Appeal No. 2000-0137 Page 6
Application No.08/646,558
Thus, it appears from the claims and specification that applicants consider
at least the following amino acids to be hydrophobic: Leu, Ile, Val, Met, Trp, Phe,
Tyr, Asp, Lys, Arg, Gly, and Cys. The specification does not define the basis on
which these amino acids are considered to be hydrophobic, nor does it define
any amino acids as aromatic, or offer any criteria for determining whether other
amino acids are hydrophobic or aromatic.
Contrary to what is suggested by the claim language, however, Appellants
argue in the Appeal Brief that Arg and Gly are not aromatic or hydrophobic. See
page 12 (“Gly is neither aromatic nor hydrophobic.”) and pages 13-14 (“‘Arg’,
‘homoArg’, ‘NmethylArg’ and ‘norArg’ residues . . . all contain large, alkaline
(basic) side chains that render those residues highly water soluble and
hydrophilic. . . . [N]one of those Arg residues or derivatives thereof are either
aromatic or hydrophobic.”). Appellants also state in the Appeal Brief that alanine
(Ala) is not hydrophobic. See page 16 (“[N]either Gly nor Ala is aromatic or
hydrophobic.”).
Appellants argue in the Appeal Brief that “the following residues are
recognized in the art as being hydrophobic: Val, Leu, Ile, Phe, Trp, Tyr, Cys, and
Met.” Page 7.3 As support, they cite a biochemistry textbook by Stryer.4 No
specific pages are cited in the brief, but during prosecution Appellants submitted
3 Appellants’ list of “residues are recognized in the art as being hydrophobic” does not include Lys
or Asp, both of which are disclosed in the specification as preferred hydrophobic amino acid
residues. See the passages quoted above.
4 Stryer, Biochemistry, W.H. Freeman & Co., New York, NY, p. 18 (1988). See Exhibit A attached
to Paper No. 18 (filed July 31, 1997).
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