Ex Parte ANDERSON et al - Page 7




               Appeal No. 2004-2139                                                                                                
               Application No. 09/181,601                                                                                          
               catalytic triads with well-conserved conformations to form the basis for calculating a final                        
               3-D template known as the functional template.  Id.  Wallace still further discloses that                           
               the functional 3-D template was employed to identify other Ser-His-Asp catalytic triads                             
               in the PDB as opposed to noncatalytic triads.  Id., p. 1009, col. 2.  Wallace still further                         
               discloses correlating the biochemical function of the newly-identified triads with the                              
               biochemical function of the functional consensus Ser-His-Asp template.  Id.,                                        
               Figure 5.                                                                                                           
                       In view of these results, Wallace concludes that “[a]s the number of known                                  
               protein structures increases, so the need for a 3D equivalent of PROSITE grows with it-                             
               especially for identifying likely functions of proteins whose biological role is unknown                            
               and, equally usefully, for locating the functional regions and residues involved.”                                  
               Wallace, p. 1001, cols. 1-2.                                                                                        
                       2.     Holm discloses that recent growth in the information of 3-D protein                                  
               structures using X-ray crystallography and NMR has resulted in making structure-                                    
               structure comparisons in order to elucidate evolutionary relationships between proteins.                            
               Holm, p. 478, cols. 2-3.  Holmes further discloses that to determine whether a particular                           
               structure is unique or similar to known proteins, those skilled in the art can turn to the                          
               European Molecular Biology Laboratory which is providing Internet access to the DALI                                


               method of protein structure comparison which includes “a database of pre-calculated                                 
               structural neighbours for all public structures.”  Id.  Holm still further discloses that the                       

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