63) Why is the amino acid proline not commonly found in a-helices or B-sheets? I
ID: 277832 • Letter: 6
Question
63) Why is the amino acid proline not commonly found in a-helices or B-sheets? In what secondary structure might proline be commonly found? 64) Identify the four images below, which represent the four classes of protein structures commonly identified across MOST structures found in the Protein Data Bank. b. 65) In the famous experiment where Christian Anfinsen unfolded and refolded the protein RNaseA, in what order was the denaturant and reductant removed to give an inactive protein? Why was the protein inactive? 66) Would a nonsense mutation in a gene encoding a protein be expected to result in a gain-of-function or a loss-of-function protein folding disease?Explanation / Answer
Ans 63 :
The proline is unable to form the hydrogen bonding in the alph ahelix , so if it is present , it causes a kink in alpha helix and beta sheets. So it is not commonly found there.
It has a unusual shape so the side chain bonds to the protein backbone twice.
The cyclic structure of this amino acid proline is most suited for beta turn , so it is most commonly found in beta turns.
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