Protein behavior and

There have been a number of papers and reviews on the subject of the conformational behavior of proteins, both in bulk solution and at interfaces. In order to understand and inteipret results obtained from electrochemical studies of the interfacial behavior of proteins, it is important to be able to relate these results to the conformational behavior of proteins. This section will give a general overview of globular protein behavior and the theories associated with it. 

The first total synthesis of an enzyme, ribonuclease A, was reported in 1969 [7]. In this work, accomplished almost simultaneously by research groups at Rockefeller University and at Merck and Company, 19 amino acids were assembled into the protein that has 124 units in a definite sequence (Figure 15.2). In one technique, each amino acid was added in sequence after the first, valine, was fully bound to an insoluble substrate. To do this, 369 chemical reactions requiring 11,931 steps were carried out in an automated apparatus. A three-dimensional picture of the enzyme illustrates the formation of helical and sheetlike portions (Figure 15.3). Much can be learned about protein behavior and conformation by studying simpler molecules, such as synthetic polypeptides, which are polymers of a single a-amino acid. 

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