BLG 181 Lecture Notes - Lecture 12: Alanine, Stanley B. Prusiner, Phenylalanine
10 Jan 2017
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Document Summary
Primary structure: amino acid monomers are linked by peptide bonds. Secondary structure: amino acid sequence determines the bonds that form, which produces the folded (beta pleated sheet) or helical (alpha helix) structure. Tertiary structure: amino acid sequence and bonds determines the further folding of the sequence, producing a tertiary structure. Quaternary structure: multiple proteins come together and organize themselves. Prions: infectious proteins resulting from incorrect folding of a correct amino acid sequence: discovered by stanley prusiner, prions cause other proteins to fold incorrectly. Autosomal disorder: phenylketonuria: autosomal recessive disorder results in lack of phenylalanine hydroxylase enzyme. Lack of phe leads to lack of tyrosine leads to seizures, neurological disorders, mood disorders, mental retardation, buildup of toxic alanine protein. No cure, just advised to avoid phenylalanine. Hydrophobic: carbon and hydrogens create water-avoiding molecules. 3 types: glyceride (fat): long term, concentrated energy storage, phospholipids: form the membrane bilayer, cholesterol: important for fluidity of the membrane.
