Biological Foundations

Part A- Carbohydrates

  1. The monosaccharides represent the simplest types of sugar that contain three carbon atoms, oxygen, and hydrogen atoms in a similar ratio (BeMiller, 2018). Fructose is found in trees, vine fruits, flowers, honey, and coretubers. Moreover, it can be imitated from honeyplants, sugarcane, and maize.
  2. Roughagecomprises about 30% of the plant cell wall and is a structural polysaccharide. Some of its functions include gesticulating cells to nurture and split the connection of cells to form tissues. Finally, it controls the shape of the plant cell. Cellobiose is the building block of cellulose and contains two glucose units.
  3. Starch is made up of two molecules, while glycogen is made up of a single molecule (Foley et al., 2015). Glycogen is produced by animals, while plants produce starch. Starch has both branched and chain components, while glycogen has a branched component. On the other hand, both are polymers of glucose. Both are storage forms for energy.
  4. Examples of three disaccharides and their components are Lactose (milk sugar), Sucrose (beat sugar, beetroot sugar, desk sugar), and Maltose (malt sugar). Lactose originate in breast milk, Maltose is found in chocolate, and Sucrose is found in sugar cane.
  5. Lactose intolerance is the inability of the body to digest lactose. When an individual eats food containing Lactose, the lactase enzyme found in the small intestine breaks it down into smaller sugar forms. I.e., galactose and glucose.

Part B- Lipids

  1. An essential fatty acid is the one that the human body cannot synthesize (Lee et al., 2016). Fatty acid includes alpha-linolenic acid and linoleic acid.
  2. It is heavy glucose than polysaccharides as it is stored as fat droplets in large amounts. It is a better energy storage source as it produces a double amount of energy produced by polysaccharides. The lipoprotein lipase enzyme is responsible for the breaking down of triglycerides in the blood.
  3. Three types of lipids include sterols, phospholipids, and triacylglycerol. Fats are indispensable for constructing the defensiveobstruction/casing around the human body cells. Sterols are required for the synthesis of sex hormones.Triacylglycerol controls and regulates the internal body climate, maintaining a constant temperature.
  4. The cell membrane is made up of a Phospholipid bilayer with attached proteins. It contains the plasma membrane, which is selectively permeable to ions and organic molecules, and it also regulates the movement of nutrients in and out of the body cells. The cell membrane's primary role is to form the permeability plasma membrane of the cell and subcellular organelles in the form of a lipid bilayer. The proteins are responsible for repairing and building body tissues, allowing the metabolic reactions to occur, and coordinating body functions (Hull, 2020).

Part C- Proteins

  1. Hemoglobin protein is used for the transportation and storage of nutrients in the body. Actin is another protein that is responsible for the growth and maintenance of the body tissues and structure. Amylase is another example of a protein which is a digestive enzyme in the body. Lastly, proteins are required for the maintenance of proper PH.
  2. Glutathione is made up of three amino acids that include glutamic, cysteine, and glycine. These components are mostly present in mammalian tissue. It acts as an antioxidant, also a detoxifying, and a free radical scavenger. According to Newton (2017), Glutathione's main function is preventing harm to important cellular strandsinstigated by responsive oxygen types like bleaches, free fanatics, fatbleaches, and substantial metals.
  3. The four common ranks of enzymeorganization are primary, secondary, tertiary, and quaternary. The primary level represents the categorization of amino acids, which comprise the polypeptide chain. There are many amino acids which comprise of 20 different amino acids in the protein structure. The sequence of the amino acid chain starts with an amino acid monomer to peptide linkage. On the other hand, the secondary level of protein represents the regular and repetitive folding of the enzymebackbone. There are two common foldaway patterns include beta-sheet and alpha-helix: for alpha spiral, the polypeptide spine coils around an imaginary spiralalignment in a right-handed direction. Next is the tertiary protein level, which refersto ageneralportable of the entire polypeptide sequence into a specific 3D shape. It is usually a compact, global shaped enzyme structure. Lastly, quaternary is comprised of more than one polypeptide chain. It also describes how the different subunits are crowded together to form the overall protein structure. E.g., the human hemoglobin molecule serves as a good example for a four subunits protein structure.
  4. In most circumstances, tertiary and secondary structure levels are altered when a protein is denatured (Heidari et al., 2018). When the two-level structures are affected, the whole protein functions can no longer be performed.
  5. Enzymes are well known as biological molecules (proteins) responsible for speeding up the rate of invisible chemical reactions that occur within human body cells. Amylase is an example of a digestive enzyme responsible for breaking down starch molecules into smaller sugar molecules. Lipoprotein lipase enzyme is responsible for the breaking down of triglycerides in the blood. The lactase enzyme found in the small intestine breaks it down into smaller sugar forms—I.e. galactose and glucose.

Part D- Nucleic Acids/cells/transport

  1. DNA (d- ribose, D- Deoxyribose), RNA (Uracil)&RNA (adenine, cytosine, Thymine)
  2. a.) the main function of DNA molecule in the cell of a human body is the permanent storage of information (Zhang et al., 2020). It is mostly compared to a blueprint, as it carries the steps to create other components of the body cells like RNA molecules and proteins.

b.) DNA replication is a four steps process that involves the creation of matchinggenetic materialspirals from a single double-stranded chromosomeparticle. The first step represents the replication fork formation, where the DNA four bases form pair between the two strands. The DNA helices then interrupt the hydrogen attachment between vilecouples to distinct the components into a Y-shaped, called the duplicationsplit. The second step is where the replication begins. It starts from a primer building where the enzyme DNA primase generates the primers. When the primer is generated, it binds to the 3' end of the components separated in the first step. From there, the process proceeds to DNA replication elongation, which is step three. This is a process to create a new strand through the help of the DNA polymerases enzyme. It is the main enzyme responsible for creating new strands, while the other enzymes are accountable for the inspectionof errors and restoration processes. Thegene polymerases enzyme then binds to the components at the site of the primer and start adding fresh base pairs complementary to the component during the real replication. The cover component is formed and starts replication through binding with multiple primers. Termination is the fourth and last step of the DNA replication process. It takes place after both unremitting and intermittentcomponents are completely shaped. The exonuclease enzyme then eliminates all ribonucleic acid primers from the uniquecomponents. Next, the removed primers are substituted with suitablecenters.

  1. Facilitated diffusion refers to a molecule's movement from the point of high concentration to the point of lower concentration with the assistance of a protein channel. On the other hand, active transport is the movement of molecules from points of low concentration to points of higher concentration. Simple diffusion is similar to facilitated diffusion. However, the substances with polar molecules in simple diffusion cannot fit between the phospholipids.
  2. Ribosomes are involved actively in the protein synthesis and translation of mRNAs. Lissome is mainly involved in intracellular digestion. Nucleus, on the other hand, is mainly involved in the direct synthesis of proteins and ribosome.

Reference for Glutathione in Prokaryotes

BeMiller, J. N. (2018). Carbohydrate chemistry for food scientists. Elsevier.

Cockburn, D. W., Orlovsky, N. I., Foley, M. H., Kwiatkowski, K. J., Bahr, C. M., Maynard, M., ... & Koropatkin, N. M. (2015). Molecular details of a starch utilization pathway in the human gut symbiont E ubacterium rectale. Molecular microbiology95(2), 209-230.

Cohen, B. J., & Hull, K. L. (2020). Memmler's Structure & Function of the Human Body. Jones & Bartlett Learning.

Heidari, S., Hemmateenejad, B., Yousefinejad, S., & Moosavi-Movahedi, A. A. (2018). Excitation-emission matrix fluorescence spectroscopy combined with three-way chemometrics analysis to follow denatured states of secondary structure of bovine serum albumin. Journal of Luminescence203, 90-99.

Lee, J. M., Lee, H., Kang, S., & Park, W. J. (2016). Fatty acid desaturases, polyunsaturated fatty acid regulation, and biotechnological advances. Nutrients8(1), 23.

Newton, G. L., & Fahey, R. C. (2017). Glutathione in prokaryotes. In Glutathione (1990) (pp. 69-78). CRC Press.

Zhang, J., Li, J., Zhu, Y., Miao, Z., & Tian, Y. (2020). Forced running exercise mitigates radiation-induced cognitive deficits via regulated DNA hydroxymethylation. Epigenomics12(5), 385-396.

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