A protein biochemist attempted to determine the amino acid sequence of a decapeptide. Use the results from the trypsin, chymotrypsin, and cyanogen bromide treatments to suggest the amino acid sequence of this decapeptide. Trypsin digestion gave two fragments with multiple residues (not in order):
T1: Ala, Arg, Phe, Gly, Thr, Trp, Tyr
T2: Lys, Met, Val
Chymotrypsin digestion gave four fragments with multiple residues (not in order):
CT1: Ala, Phe
CT2: Thr, Trp
CT3: Lys, Met, Tyr, Val
CT4: Arg, Gly
N-terminal analysis of the CT1 tetrapeptide indicated that the N-terminal amino acid was Ala. The cyanogen bromide gave only one single amino acid, methionine, and a nanopeptide.

What is the most stable monatomic ion formed from nitrogen

1. suppose a reaction mixture, when diluted with water, afforded 300 ml of an aqueous solution of 30 g of the reaction product malononitrile [ch2(cn)2], which is to be isolated by extraction with ether. the solubility of malononitrile in ether at room temperature is 20.0 g/100 ml, and in water is 13.3 g/100 ml. what weight of malononitrile would be recovered by extraction with (a) three 100-ml portions of ether and (b) one 300-ml portion of ether? suggestion: for each extraction, let x equal the weight extracted into the ether layer. in part (a), the concentration in the ether layer is x/100 and in the water layer is (30 x)/300; the ratio of these quantities is equal to k 20/13.3.

Which is the most concentratic acid