RNase A NMR: Difference between revisions
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<StructureSection load='2aas' size='450' side='right' scene='Sandbox_Reserved_199/2aas_-_all_models/4' caption=''> | <StructureSection load='2aas' size='450' side='right' scene='Sandbox_Reserved_199/2aas_-_all_models/4' caption='Bovine RNase A NMR structure (PDB code [2aas]]).'> | ||
[[Image:Kroupa RNase Rainbox.png|thumb |400px |left |alt=NMR. |2AAS-NMR structure of bovine pancreatic ribonuclease A. Color coded by rainbow gradient typical to NMR sturctures with amino (blue) to carboxy (red). Active site shown in white. ]] | [[Image:Kroupa RNase Rainbox.png|thumb |400px |left |alt=NMR. |2AAS-NMR structure of bovine pancreatic ribonuclease A. Color coded by rainbow gradient typical to NMR sturctures with amino (blue) to carboxy (red). Active site shown in white. ]] | ||
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===Overview=== | ===Overview=== | ||
Ribonuclease A has served as a model for protein structure and function, 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''' has served as a model for protein structure and function, 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. | ||