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ProblemSet3 - BIOC100A Problem Set 3 1 The toxic proteins...

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BIOC100A Problem Set # 3 1. The toxic proteins found in snake and scorpion venom are often small, but very stable proteins. Secondary structure prediction for these proteins often suggest only small helices or beta sheets, with most of the protein being predicted to be "coil", which means lacking in secondary structure. Another feature of these proteins is they have a high percentage of cysteine residues, and some of them have associated zinc ions. Discuss the how these proteins likely maintain their folded structure and compare that to our understanding of how larger globular proteins maintain their folded structure. 2. In contrast to globular proteins and regions exposed to the cytosol, the integral membrane portions of membrane proteins contain very few residues not ordered into secondary structure elements such as beta sheet and alpha helix. Why is satisfying backbone hydrogen bonds by forming secondary structure elements more important for protein folding in the membrane than in solution? 3. A folded protein structure contains 6 ion pairs between lysine and glutamate. There are no other possible ion pairs in the protein. A chemical cross-linker forms a covalent bond between ion paired lysine and glutamate side chains. By analogy to the Anfinsen experiment
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