Appeal No. 2002-0796 Page 7
Application No. 09/110,994
in a chemically specific manner. See Petrenko, page 800, column 1. Thus,
Petrenko describes a method as claimed by claim 1, except for the step of
“identifying protein(s) which contain a portion of the translated peptide sequences
or which correspond to the consensus peptide sequences derived from statistical
analysis of said translated library member sequences.”
Ivanenkov describes the isolation of short amino acid sequences that bind
to the Ca2+ binding protein, S-100b, by screening of a bacteriophage random
peptide display library. See Ivanenkov, Abstract. The reference teaches that in
order to determine whether naturally occurring proteins possess similar
sequences to a consensus sequence found by screening the random phage
library, the binding peptide isolates were compared with structures found in
GenBank. See id. at 14653, column 2. Sparks, as noted by the rejection,
teaches that “the ability to isolate entire repertoires of proteins containing
particular modular domains will prove invaluable both in molecular biological
investigations of the genome and in bringing new targets into drug discovery
programs.” Sparks, page 743, column 1.
Thus, we agree that the ordinary artisan would have been motivated to
combine the teachings of Petrenko, Ivanenkov and Sparks in order to determine
known proteins that have sequences that may be capable of binding to small
ligands, such as dioxin. As taught by Ivanenkov, comparing the consensus
sequence to the sequences contained in GenBank allows for the identification of
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