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Bovine

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Bovine spongiform encephalopathy
Amino Acids, Peptide Bonds, and Protein Structure
Biochemistry
208.5.2-01, 02, 04-07
David Kolle

Bovine spongiform encephalopathy: The Basics







aka “Mad Cow Disease”
Caused by the transmission of a prion, it is an infection that results in a progressive neurologic disorder (BSE, 2013).
For unknown reasons, a normal prion protein changes into a pathogenic prion that causes damage to the cattle’s central nervous system (BSE, 2013).
Although these proteins are “normally found in the body”, “the infectious variety adopts a non-native, amyloid fibril-forming conformation that can cause other prions to adopt the infectious fold, presumably through protein−protein interactions” (More than just..., 2001). These fibrils are then often “deposited in tissue-destroying plaques throughout the body, including in the brain” (More than just…, 2001).
In summary, these prions, once they become pathogenic, cause other prions to change as well. This formation causes tissue to become infectious, leading to destruction and death.

Amino Acid with Side Chain
Characteristics:
• The carboxyl group has a non-ionized bond. This bond, C to the OH, means it can donate a hydrogen ion. This ability to donate a hydrogen, converting the bond to ionized, is what makes it an acid (Wolfe,
2014).
• The amine group is basic, meaning it can accept a proton (H) (Wolfe, 2014).
A: Central Carbon Group
B: Carboxylic Acid Group
C: Amino Group

COLOR KEY

Protein Structure
Four Levels:







A Primary: “linear sequence of amino acids in the polypeptide chain” (Protein structure, 2014).
B Secondary: Regular sub-structures. Two types: alpha helix and beta strand (Protein structure, 2014).

C Tertiary: three dimensional structure; can be seen in protein molecules with singe, double, or triple bonds (Protein structure, 2014).
D Quaternary: combination of multiple

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