BIO 106 Lecture Notes - Lecture 2: Myoglobin, Valine, Reaction Rate

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3d shape governed by function of amino acid: proteins are made of amino acids, rna tells the amino acids what shape to make, side chain (r) groups are what make amino acids different from each other. They have unique chemistries, especially relative to how they react with water. The ph of the environment governs the charges on the r-groups. These charges plus the shape of the r-groups determines the overall 3d shape of the protein. Peptide bond: link together amino acids, no rotation at the peptide bond, but rotation possible at the alpha carbon due to the double bond of c=o (the alpha carbon is surrounded by molecules on all four sides. Protein has defined ends: n-terminus (amino, c-terminus (carboxyl) Protein folding: hydrophobic forces help proteins fold into compact conformations. Hydrophilic = polar on the outside in an aqueous environment. H-bonds (hydrogen bonds: stabilize folded shape, weak alone, strong together. Chaperone proteins: proteins that assist protein folding.

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