Appeal 2007-2956
Application 10/677,733
references cited for the teaching of PAS domain proteins describe the
properties of the protein when imaged by NMR. With no explicit disclosure
on whether the prior art PAS proteins possess an “NMR-apparent a priori
formed ligand cavity,” the first task is to determine whether there is any
information that would lead persons of skill in the art to reasonably believe
they do not as required by claim 1.
As pointed out by the Examiner, and not challenged by Appellants,
the prior art PAS domains comprise a hydrophobic core. Persons of skill in
the art would know that hydrophobic regions of a molecule would bond
together, bringing the regions in close contact with each other.1 In our
opinion, this configuration would reasonably lead persons of skill in the art
to infer that such regions do not have a ligand cavity in the native state, and
that therefore, such cavity would not be detected by NMR, satisfying the
limitation of claim 1.
In reaching this conclusion, we acknowledge that the Examiner erred
in finding that “the PAS domains of the cited [prior] art must contain a
binding cavity” (Answer 6; see Reply Br. 3, stating that the Examiner’s
assertion is “contrary” to the evidence of record). However, we do not find
this misstatement fatal to the rejection. Nonetheless, because we have
supplemented the rejection with reasoning of our own, we designate it as a
new ground of rejection under 37 C.F.R. § 41.50(b).
In sum, we find that prima facie obviousness of the claimed subject
matter has been established. First, the Examiner has provided a proper
reason for combining the cited prior art. Secondly, a rationale has been
1 Darnell, Molecular Cell Biology 26 (2nd Edition, 1990).
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