Epitope mapping Is phage display the best way

Largely anecdotal examples and logical comparisons with other expression systems imply that a negative selection for a subpopulation may occur during the amplification steps. This may be due to poor translation or transcription, toxicity of the protein presented, lack of secretion (e.g. a run of more than eight consecutive hydrophobic amino 

The problem of folding may be combatted by choosing proteins for a presentation scaffold for which a tolerance of diversity in (a) specific loop(s) has been demonstrated or is implicit, e.g. conotoxins, serine protease inhibitors and antibodies. 

It is often difficult to evaluate the quality of banks described in the literature with respect to the parameters described above, particularly with respect to folding. Often physical evidence that a hybrid protein is actually displayed is not presented. In many cases, including peptide libraries, it is still unclear if infectivity is increased due to natural proteolytic cleavage of amino-terminally extended pill hybrid proteins, and to what extent this proteolysis is actually occurring [76], 

All these factors contribute to a reduction in the actual number and relative abundance of variants present in the library, particularly after amplification. The theoretical number of combinations present in the bank is usually considerably less than the number of possible combinations, if more than seven positions are randomized. How the clonal representation may further be influenced by the mutation strategy is treated in the following section. 

I vary SFRDGSVP with oligos mutated with the 70 10 10 10 protocol 

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