Sandbox Reserved 192: Difference between revisions

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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/1'>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.
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.


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

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