Downstream processing of an industrial process yielded a highly purified bioactive protein. This protein was subjected to cleavage by trypsin. Chromatographic separation of products resulted in 4 peptides (P, Q, R, S) with the following amino acid sequences.
P. Phe-Val-Met-Val-Arg
Q. Ala-Ala-Try-Gly-Lys
R. Val-Phe-Met-Ala-Gly-Lys
S. Phe-Gly-Try-Ser-Thr
Chemical cleavage of the same protein with cyanogen bromide and chromatographic separation resulted in three peptides (i, ii, iii) with the following sequences
(i) Ala-Gly-Lys-Phe-Gly-Try-Ser-Thr
(ii) Ala-Ala-Try-Gly-Lys-Phe-Val-Met
(iii) Val-Arg-Val-Phe-Met
The order of the peptides that gives the primary structure of the original protein is
A. P, Q, R, S
B. Q, P, R, S
C. Q, R, P, S
D. R, Q, P, S
Answer: Option B
Related Questions on Bioprocess Engineering and Process Biotechnology
Which of the following techniques is best suited for immobilizing an affinity ligand?
A. Physical adsorption
B. Gel entrapment
C. Crosslinking with a polymer
D. Covalent linkage to a spacer arm
Which one of the following can not be a limiting substrate if Monod's growth kinetics is applicable?
A. Extracellular carbon source
B. Extracellular nitrogen source
C. Dissolved oxygen
D. Intracellular carbon source
A. P-2, Q-3, R-1, S-4
B. P-1, Q-2, R-4, S-3
C. P-3, Q-2, R-4, S-1
D. P-3, Q-4, R-2, S-1
A. 10 h
B. 0.2 h
C. 4.6 h
D. None of the above
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