Chapter 21: Q13P (page 996)
a. What percentage of the -amino group of lysine will be protonated at its pI?<25%50% >75%
b. Answer the same question for the-amino group of lysine.
Short Answer
- >75%
- >75%
Chapter 21: Q13P (page 996)
a. What percentage of the -amino group of lysine will be protonated at its pI?<25%50% >75%
b. Answer the same question for the-amino group of lysine.
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Get started for freeQuestion: In determining the primary structure of insulin, what would lead you to conclude that insulin had more than one polypeptide chain?
alpha- Amino acids can be prepared by treating an aldehyde with ammonia/trace acid, followed by hydrogen cyanide, followed by acid-catalyzed hydrolysis.
a. Draw the structures of the two intermediates formed in this reaction.
b. What amino acid is formed when the aldehyde that is used is 3-methylbutanal?
c. What aldehyde is needed to prepare isoleucine?
a.Which amino acid has the lowest pI value?
b.Which amino acid has the highest pI value?
c.Which amino acid has the greatest amount of negative charge at pH = 6.20?
d.Which amino acid has a greater negative charge at pH = 6.20, glycine or methionine?
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)?
a. Which isomer—(R)-alanine or (S)-alanine—is d-alanine?
b. Which isomer—(R)-aspartate or (S)-aspartate—is d-aspartate?
c. Can a general statement be made relating R and S to d and l?
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