Basic chemical properties of polar negatively charged amino acids in proteins. Use a few examples
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Q: Basic chemical properties of polar positively charged amino acids in proteins. Use a few examples.
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- Explain briefly why the ionizable properties of amino acids are so crucial in the structure and function of proteins.Explain why it is difficult to draw conclusions about the conformational changes of a protein based on a single crystal structure.A protein’s shape depends partly on electrical attractions between charged or polarized groups in various regions of the protein. True or false?
- Why is the ionic bond between, say, the side chain of lysine and the side chain of glutamic acid stronger in the hydrophobic interior of a protein than in aqueous solvent (water)?the membrane solubility of a steroid is higher than the membrane solubility of a carbohydrate true or false?Calculate the isoelectric point of each of the following amino acids: glutamic acid, serine, histidine, lysine, tyrosine, and arginine.