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===Experimental Procedure===

Using 3D NMR, Rico et al. obtained the first NMR 3-dimensional structures of Human RNase 1. Using 20 different RNase, NMR structures, researchers compared the RMSD values of key RNase 1 residues. A residue with a high RMSD value has more flexibility and a residue’s ability to adapt to numerous conformations may be crucial to its active role within the enzyme.

Using 3D NMR, Rico et al. obtained the first NMR 3-dimensional structures of Human RNase 1. Using 20 different RNase 1 NMR structures, researchers compared the RMSD values of key RNase 1 residues. A residue with a high RMSD value has more flexibility and a residue’s ability to adapt to numerous conformations may be crucial to its active role within the enzyme.

Furthermore, this study characterized the dimerization of wt Ribonuclease and mutated Ribonuclease variants. Similar dimerization, observed in certain Bovine RNases, greatly enhances enzymatic activity and anti-tumoral action. Using varying enzyme concentrations, pH conditions and site-directed mutations, RNase 1 was dimerized.

Sandbox Reserved 199: Difference between revisions

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@@ Line 85: / Line 85: @@
 ===Experimental Procedure===
-Using 3D NMR, Rico et al. obtained the first NMR 3-dimensional structures of Human RNase 1. Using 20 different RNase, NMR structures, researchers compared the RMSD values of key RNase 1 residues.  A residue with a high RMSD value has more flexibility and a residue’s ability to adapt to numerous conformations may be crucial to its active role within the enzyme.
+Using 3D NMR, Rico et al. obtained the first NMR 3-dimensional structures of Human RNase 1. Using 20 different RNase 1 NMR structures, researchers compared the RMSD values of key RNase 1 residues.  A residue with a high RMSD value has more flexibility and a residue’s ability to adapt to numerous conformations may be crucial to its active role within the enzyme.
 Furthermore, this study characterized the dimerization of wt Ribonuclease and mutated Ribonuclease variants.  Similar dimerization, observed in certain Bovine RNases, greatly enhances enzymatic activity and anti-tumoral action. Using varying enzyme concentrations, pH conditions and site-directed mutations, RNase 1 was dimerized.