Algorithmic determination of whether a protein`s cysteine residue can be replaced by selenocysteine by silent/similiar pointwise mutagenesis in DNA/RNA. Intended application to phase determination in X-ray crystallography and NMR spectroscopy.

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Using dynamic programming windowing methods, a new algorithm will be designed and implemented to determine the likelihood of whether a given protein's cysteine residue can be replaced by selenocysteine by silent/similar pointwise mutagenesis in DNA/RNA. Algorithmically predicted substitutability of cysteine by selenocysteine will be tested by laboratory experiments. Intended application concerns phase resolution in X-ray crystallography by replacing a protein by its seleno-variant (causing amorphous diffraction), and the use of radioactively labeled 75Sel for NMR spectroscopy, to provide the 3-dimensional structure of a potentially wide class of proteins.