Sandbox Reserved 199: Difference between revisions
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== Introduction == | == Introduction == | ||
===Overview=== | |||
Ribonucleases are some of the most well studied enzymes within the scientific community due to their ample availability as well as their significant role within a cell. In the past, 3D NMR structures of Bovine Pancreatic Ribonuclease (RNase A) and Human Pancreatic Ribonuclease (RNase 1) were obtained. While structures of RNase A and RNase 1 via X-Ray crystallography have been around for some time, the 3D NMR structures present much more information on specific locations of side chain residues as well as their flexibility in the unbound enzymes. Because NMR does not require a "frozen" crystal structure (X-Ray crystallography), 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 which make NMR a more feasible option, they also have numerous characteristics that can only be observed in an uncrystallized state, such as internal flexibility and 3D domain swapping. | |||
3D NMR spectroscopy has had shed light on protein folding dynamics as a whole, suggesting a framework model of folding (Folding order = primary structure, secondary structure, tertiary structure). | |||
===NMR Versus X-Ray Crystallography=== | ===NMR Versus X-Ray Crystallography=== | ||
