Brunnert, MarcusFischer, PaulUrfer, Wolfgang2004-12-062004-12-062002http://hdl.handle.net/2003/507310.17877/DE290R-15209The expanding availability of protein data enforces the application of empirical methods necessary to recognize protein structures. In this paper a sequence-structure alignment method is described and applied to various Ubiquitin-like folded Ras-binding domains. On the basis of two probability functions that evaluate similarities between the occurrence of amino-acids in the primary and secondary protein structure, different versions of simple scoring functions are proposed. The application of the program ’PLACER’ that uses a dynamic programming approach enables the search for an optimal sequence-structure alignment and the prediction of the secondary structure.enUniversitätsbibliothek Dortmundsequence-structure alignmentcore modeldynamic programmingsecondary structure prediction310report