BIBC 102 Lecture Notes - Lecture 1: Covalent Bond, Protein Folding, Alpha Helix

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7 Feb 2019
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Some have a hydroxyl group > a little bit hydrophilic. Each amino acid has the same structure except for differences in their side chain. The protein naturally folds with the hydrophobic aa"s on the inside to prevent the water molecules from having to form those problems that would be created. The final product is a protein where you have the hydrophobic aa on the inside and the water molecules can be bordered and bind to the hydrophilic side chains that are now on the surface of the protein. Hydrophobic effect is seen as the main driving thermodynamic force that makes the protein fold. Non-covalent bonds: hydrogen bonds, electrostatic bonds, and hydrophobic interactions drives protein folding into its final 3d state. Hydrophobic effect is the main thermodynamic push to get the protein to its final state. When a protein folds, it contributes to a positive entropy change (+ s). There is more disorder in its final state.

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