Chapter 21: Q28P (page 1004)
Which bonds in the backbone of a peptide can rotate freely?
Short Answer

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Chapter 21: Q28P (page 1004)
Which bonds in the backbone of a peptide can rotate freely?

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In what order would histidine, serine, aspartate, and valine be eluted with a buffer of pH 4 from a columncontaining an anion-exchange resin (Dowex 1)?
Explain why the pI of lysine is the average of the pKa values of its two protonated amino groups.
What dipeptides would be formed by heating a mixture of valine and N- protected leucine?
Draw the product obtained when a lysine side chain in a polypeptide reacts with maleic anhydride.

Why are the carboxylic acid groups of the amino acids more acidic
(pKa ~ 2) than a carboxylic acid such as acetic acid (pKa = 4.76)?
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