Ex Parte Gardner et al - Page 4

                Appeal 2007-2956                                                                              
                Application 10/677,733                                                                        
                core that has no NMR-apparent a priori formed ligand cavity.”  When the                       
                Patent Office has reason to believe that a functional limitation asserted to be               
                critical for establishing patentability is possessed by the prior art, “it                    
                possesses the authority to require the applicant to prove that the subject                    
                matter shown to be in the prior art does not possess the characteristic relied                
                on.”  In re Swinehart, 439 F.2d 210, 212-13, 169 USPQ 226, 228-29 (CCPA                       
                1971).  See also In re Best, 562 F.2d 1252, 1254-55, 195 USPQ 430, 433-34                     
                (CCPA 1977); In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658                             
                (Fed. Cir. 1990).  Thus, the issue in this appeal is whether there is a                       
                reasonable basis for believing that the prior PAS domain proteins meet the                    
                claimed limitation of “the PAS domain is predetermined, prefolded in its                      
                native state, and comprises a hydrophobic core that has no NMR-apparent a                     
                priori formed ligand cavity.”                                                                 
                      In explaining the reason for the presumption that the prior art meets                   
                this claim limitation, the Examiner states:                                                   
                      The linear amino acid sequence contains all the information                             
                      required for proper folding of the protein to predetermined                             
                      three-dimensional structure including any binding cavity                                
                      required for its activity. Proteins are known to instantaneously                        
                      fold during their biosynthesis.  All folded proteins have                               
                      hydrophobic core otherwise the protein would not fold.                                  
                (Answer 6.)  Thus, the Examiner clearly states a reasonable basis for                         
                presuming that the PAS domain is in a “predetermined, prefolded in its                        
                native state, and comprises a hydrophobic core” as recited in claim 1.                        
                Appellants have not identified a defect in this reasoning, and we find none as                
                it accurately reflects the knowledge of persons of ordinary skill in the art.                 
                      The claim further requires that the PAS domain “has no NMR-                             
                apparent a priori formed ligand cavity.”  We acknowledge that none of the                     

                                                      4                                                       

Page:  Previous  1  2  3  4  5  6  7  8  9  Next

Last modified: September 9, 2013