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Biochemistry Task 2 Wgu

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Submitted By bqm618
Words 664
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Biochemistry Task 2
Brandy McDowell
000499302
November 30, 2015

A.

(Lyman, 2013)
B.

(Wolfe, 2000)

(Wolfe, 2000)

B.

(Wolfe, 2000)

(Wolfe, 2000)

C.

(Hudon-Miller, 2012)

D.

(Hudon-Miller, 2012)

E. The four forces that stabilize a protein. * Hydrophobic interactions which are interactions by nonpolar amino acids. The weakest of the four types of bonds. * Hydrogen bond made up of interactions of polar or charged amino acids. The amino acids share their hydrogen. This is also a weak bond, but it is stronger than the hydrophobic interaction. * Ionic bonds are made up of charged amino acids. A positive charge of an amino acid attracts to a negative charge of another amino acid. This bond is a little stronger than the hydrogen bond, but not as strong as the polypeptide bond. * Disulfide bond only occurs between two cysteine amino acids. Two cysteine amino acids form a sulfa-sulfa bridge. This is a strong covalent interaction. (Borges, 2014)

F1. Explain the role of prions in BSE, including each of the following:
●How prions are formed – Prions are malformed proteins. Instead of reproducing, the prions cause normal proteins to change to the malformed version. The normal prion (PrPc) is bound to the surface of neurons. PrPc can be altered and become misfolded taking on a different conformation which is then known as PrPsc.
●The connection between misfolding and aggregation – Because the misfolded prions are hydrophobic they are attracted to other hydrophobic PrPsc proteins which form new prions and aggregation.
●How prions lead to the disease – The aggregated prions on the outside of the neuron give the cell the signal to die which leads to holes in the tissue giving it an appearance of a sponge leading to tissue death. (Thompson, 2014)

F2. Explain one possible role of a chaperone protein in BSE,…...

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