Functional Protein and Genes 1

Functional Proteins and Genes

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Quiz 1
 Functional Protein and Genes 2

Glutamate dehydrogenase
Proteins are structures that are related to genes. Genes are made of Amino Acids hence
now the effects of these Amino Acids are evident in proteins. They influence the protein nature
and composition. For the human bodys physiological processes to go on well, they are very
essential. There are different types of proteins, including the enzyme. Enzymes play a critical
role of being a promoter in the biological reactions. The relationship between Amino Acids and
proteins has been discovered through mass spectrometry, where the study of the sequence is done
by scientists. (Chauhan et al., 2014, p.90).
Quiz 2
Function of glutamate dehydrogenase to the body.
Glutamate hydrogenase is abundant in the liver, kidney, brain and pancreas of a mammal.
The chief importance of the latter is catalyzing the revocable of the conversion of glutamate to
keroglutarate ant to ammonia and the vice versa of the process. The glutamate dehydrogenation
response takes place in the liver that seems to be next to the equilibrium if the suitable ratio of
ammonia and amino acid for urea fusion in the perioral hepatocytes (Chung Dick and Lee, 2013,
p.87). Nitrogen, nitric and nitrates are represented by nitrogen fixation and floras confirmed as
the protein in our nutrition, glutamate shows the vital role in mammalian nitrogen tide that act as
the nitrogen helper and nitrogen acceptor (Hric et al., 2017, p.72). The decreased nitrogen goes
to the humanoid body as free amino acid, proteins, amino formed via intestinal zone
microorganism, with the help of two enzymes that is glutamate dehydrogenase and glutamate
syntheses change of amino into amino acid.
Quiz 3

Structures of glutamate dehydrogenase

Among the structures of the proteins, they are grouped into two that is;
Primary structures
They are made of polypeptides chains that are the combination of amino acids and
peptides link. The uniqueness arrangement of amino acids that constitutes proteins or
polypeptides referred to as primary structure (Kara et al., 2015, P. 27).
Secondary structure
Immediately after the synthesis, polypeptides chains are folded and gathered into several
designs. Examples include Alpha Helices and Beta Pleated Sheets. It is connected by hydrogen
bonds.
3D structure
The last 3D structures of a protein are its tertiary structure, which retains to the
determinations of the secondary structure. Generally, it involves winding and tackling. It
gathered by different bond including Disulphide Bonds- formed when Cysteine amino acid s are
discovered, a strong double bond(S=S) formed between Sulphur within Cysteine monomers
(Papanikolaou et al., 2015).
 Functional Protein and Genes 3

Ionic Bond-when two oppositely charged R groups are located next to each other amid
them. Hydrogen Bond- its ones characteristics in daily Hydrogen bond, Hydrophobic and
Hydrophilic Interaction- some of the amino acids are hydrophilic while some are hydrophobic.
There are three isoform of glutamate dehydrogenase. This is a form catalases glutamate
to blend after 2-oxoglutamate and ammonium consuming NAD (P) H. Ammonia absorption
stands for critical aimed at vegetation progress.
Quiz 4
Features of glutamate dehydrogenase proteins structure in adult hemoglobin?
Hemoglobin is the iron containing oxygen transport that makes the red blood cells of all
the vertebrates in exclusion of the fish families, with the help of blood the hemoglobin transports
oxygen from the breathing system the whole body tissues where it discharges oxygen to allow
aerobic respiration to deliver vigor to control the task of the creatures through metabolism (Wang
et al., 2013, P.52).
Quiz 5
How sensitive is glutamate dehydrogenase when denatured by heat?
The action of denaturing is when proteins or nucleic acid tend to lose their tertiary
structures and secondary subordinate by the submission of exterior force or compound or health.
Usually thermophilic protein gets denatured by heat that is of high temperatures when compared
to the regular mesophilic proteins. Most of the analysis gives the chance of knowing the source
of stableness for proteins under specified high temperature.

References
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Chauhan, R.S., Chanumolu, S.K., Rout, C. and Shrivastava, R., 2014. Can mycobacterial
genomics generate novel targets as speed-breakers against the race for drug resistance.
Current pharmaceutical design, 20(27), pp.4319-4345.
Chung, B.K.S., Dick, T. and Lee, D.Y., 2013. In silico analyses for the discovery of tuberculosis
drug targets. Journal of Antimicrobial chemotherapy, 68(12), pp.2701-2709.
Hric, D., Kaski, K. and Kivel, M., 2017. Stochastic Block Model Reveals the Map of Citation
Patterns and Their Evolution in Time. arXiv preprint arXiv:1705.00018.
Kara, A., Vickers, M., Swain, M., Whitworth, D.E. and Fernandez-Fuentes, N., 2015. Genome-
wide prediction of prokaryotic two-component system networks using a sequence-based
meta-predictor. BMC bioinformatics, 16(1), p.297.
Papanikolaou, N., Pavlopoulos, G.A., Theodosiou, T. and Iliopoulos, I., 2015. Proteinprotein
interaction predictions using text mining methods. Methods, 74, pp.47-53.
Wang, H., Huang, H., Ding, C. and Nie, F., 2013. Predicting proteinprotein interactions from
multimodal biological data sources via nonnegative matrix tri-factorization. Journal of
Computational Biology, 20(4), pp.344-358.