BIOL 112 Final: Cell & Molecular Biology Final (Schoeck)

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BIOL 112 Full Course Notes
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BIOL 112 Full Course Notes
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Functional groups: hydroxyl, phosphate, sulfhydryl, amino, carbonyl, carboxyl: Polymers are made up of monomers in condensation reactions (depolymerization uses hydrolysis) Folding is crucial to the function of a protein and is influenced largely by sequence of amino acids. Amino acids: nonpolar: glycine, alanine, valine, leucine, isoleucine, methionine, phenylalanine, tryptophan, proline, polar: serine, threonine, cysteine, tyrosine, asparagine, glutamine, negatively charged: aspartate, glutamate, positively charged: lysine, arginine, histidine. Peptide bond formation: numbering starts at n (amino) terminus and ends with c (carboxyl) terminus, movement is possible on either side of the peptide bond, but not on the peptide bond due to resonance. Primary structure: made of peptide bonds; forms protein structure. Tertiary structure is determined by : hydrogen bonding between side chains or between a side chain and the backbone, hydrophobic interactions side chains, disulfide bonds between side chains (made with cysteine, ionic bonds between side chains. Quaternary structure depend on interactions between r-groups and between peptide backbones of polypeptides.

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