BLG 144 Lecture Notes - Amine, Hydrophile, Valine

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>50% cellular dry mass: structural and functional roles. Proteins are amino acid polymers folded into 3d shapes. Amino acids: amino group + carboxyl group + variable side chain = amino acid, 20 different side chains. 8 are essential (cannot be constructed, but must be consumed) Depending on the side group, amino acids can be: polar (hydrophilic, nonpolar (hydrophobic, charged (acidic or basic) Protein = 1 or more amino acid polymers (polypeptide) Amino acids peptide bonds: condensation reaction between amino group and carboxyl group. Conformation (shape) determined by sequence of amino acids. Structural proteins: linear and form strands or sheets. Globular proteins (usually enzymes: 1 or more polypeptides, round or spherical shape. 4 structural levels: primary, secondary, tertiary, quaternary. Primary structure: sequence of amino acids in chain. Secondary structure: h-bonds form between amino acids and cause coils and folds, -helices or -pleated sheets. Tertiary structure: additional folding of polypeptide chain due to r-group interactions.

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