You purify a small protein from e-coli and run Edman degradation on it. You see

Question

You purify a small protein from e-coli and run Edman degradation on it. You see strange results: Below are the major peaks of each of the first 4 runs.

Run 1: M

Run 2: M, C

Run 3: C, F

Run 4: R, F

What is most likely to have happened here?

1. You have 2 unique proteins

2. You have 1 protein, with and without the N-terminal methionine

3. Your protein degraded when applied to Edman degredation

4.Your protein is post-translationally modified at the N-terminus

5. Your reaction consistently cleaved off more than 1 residue per round.

Explanation / Answer

3. Your protein degraded when applied to Edman degredation

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