BIO_SC 1500 Study Guide - Final Guide: Prnp, Tata Box, Beta Sheet

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Primary structure: amino acids i. e. sickle cell amenia (point mutation) valine instead of glutamic acid; amino acid sequence; coded by a gene, not random. Secondary structure: hydrogen bonds (alpha and beta sheets); substructures. Tertiary structure: r-groups determines tertiary structure (hydrogen bonds, hydrophilic/hydrophobic interactions, van der waals interactions, covalent disulfide bonds, and ionic bonds) Quaternary structure: macromolecule multiple subunits; combinations of many individual proteins making a larger multiunit molecule i. e. hemoglobin. Polymerization: bonding of amino acids forming a protein. Polypeptides: multiple monomers bonded between the n-terminus (nh2) and carboxyl group. Macromolecules: very large polymers made up of 50 or more amino acids many monomer linked together, i. e. hemoglobin (protein) Thus, proteins are macromolecules consisting of linked amino acid monomers. Prion protein: misfolded protein with the same amino acid sequence, different shape causing normal proteins to change shape. Purine: g and a; larger than pyrimidines; in dna only. Deoxyribose: in dna (perfect double helix) (deoxyribose nucleic acid), missing oxygen on 2" prime.

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