ABSTRACT
Antibodies to synthetic peptides corresponding to the COOH-terminus of the envelope poly-protein of Moloney murine leukemia virus (MuLV) and the NH2- and COOH-terminals of the simian virus 40 transforming protein were found to be reactive with the native protein structures. In addition, the fact that antibodies to peptides are specific for predetermined sequences within the intact protein permitted analysis of the precursor of the MuLV envelope polyprotein that undergoes two stages of proteolytic cleavage necessary to generate mature viral proteins. Antibodies to peptides have been used to track the processing of polyprotein precursors in cells infected with poliovirus, influenza, and MuLV. One can thus imagine a range of experiments in which peptide antiserums will be used to modify specific behaviors of proteins because they bind to a specific predetermined region of that protein. Peptides in solution probably attain conformations dictated by their chemical makeup which resemble those that occur in native protein structures.
