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Biochemistry Task 2

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BIOCHEMISTRY TASK 2

Running head: BIOCHEMISTRY TASK 2 1
A.

BIOCHEMISTRY TASK 2 2
B.

BIOCHEMISTRY TASK 2 3
C.

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D.

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E.
The four forces that stabilize a protein’s structure at the tertiary level are as followed:
Hydrophobic is the interaction between nonpolar amino acids (Borges, 2014). These amino acids are not capable of hydrogen bonding, however their hydrocarbon regions interact closely by pulling together tightly tucking away from the exterior of the cell (Borges, 2014). This is the weakest of bonds (Borges, 2014). Next, Hydrogen bonds are polar or charged amino acids
(Borges, 2014). This is where one amino acid is sharing its hydrogen atom with another oxygen atom (Borges, 2014). This is a stronger bond than hydrophobic interaction but still weak
(Borges, 2014). The third bond is called Ionic Bond. This is when you have charged amino acids, opposites attracting one another (Borges, 2014). Ionic bond is stronger than a hydrogen bond but not as strong as a polypeptide bond (Borges, 2014). The final bond is a Disulfide bond.
The disulfide bonds are only formed between two Cysteine amino acids that are brought together to form a Sulfa­Sulfa bridge (Borges, 2014). This bond is a strong interaction and is a covalent like bond to hold peptide chains together (Borges, 2014). With all these bonds and interactions together they help stabilize the proteins at the tertiary level and form its shape.

BIOCHEMISTRY TASK 2 6
F.
Bovine spongiform encephalopathy (BSE) occurs at a molecular level by a type of misfolded proteins called prion. Prions are malformed proteins not capable of reproducing or making copies of themselves ("Biology, Eighth Edition (Raven)"). There are two forms of prions, harmless and harmful (Wolfe, 2000). If the cow is fed contaminated feed which includes infectious sheep brain, the harmless prions become infectious prions (Wolfe, 2000). The harmful protein (PrPsc) comes in contact with the PrPc around the neurons of the brain and therefore binds to the normal cell induces the cell to fold into an abnormal conformation converting the
PrPc to PrPsc ("Biology, Eighth Edition (Raven)"). With improper folding of the brain protein
PrPc the misfolded protein leads to disease. The harmful protein aggregates of prions to form a plaque that surrounds the neuron and also influences nearby neurons to aggregate and leads to cell death, death leads to little “holes” in the brain giving it a spongy look (Thompson, 2014).
The Chaperone provides and promotes a young protein to take on a proper fold and shape conformation, it is the protector of the young protein (Thompson, 2014). A Chaperone can contribute to BSE by binding with the abnormal prion and influence other proteins to change conformation (Thompson, 2014).
Countries without regulations in place can decrease the risk of transmitting the prion involved in BSE by not feeding cattle remnants of other animals, also called meat and bone meal
(Food and Agriculture Organization, 2001). These countries can feed animals vegetable proteins resources instead (FOA, 2001). Another way is to dispose of carcasses with BSE properly best by incineration. Incineration is a valuable process for it’s ability to stabilize and

BIOCHEMISTRY TASK 2 7
F. (continue) eliminate hazardous material, according to Franco (2002). By doing these, the countries will be able to decrease the spread of BSE.

BIOCHEMISTRY TASK 2 8 References Wolfe, George (2000). Thinkwell Biochemistry sections 2.7.3 Primary and Secondary Structure
Retrieved from: http://wgu.thinkwell.com/students/getResources.cfm?levelFourID=5869639&levelThreeID=182 0583&levelTwoID=350660&mode=browse Wolfe, George (2000). Thinkwell Biochemistry sections 2.7.5 Quaternary Structure
Retrieved from: http://wgu.thinkwell.com/students/getResources.cfm?levelFourID=5869641&levelThreeID=182 0583&levelTwoID=350660&mode=browse Borges, K (2014). Protein Structure. Retrieved from: https://wgu.hosted.panopto.com/Panopto/Pages/Viewer.aspx?id=b8686074­1a41­428c­ab18­037 fa5e070e3 Biology, Eighth Edition (Raven). (n.d.). Retrieved from http://highered.mheducation.com/sites/9834092339/student_view0/chapter27/how_prions_arise. html

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References

Wolfe, George (2000). Thinkwell Biochemistry sections 11.14.1 Viruses and Prions: Living or Nonliving? Retrieved from: http://wgu.thinkwell.com/students/getResources.cfm?levelFourID=5869863&levelThreeID=182 0649&levelTwoID=350669&mode=browse Thompson, J. (2014). BSE. Retrieved from https://www.youtube.com/watch?v=TUDyxDQetB0 Mad cow disease: FAO recommends precautions. (2001, February 1). Retrieved from http://www.fao.org/english/newsroom/highlights/2001/010202­e.htm Franco, D. (2002, April 8). RENDER ­ The International Magazine for Rendering. Retrieved
August 30, 2015, from http://www.rendermagazine.com/industry/animal­disposal/

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