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You are replacing different amino acids of a protien to testpredictions about which residues are essential for the protien'sfunction. Which of each pair of amino acid substitutions belowwould you expect to disrupt protien structure the most? justifyyour answer.

a) Valine replaced by Alanine or by Phennylalanine

b) Lysine replaced by Aspartic acid or by Arginine

c) Glutamine replaced by Glutamic acid or by Asparagine

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Lelia Lubowitz
Lelia LubowitzLv2
29 Sep 2019

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Related questions

Type molecular weight Number in lysozyme

Alanine 89 12

Arginine 174 11

Asparagine 132 13

Aspartic acid 133 8

Cysteine 121 8

Glutamic acid 147 2

Glutamine 146 3

Glycine 75 12

Histidine 155 1

Isoleucine 131 6

Leucine 131 8

Lysine 146 6

Methionine 149 2

Phenylalanine 165 3

Proline 115 2

Serine 105 10

Threonine 119 7

Tryptophan 204 6

Tyrosine 181 3

Valine 117 6

1. The sequence of amino acids of the enzyme lysozyme is known. Below is a list of amino acids

and the number of each in the lysozyme molecule

Questions:

a. What is the average molecular weight of the 20 amino acids?

b. What is the molecular weight of lysozyme?

c. What is the average molecular weight of the amino acids in lysozome?

d. How many S-S bonds are possible in lysozyme?

(hint: look at the structures of each amino acid, and figure out which of these have sulphurs

that are FREE to form bonds).

e. Is the net charge on lysozyme positive or negative?

You are studying a protein that you call Protein X. There is an aspartic acid at a key position in Protein X that is important in the folding and stabilization of that protein. If this aspartic acid is changed to a different amino acid, which one of the following amino acid substitutions is MOST likely to allow the protein to fold normally?

threonine

arginine

serine

glycine

glutamic acid

1.You are studying the world’s smallest enzyme which has the amino acid sequence of:

Met Ala Ser Met Tyr Ala Glu

You know that activity of this enzyme requires phosphorylation. You wish to design an inactive mutant form of this enzyme that can never be phosphorylated. You will use site-directed mutagenesis to alter the DNA sequence of this protein, resulting in a mutant protein.

Additional information: The most common resides to be phosphorylates are serine, threonine and tyrosine. In theory, these can be replaced with any other amino acid except for glutamic and aspartic acid, the shape and charge of a phosphorylated serine and aspartic acid are similar. Substitution with one of these amino acids would create a protein that looked like it was always phosphorylated (phosphomimic). Alanine is one of the most common substitutions, but others are possible and sometimes preferable to preserve other characteristics of the amino acid.

1. Write out the resulting amino acid sequence corresponding to your designed mutant protein here:

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