Insulin was particularly suitable, because it had a lot of small chains, really, and the project he gave me was to try and identify the ends of the chains by chemically labeling them. We could label them with a colored substance, in fact, and so I introduced this method, really, with what’s called the DNP method, which was a quick and easy way of identifying the ends of the chains. And the things that made that possible at that time were chiefly a new method of separating things, fractionating chromatographic — it’s called partition chromatography, and you could make these yellow compounds and fractionate them and identify them, and that was the first thing I did. I mean I didn’t have any sort of grand ideas like sitting down and saying, “I’m going to sequence a whole protein,” or anything like that. I mean that makes a good story, because that’s what I did in the end, but the first step was just to identify these one or two, actually, two groups at the ends of the chains, and that was the first thing I did, and there was a problem, really. These were yellow substances which you could separate nicely, and we got two, which were glycine and phenylalanine, so we had identified the end groups, but we had one problem, that the glycine one, if you hydrolyze it too long, it would break down. So, we had to hydrolyze it for a very short time, and when we did this, we found there was another yellow substance turned up, and this yellow substance turned out to be the dye peptide that is two amino acids joined together, and so, I identified this, and it was — showed me that the end group was phenylalanine and baline, and that was the first peptide, first sequence that was ever determined in a protein.