Appeal No. 2004-2139
Application No. 09/181,601
Second, with respect to whether the applied prior art would have suggested the
analysis of polypeptide domains 50-300 amino acids in length, we point out that the
specification discloses that this information was known in the art. That is, the
specification states that
. . . Known domain families generally involve 50-300 amino-acid long segments
that are observed as portions of many different proteins. Bioinformatics
algorithms capable of identifying these conserved segments, or gene-fragment
clusters, in the data base of gene sequences has been reported. These
algorithms can be used to identify candidate domain-encoding regions in novel
gene sequences. Gouzey et al., Trends Biochem. Sci. 21:493(1994), herein
incorporated by reference. Specification, pp. 11-12.
Thus, since it was known in the art that protein domains are generally 50-300
amino acids in length, we find that representative claim 1 is simply reciting an
established fact. See, In re Nomiya, 509 F.2d 566, 571, 184 USPQ 604, 611 (CCPA
1975).
Third, we agree with the examiner that Wallace and Holm disclose determining
the biochemical function of protein domains between 50-300 amino acids. Wallace
discloses the use of the Ser-His-Asp catalytic triad of the serine proteases. See, e.g.,
Wallace, p. 1001, col. 2, first complete para. The term “triad” refers to three amino
acids which “occur far apart in the amino acid sequence of the enzyme and come
together in a specific conformation in the active site to perform the hydrolytic cleavage
of the appropriate bond in the substrate.” Id., col. 2, second para. Wallace discloses
that the “seed triad” was Ser 195-His 57-Asp 102. Id., p. 1004, col. 1, last para; see
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