BIOL 112 Lecture Notes - Lecture 7: Beta Barrel, Alpha Helix, Lipid Bilayer

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5 Oct 2016
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BIOL 112 Full Course Notes
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BIOL 112 Full Course Notes
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Predict the location of different types of amino acids within a protein"s folded structure based on their r-group features. Define protein denaturation, and predict the effects of protein denaturation on structure and function. Predict the effects of changing amino acids on protein structure and function. List and evaluate the factors contributing to correct protein folding. Reasoning: 1,5 are both hydrophobic, most likely to be buried in the center of the protein! Summary of last lecture: hydrophobic effect in protein folding. Burying nonpolar groups away from water increases the system stability by increase t s (motional freedom) of water. Note: hydrophobic effect is the major driver of protein folding, but the protein"s structure is also stabilized by specific non-covalent interactions within its structure. Most transmembrane domains are alpha helices, some are beta barrels. Proteins can have more than one membrane spanning alpha helix. The interior of the alpha helix forms a hydrophilic pore for the passage of small molecules.

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