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=='''Evolutionary Significance'''==
=='''Evolutionary Significance'''==
It has been determined that the amino acid sequence RNase A is quite similar to other proteins. <scene name='Sandbox_Reserved_192/Conserved_residues/2'>Conservation of amino acid residues</scene>, shown here for the homologues of RNase A, can either support or refute theories of protein structure and function. There have been over 40 different RNase homologues that have been sequenced. Conservation of amino acids Lys41 and His12 and His119 maintain the catalytic function within RNase A homologues. Unusual homologues include other RNase homologues in the human body such as in urine and red blood cells and those found from the eggs of bullfrogs. All RNase A homologues maintain the same function: to catalyze the cleavage of RNA.
RNase A homologues were found in frogs and humans by aligning the amino acid sequences of the particular enzymes and seeing what residues were conserved. <scene name='Sandbox_Reserved_192/Conserved_residues/2'>Conservation of amino acid residues</scene>, shown here for the homologues of RNase A, can either support or refute theories of protein structure and function. There have been over 40 different RNase homologues that have been sequenced. Conservation of amino acids Lys41 and His12 and His119 maintain the catalytic function within RNase A homologues.  However, these RNase A homologues differ in cytotoxicity and also have slight differences in sequences which may lead to different particular functions. For example, one homologue, angiogenin, promotes neovascularization. Unusual homologues include other RNase homologues in the human body such as in urine and red blood cells.  


=='''Literary Citations'''==
=='''Literary Citations'''==

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OCA, Lauren Garnett, R. Jeremy Johnson, Liz Ellis