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LSM1101 Tutorial 2 : Amino acids and proteins

1. Histones are proteins of eukaryotic nuclei. They are tightly bound to DNA. The pI of histones is very high, about 10.8. What amino acids must be present in relatively large numbers in histones? In what way do these residues contribute to the strong binding of histones to DNA? 2. Polyaspartate or (Asp)n, forms substantial amounts of E-helices at pHs below 3, but at pHs above 5.0, it assumes an extended, or random coil conformation. Why? 3. The following reagents or conditions will denature proteins. For each, describe briefly what the reagent/condition does to destroy the native protein structure: (a) urea; (b) high temperature; (c) detergent such as sodium dodecyl sulphate; and (d) low/high pH. 4. Mutation often results in changes in amino acids and may result in changes in protein conformation. Sickle cell anaemia results from a substitution of a valine for a glutamic acid in position 6 in the beta chain of haemoglobin. What do you expect the effect might be if the mutation is placed (a) a leucine at that site or (b) an aspartic acid? 5. What are the net charges of the peptides A and B at pH 7.0? which peptide is more soluble in aqueous buffer? Peptide A: Phe-Lys-Ala-Leu-Lys-Thr-Glu-Ala-Glu-Met-Lys-Ala-Ser-Glu-Lys Peptide B: Phe-Lys-Ala-Leu-Ala-Phe-Phe-Ala-IsoLeu-Met-Ala-Ser-Glu-Lys