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Chapter 29: Q35P (page 1192)

What is the structure of each amino acid at its isoelectric point: (a) alanine (b) methionine; (c)aspartic acid; (d) lysine?

Short Answer

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Amino acids constitute primary importance as they carry out several functions. Numerous amino acids are present; however, the proteins are created from twenty amino acids.

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01

Step 1:Amino acid

Amino acids constitute primary importance as they carry out several functions. Numerous amino acids are present; however, the proteins are created from twenty amino acids.

02

Isoelectric point

The isoelectric point indicated as pI, impacts the solubility of a specific molecule at a particular pH. Proteins comprise a net positive charge at a pH less than pI. A net negative charge is present at a pH larger than pI.

03

Structure of each amino acid at the isoelectric point

The amino acid is found as a zwitterion at the isoelectric point. At the isoelectric point, the deprotonation of and the protonation of takes place.

(a)The structure of the amino acid, alanine at its isoelectric point can be given as:

(b)The structure of the amino acid, methionine at its isoelectric point can be given as:

(c)The structure of the amino acid, aspartic acid at its isoelectric point can be given as:

(d)The structure of the amino acid, lysine at its isoelectric point can be given as:

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Most popular questions from this chapter

Consider two molecules of a tetrapeptide composed of only alanine residues. Draw the hydrogen bonding interactions that result when these two peptides adopt a parallel 尾-pleated sheet arrangement. Answer this same question for the antiparallel 尾-pleated sheet arrangement.

Explain why the pKaof the -NH3+group of an 伪-amino acid is lower than the pKaof the ammonium ion derived from a 1掳amine (RNH3+). For example, pKaof the -NH3+group of alanine is 9.87 but the pKaof CH3NH3+is 10.63.

Deduce the sequence of a heptapeptide that contains the amino acids Ala, Arg, Glu, Gly, Leu, Phe, and Ser, from the following experimental data. Edman degradation cleaves Leu from the heptapeptide, and carboxypeptidase forms Glu and a hexapeptide. Treatment of the heptapeptide with chymotrypsin forms a hexapeptide and a single amino acid. Treatment of the heptapeptide with trypsin forms a pentapeptide and a dipeptide. Partial hydrolysis forms Glu, Leu, Phe, and the tripeptidesGly鈥揂la鈥揝er and Ala鈥揝er鈥揂rg

Draw the organic products formed in each reaction.

a.

b.

c.

d.

e.

f.

What is the predominant form of each of the following amino acids at pH=11? What is the overall charge on the amino acid? (a)valine; (b)proline; (c)glutamic acid; (d)lysine?
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