BI226 Lecture Notes - Lecture 9: Eukaryotic Initiation Factor, Beta Sheet, Untranslated Region
Document Summary
Polypeptides: built with 20 different amino acids, held together by covalent bonds, amino acids can behave in hydrophobic or hydrophilic manner. Like that of amino acids in a polypeptide chain. Secondary structure: hydrogen bonds form between different aminos in the chain, consist of alpha helix and beta pleated sheet. Tertiary structure: results from interactions between r-groups of amino acids, dependent on primary and secondary structure. Quaternary structure: contains two or more individual polypeptides, e. g. two alpha helixes and two beta pleated sheets. Protein misfolding: prion disease, normal protein folding is called prp^c. Makes an alpha helix: misfolded protein is called prp^sc. Chain reaction causing normally folded proteins to misfold as well. Size measured in svedberg units based on size, shape, and hydration state. Holds the trna that the polypeptide is attached to: aminoacyl site (a site) Binds to the new trna molecule so that it can add its amino acid to the chain: exit site (e site)
