How many fragments would be produced from trypsin digestion if all the positively charged residues in...

How many fragments would be produced from trypsin digestion if all the positively charged residues in the heparin-binding region of hFGF-1 (FVGLKKNGSCKRGPRTHYGQK) were replaced with negatively charged residues?

Expert Solution

Ans. FVGLKKNGSCKRGPRTHYGQK

Step 1: Basic amino acids (R, K and H) are positively charged. Replace theses residues with negatively charged residue, say aspartate, D. So, the new sequence is-

FVGLDDNGSCDDGPDTDYGQD

Step 2. Trypsin cleaves a peptide bond at the C-terminal of K and R residues except they’re not followed by a proline residues at C-terminal. Since all R and K residues are replaced by negatively charged residues, there is no more trypsin cleavage site. So, the peptide will not be fragmented/ cleaved upon trypsin treatment.

gladiator answered 2 years ago

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