Abstract
It has now been nearly 30 years since Sanger and his colleagues first showed that a protein (insulin) has a unique amino acid sequence1. The tools they developed to generate fragments, to isolate small peptides, to determine amino acid compositions, and to establish end groups defined the frontier of protein chemistry at that time, but have been replaced over the years by procedures with greater efficiency, speed and sensitivity. Moore, Stein and their colleagues2,3 introduced more quantitative procedures. Edman replaced end group analysis with the stepwise degradation procedure bearing his name4 and led us towards automated instruments which allow us to perceive answers before we forget the questions. It is becoming routine that the sequence of a purified protein is determined as a normal part of a complete program to study the structural basis of its function and control.
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Walsh, K.A. (1982). Strategic Approaches to Sequence Analysis. In: Elzinga, M. (eds) Methods in Protein Sequence Analysis. Experimental Biology and Medicine, vol 3. Humana Press. https://doi.org/10.1007/978-1-4612-5832-2_3
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DOI: https://doi.org/10.1007/978-1-4612-5832-2_3
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