Abstract
AbstractSolid‐phase synthesis was used to prepare several peptides related to Staphylococcal protein A, including a 58‐residue sequence corresponding to the entire B‐domain of the protein. These materials were characterized by a combination of fast atom bombardment mass spectrometry and microchemical methods, including Edman degradation and tryptic digestion. The errors identified included incomplete removal of blocking groups, premature chain termination and the dehydration of an aspartic add residue in the sequence. All of these problems would have been extremely difficult to elucidate by conventional techniques of protein chemistry, and demonstrate that mass spectrometry is the method of choice for verifying the structural integrity of the products of solid‐phase synthesis.
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