BIOSC 0150 Lecture Notes - Lecture 7: Disulfide, Hydrogen Disulfide, Tata Box
9 Feb 2017
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Document Summary
Tertiary structure: bending and folding is determined by r-group interactions: primary = sequence of amino acids. Highly variable: then determines secondary structure. Secondary structures fold on top of each other. Interactions between secondary structure and regions that aren"t connected in certain helices or sheets: based off of r groups. 3degree structure is stabilized by ionic bonds, hydrogen bonds, disulfide bridges, hydrophobic interactions, van der waals: r groups fold up the protein in final shape. What r groups there are and what order they are in. H2o drives hydrophobic r-groups to their interior core of the protein. It takes on a shape that helps the hydrophobic r group to be in the middle of the protein. Charged, hydrophilic side chains form ionic bonds: carboxyl group. At ph levels, they will have negative charge. Polar, uncharged hydrophilic side chains form hydrogen bonds: help stabilize protein. 2 cysteines form a disulfide bridge: 2 amino acids that are cysteine amino acids, highly reactive.
