformation is offset by the favorable entropic increase of the solvent upon formation of the hydrophobic core. ONone of the above statements are true

Explanation / Answer

Ans.5. The final native structure represents the absolute lowest free energy value the peptide chain can achieve in all conditions.

Ans. 6. All atoms within a protein excluding - A. Peptide backbone

those those found in the side chains

Holds amino acids together in a protein - B. peptide bond

One atomic mass unit - F. Dalton

Allows for ideal hydrogen bonding geometry - C. Anitparallel strands

Between backbones within adjacent beta

Strands

Precludes the formation of ideal hydrogen - G. Parallel beta sheet

bonding geometry between backbones

Within adjacent beta strands

The heme group is an example of this - E. Prosthetic group

A protein that is soluble in the aqueous - D. Globular protein

Enviroments of the cell.

Ans.7. Option 2 is correct. N-alpha-C-alpha-C-N-alpha-C-alpha-C

Ans.8. Atleast two dihedral angles are available for each alpha carbon except C-N bonding. These two angles are phi and psi but their rotation is fixed. Cis and trans geometric isomer is posaible in proline residue in peptide bond.

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