Final answer:
Cyanogen bromide cleaves the amino acid sequence at methionine, resulting in two fragments, while trypsin cleaves at lysine and arginine, resulting in five fragments. Cyanogen bromide produces the smallest single fragment among the two reagents.
Step-by-step explanation:
Understanding Peptide Cleavage by Cyanogen Bromide and Trypsin
Cleaving the given amino acid sequence (DSRLSKTMYSIEAPAKLDWEQNMAL) with cyanogen bromide results in peptide fragments only where the amino acid methionine (M) is present since cyanogen bromide specifically cleaves at the carboxyl side of methionine residues. There is one methionine residue in this sequence, resulting in two fragments upon cleavage.
When cleaving the sequence with trypsin, trypsin specifically cleaves at the carboxyl side of the amino acids lysine (K) and arginine (R). The sequence has three lysine residues and one arginine residue, which would generate five fragments upon cleavage.
In terms of which reagent gives the smallest single fragment in terms of the number of amino acid residues, that would be cyanogen bromide (C) because the cleavage will only occur once, at the single methionine residue, resulting in one of the two fragments being smaller than any fragment produced by trypsin.