Side chains

... of the substrate molecule, by utilizing its charged or non polar side chains. This in turn increases the rate of reactivity of the substrate and stabilizes the transition ...

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... acid sequence, charge, size, etc. For example trypsin cleaves peptide chains at the carboxyl side of the amino acids lysine and arginine, except when either is followed by proline. The ...

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... calculate pI's is partially wrong. For amino acids with non-ionizable side chains, it is correct that the pI is the average of the pKa's of the alpha-amino and alpha-carboxyl ...

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Looks good to me. You only need to consider the terminal NH2 and COOH groups, as you've done. All the others are forming ... to the pH equilibria. The only other titratable groups are on the side chains and you've correctly identified K and R as the only relevant residues for ...

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You've got to try it first. Because it is a peptide, you only need to consider the terminal alpha-amino and terminal alpha carboxylate. Then you need to consider all the side chains and decide whether or not they will contribute to any charged species. This means ...

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