How can we utilize the properties and bonding of atoms to further study human diseases in various tests? BY: HELENA HALL-THOMSEN & DEVYN HETU

Atomic Bonding & its Relation to Disease

Covalent Bonds

Natural covalent bonds not made in a lab can result in diseases if they are present in large quantities. Covalent bonds are the bonding of atoms by sharing electrons, and have a neutral charge; ionic bonds have positive and negative charges. By sharing electrons, atoms can achieve a full shell of valence electrons (8) to satisfy the octet rule. The octet rule is a standard chemical rule in which atoms typically combine in ways that satisfy the outer shell electrons, by sharing electrons in order to get eight. However, sometimes atoms are not always satisfied in a covalent bond if the share of electrons is unequal. This can lead to polar covalent bonds with positive and negative charges. Ionic bonds are less involved in diseases.

In this example, two oxygen atoms and one carbon atom establish a covalent bond. As you can see, the each atom is sharing two electrons so every atom has a full outer electron shell.

Proteins and Peptide Bonding

Proteins are organic compounds comprised of nitrogen, carbon, hydrogen, and oxygen. Within a protein is multiple chains of amino acids, the monosaccharides of proteins. The chains of amino acids or the polypeptide chain's sequencing is controlled by enzymes (type of protein) and other proteins known as chaperones. It is the enzymes' function to reorganize the covalent bonding between the atoms to assemble the order of amino acids. With diseases, mutations in the DNA can cause inaccuracy of modifying covalent bonds and amino acid sequencing when sent to the enzymes and chaperones in a cell. This leads to the misfolding of proteins as a whole. Proteins are used in the body to build and repair tissues; bones, muscles, and cartilage have proteins in them. Furthermore, proteins make enzymes, hormones, and other important bodily chemicals. When proteins are not folded correctly and the covalent bonds are not in the correct sequence diseases can form.

This illustrates an entire protein, which each little dot represents an amino acid. Each amino acid group is comprised of the R, carboxyl, and amino group. The R group is the only group in an amino acid that changes. Together these amino acids form the polypeptide chain.

Real World Examples: Cancer, Alzheimer's, Heart Disease


Cancer can be caused by a genetic mutation, often correlated with the misfolding of proteins. There is a variety of different mutations that lead to different cancers; genetic mutations lead to protein misfolding. When proteins are not correctly assembled in the endoplasmic reticulum stress increases within the cell. Homeostasis can no longer be maintained in the cell, and large groups of dysfunctioning cells can make tissues lose function. Cells that cannot fix their proteins will shut down and no longer work correctly. A specific example of cancer caused by incorrect sequencing of proteins would be breast cancer. Many women and sometimes men are born with a gene increases the likeliness of getting breast cancer. Cells with DNA to create proteins that do not work efficiently leads to the development of tumors within the breast as the cells are still identified as cells, but they are shut down.

The image above shows a malignant tumor formed within the breast tissue. Although small, the tumor will continue to grow if not treated because more cells will continue to lose function; other existing cancer cells will divide and multiply.

Alzheimer's Disease

Alzheimer's disease occurs when highly soluble neuronal proteins folding incorrectly with the covalent bonding and other properties of amino acid sequencing. Without correctly functioning neuronal proteins, individuals diagnosed with Alzheimer's forget important details in regards to their own life. As more cells reproduce with binary fission more and more cells within the brain do not work properly to maintain homeostasis and memory function.

In a brain with Alzheimer's certain cells of the brain multiply that do not function properly and shrink out other important components needed for the human brain to work.

Heart Disease

Heart Disease coincides with the personal choice of eating mass quantities of fatty foods as well genetic predisposition. Due to the fact that covalent bonds can be made in a variety of different ways its possible to make many different types of molecules. These covalent bonds can be formed naturally in living organisms within their cellular structure. One example that agrees with a cause of heart diseases would be cholesterol, which is a leading factor in heart disease.

(C27H46O) or cholesterol is shown here, cholesterol is a leading factor in heart disease. If present in large quantities cholesterol can be very harmful to the human body especially the heart.
This shows various neurological diseases that are caused by protein misfolding. Most of the following diseases end lead to neurodegeneration.

Statistics/ Quantitative Data

Amounts Spent Yearly on Research (U.S.) Approx

Diseases caused by proteins not folded correctly require lots of research and are some of the most damaging ones to the human body.

Amounts of New Cases Each Yeah (U.S) Approx

tests for diseases w/ covalent bonding and protein folding

Using Yeast to Further Examine Proteins

Examining yeast cells can help understand neurodegenerative diseases caused by the misfolding of proteins such as Alzheimer's or Parkinson's. Yeast is highly available and cheap to buy in large quantities, and it can be easily genetically mutated. Different genomes and genetic mutations can be applied to different groups of yeasts to compare. By doing so, scientists can look at different parts of the yeast cell as it is easy to examine. They can view the endoplasmic reticulum, Golgi apparatus, ribosomes, and nucleus to see the manufacturing of proteins in instances of mutated DNA. Viewing yeast although not quite alike a human brain cell can help people understand how the process of proteins is made when mutations are present; yeast provides a more close up and direct examination.

As shown in the diagram yeast contains the same organelles used to make cells that human brain cells have. The nucleus, Golgi apparatus, ribosomes, and endoplasmic reticulum can all be observed when genetic mutations are present.

Heat Shock

Although heat shock therapy is more of a treatment for cancer, it can still be observed to observe the cancer cells. By heating up the protein cells within cancer tumors, some of the cells can be destroyed. Scientists are able to observe how different cancer cells with incorrect protein folding within the endoplasmic reticulum react to different therapies to exterminate them.

Heat shock therapy as shown above kills and dismantles the dysfunctional proteins in cancer cells, which can help heal it.

Work Cited:

"Structure and Bonding in Chemistry." Structure and Bonding: Covalent Bonds. N.p., n.d. Web. 08 Dec. 2016.

Selkoe, Dennis J. "Cell Biology of Protein Misfolding: The Examples of Alzheimer's and Parkinson's Diseases." Macmillan Publishers,2004,N.p, n.d. Web.08 Dec.2016.

Cooper, Geoffrey M. "Protein Folding and Processing." The Cell: A Molecular Approach. 2nd Edition. U.S. National Library of Medicine, 01 Jan. 1970. Web. 08 Dec. 2016.

Kain, Kristin. "Using Yeast to Understand Protein Folding Diseases: An Interview with Susan Lindquist." Disease Models & Mechanisms. The Company of Biologists Ltd, 2008. Web. 08 Dec. 2016.

Pattison, J. Scott, and Jeffrey Robbins. "Protein Misfolding and Cardiac Disease: Establishing Cause and Effect." Autophagy. U.S. National Library of Medicine, 2008. Web. 08 Dec. 2016.

Reid, T.R. "Alzheimers Research Funding Lags Other Diseases- Dementia - AARP." AARP. N.p., n.d. Web. 08 Dec. 2016.

"Budget and Appropriations." National Cancer Institute. N.p., n.d. Web. 08 Dec. 2016.

"Alzheimer's Association - Boomer Report." Alzheimer's Association. N.p., n.d. Web. 08 Dec. 2016.

"Cancer Facts & Figures 2016." Cancer Facts & Figures 2016 | American Cancer Society. N.p., n.d. Web. 08 Dec. 2016.

"Heart Disease Facts." Centers for Disease Control and Prevention. Centers for Disease Control and Prevention, 10 Aug. 2015. Web. 08 Dec. 2016.

"Facts and Figures | Alzheimer's Association." Facts and Figures | Alzheimer's Association. N.p., n.d. Web. 08 Dec. 2016.

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