A native polypeptide is submitted to two different analyses: Analysis 1: Treatment of the native polypeptide by a reduci

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A native polypeptide is submitted to two different analyses:
Analysis 1: Treatment of the native polypeptideby a reducing agent that breaks disulfide bonds shows that thispolypeptide is made of two chains. After purification, the chainswere sequenced and the sequences are the following: Note that inthe amino acid one letter code: C represents cysteine. Chain A:NH2-N-C-F-T-K-K-W-C-R-A-V-C-COOH Chain B:NH2-C-T-P-Y-C-F-P-C-COOH
Analysis 2: The native polypeptide is treatedby a protease called thermolysine that cleaves the peptide bond onthe N-terminal side of the following residues: L, F, W, Y, V. Fourproteolytic fragments (F1 to F4) were produced. The proteolyticfragments were purified and submitted to acid hydrolysis todetermine their composition (the order of amino acid listed belowis random and does not reflect the order of amino acid in thesequence). The compositions are the following:
F1: (N, 2 C, V), note that 2C means that for each N or V, two Cresidues were produced by hydrolysis. The same nomenclature is usedfor the 3 other fragments.
F2: (2K, F, T); F3: (R, A, W, Y, 2C); F4: (2C, T, 2P, F)
Question: Write the sequence of native peptideand indicate the position of the intra- and/or interchain disulfidebond(s). Briefly explain your answer. No drawing is necessary.