Você está na página 1de 3

1.

How do D-amino acids differ from L-amino acids? What biological roles are played by peptides that contain D-amino acids?
Amino acids are designated L or D based on the direction on which they rotate polarized light. L-amino acids rotate polarized
light to the left (levo) while D-amino acids rotate polarized light to the right (dextro).
Peptides containing D-amino acids (or D-peptides) are less susceptible to degradation in the stomach or inside the cells. Thus,
they are usually useful and effective drugs for longer period of time.

2.

For each of the following, name an amino acid in which the R group contains it: a hydroxyl group, a sulfur atom, a second
chiral carbon atom, an amino group, an amide group, an acid group, an aromatic ring, and a branched side chain.
Amino acid with R (hydroxyl group) - threonine, serine, and tyrosine
Amino acid with R (sulfur atom) - cysteine, methionine
Amino acid with R (second chiral carbon atom) - isoleucine, threonine
Amino acid with R (amino group) - tryptophan, histidine, arginine, lysine, histidine
Amino acid with R (amide group) - asparagines, glutamine
Amino acid with R (an acid group) - aspartate, glutamate
Amino acid with R (aromatic ring) - phenylalanine, tryptophan, tyrosine
Amino acid with R (branched side chain) - valine, leucine, isoleucine

3.

Predict the predominant ionized forms of the following amino acids at pH 7: glutamic acid, leucine, threonine, histidine, and
arginine.
Glutamic acid glutamate
Histidine

Leucine

Arginine
Threonine

4.

Calculate the isoelectric point of each of the following amino acids: glutamic acid, serine, histidine, lysine, tyrosine, and
arginine.
Isoelectronic point or pI
pI = 1/2 (pK1 + pK2)

5.

Suggest a reason why amino acids are usually more soluble at pH extremes than they are at neutral pH.
Amino acids are more soluble at extreme pH because they react reversibly. Moreover, amino acids have -COOH group that
can donate H readily and -NH2 group that can attract H. Thus, they are amphoteric.

6.

Based on the pKa values of the amino acids, is there any amino acid that could serve as a buffer at pH 8? If so, which one?
Asparagine can be used as buffer at pH 8 based on its pKa2 value of 8.80 that is close enough to the desired pH.

7.

If you were to have a mythical amino acid based on glutamic acid, but one in which the hydrogen that is attached to the gcarbon were replaced by another amino group, what would be the predominant form of this amino acid at pH 4, 7, and 10, if
the pKa value were 10 for the unique amino group?

8.

Consider the peptides SerGluGlyHisAla and GlyHisAlaGluSer. How do these two peptides differ?
The two peptides have the same amino acid residues however they have different sequence. Thus, they are expected to have
different primary structure. Cleavage of peptide bonds using specific proteases will yield different residues.

9.

What is the stereochemical basis of the observation that D-aspartyl-D-phenylalanine has a bitter taste, whereas L-aspartyl-Lphenylalanine is significantly sweeter than sugar?
D-aspartyl-D-phenylalanine and L-aspartyl-L-phenylalanine differ on how they rotate polarized light. Moreover, chirality of
carbon centers in the two compounds also differs. Chirality played a major role on how taste receptors react with compounds
causing them to release different tastes. Thus, even though the compounds are mirror images, they have different taste.