Lecture : Bio Notes 210 - Glutamic Acid

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azaillia

30 Mar 2023

School

UCF

Department

Biology

Course

BSC 2010C

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Document Summary

Glutamic acid is one of the 20 amino acids that make up proteins, and is classified as an acidic, polar amino acid due to the presence of a carboxyl (-cooh) group in its side chain. It is a non-essential amino acid, meaning that it can be synthesized in the body. Glutamic acid plays several important roles in the body. It is involved in the biosynthesis of other amino acids, including proline and arginine. It is also a key component of the neurotransmitter glutamate, which plays a crucial role in neural communication and the regulation of synaptic plasticity. In addition to its role in neurotransmission and amino acid biosynthesis, glutamic acid is important for maintaining acid-base balance in the body. It can act as a buffer, helping to maintain the ph of bodily fluids within a narrow range.

Related Questions

wild type e. coli can synthesize all 20 common amino acids, butsome mutants, called amino acid auxotrophs, are unable tosynthesize a specific amino acid and require its addition to theculture medium for optimal growth. Besides their role is proteinsythesis, some amino acids are also precursers for othernitrogenous cell products. COnsider the following amino acidauxotrophs that are unable to synthesize the identified amino acid.For each mutant, what nitrogenous products other than proteinswould the cell fail to syntehsize?

a. glycine

b. glutamine

c. aspartate

crimsonmammoth698

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

carminesea-lion900

Assuming that the mutations are adaptive, how would that affect the stability of a protein at low and high temperatures?

Given:

1) Glutamine to lysine in a warm adapted species.Glutamine is uncharged while lysine is positively charged, therefore there would likely be a change as an uncharged amino acid is being replaced with positively charged amino acid.

2) Threonine to Alanine in a warm adapted species. Threonine is polar uncharged while Alanine is hydrophobictherefore there would likely be a change, as a polar charged amino acid is being replaced with a hydrophobic amino acid.

3) Glutamic acid to aspartic acid in a cold adapted species. Both Aspartic acid to Glutamic acid are negatively charged, therefore, there would likely be no effect with this change as both are negatively charged amino acids.

4) Glycine to alanine in a warm adapted species. Both Glycine to Alanine are non polar amino acids, therefore the change would likely have no effect as both are non polar and hydrophobic.

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Lecture : Bio Notes 210 - Glutamic Acid

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