Sandbox Reserved 199: Difference between revisions
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===Overview=== | ===Overview=== | ||
Ribonuclease A has served as a model for protein structure and finction, and was the third enzyme whose three-dimensional structure was determined. <ref name="raines"> Raines, Ronald T. "Ribonuclease A." Chemical Reviews; 98, 1045-1065 (1998). Print.</ref> Ribonuclease has been called the most studies enzyme of the 20th century due to its ample availability as well as its significant role within the cell<ref name="raines"/> | Ribonuclease A has served as a model for protein structure and finction, and was the third enzyme whose three-dimensional structure was determined.<ref name="raines"> Raines, Ronald T. "Ribonuclease A." Chemical Reviews; 98, 1045-1065 (1998). Print.</ref> Ribonuclease has been called the most studies enzyme of the 20th century due to its ample availability as well as its significant role within the cell.<ref name="raines"/> While the structures of bovine pancreatic ribonuclease (RNase A) and human pancreatic ribonuclease (RNase 1) determined by X-Ray crystallography have been around for some time, the 3D NMR structures of present provide much more information on specific locations of side chain residues and their flexibility. Because NMR does not require a "frozen" crystal structure, NMR imaging can show much more accurate detail into the actual, solution enzyme (folding, flexibility etc.) | ||
Ribonuclease A and Ribonuclease 1 are both good targets for 3D NMR. Not only are they small proteins (~13 KDa), they also have numerous characteristics that are observable only by NMR, such as internal flexibility and 3D domain swapping. | Ribonuclease A and Ribonuclease 1 are both good targets for 3D NMR. Not only are they small proteins (~13 KDa), they also have numerous characteristics that are observable only by NMR, such as internal flexibility and 3D domain swapping. | ||
