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Which of the following amino acids can be used in place of lysine, arginine, and histidine to remove the electrostatic charge but retain the hydrophilic nature of the side chain?

Which of the following amino acids can be used in place of lysine, arginine, and histidine to remove the electrostatic charge but retain the hydrophilic nature of the side chain? Correct Answer Asparagine and glutamine

Asparagine and glutamine can be used in place of lysine, arginine, and histidine to remove the electrostatic charge but retain the hydrophilic nature of the side chain. Aspartic acid and glutamic acid cannot be used in place of lysine, arginine, and histidine to remove the electrostatic charge and retain the hydrophilic nature of the side chain. Asparagine and glutamine contain neutral but polar side chains.

Related Questions

Consider the following statements regarding genetic code and choose the correct answer:
1. The genetic code is degenerate
2. In all amino acids the first two bases are the same in all the codons that represent a particular amino acid
3. The number of codons an amino acid can claim is proportional to the frequency of the amino acid in proteins
4. Amino acids with codons ending in U or A also have codons ending in C or G respectively
Mineral acids are stronger acids than carboxylic acids because (i) Mineral acids are completely ionised. (ii) Carboxylic acids are completely ionised. (iii) Mineral acids are partially ionised. (iv) Carboxylic acids are partially ionised.
Lysine is being produced in a lab-scale reactor by a threonine auxotroph. After 2 weeks of operation it was observed that the concentration of lysine in the reactor was gradually decreasing. Microbiological assays of reactor samples showed absence of contamination and recorded data showed no change in the operating conditions. The most probable reason for decrease in lysine concentration may be attributed to
Analysis of a hexapeptide using enzymatic cleavage reveals the following result:
• Amino acid composition of the peptide is: 2R, A, V, S, Y
• Trypsin digestion yields two fragments and the compositions are: (R, A, V) and (R, S, Y)
• Chymotrypsin digestion yields two fragments and the compositions are: (A, R, V, Y) and (R, S)
• Digestion with carboxypeptidase A yields no cleavage product.
Given: Trypsin cleaves at carboxyl side of R. Chymotrypsin cleaves at carboxyl side of Y. Carboxypeptidase A cleaves at amino side of the C-terminal amino acid (except R and K) of the peptide.
The correct amino acid sequence of the peptide is:
In a substrate X catabolic gene promoter you replace the normal histones by your experimental histones – ones with arginine side chains in place of histidine. What will be the effect on the concentration of substrate X against the control?
Human insulin molecule is composed ofone α-chain having 21 amino acids andone β-chain having 30 amino acids. How many functional insulin genes occur in adult humans?
Which of the following statements are true in case of fluid-mosaic model for cell membrances
P. Between 5 - 8 nm thick and appear trilaminar when viewed in cross-section under electron microscope
Q. Less than 1 nm thick and consist of a layer of protein sandwitched between two layers of phospholipids
R. In the lipid bilayer, proteins are embedded at irregular intervals and held by hydrophilic interactions between lipids and hydrophilic domains of the proteins
S. The protein domains exposed on one side of the lipid bilayer are different from those exposed on the other side
Often, protein to be expressed is fused with histidine and it is called as histidine tags. For their purification, matrix containing ______ is used.
The common amino acids are also called as alpha-amino acids because they contain their amino group attached to the alpha carbon.
You design a plasmid with a gene for Histidine synthesis and a fragment containing ARS. You introduce it yeast culture and try to grow then in Histidine deficit media. What will be your observation?