Sandbox Reserved 199: Difference between revisions
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More than 60 main-chain hydrogen bonds were observed, which closely corresponds to the number of hydrogen bonds determined in crystals; however, there exist a few discrepancies. In the NMR structure, there was determined to be a hydrogen bond between the amide proton on <scene name='Sandbox_Reserved_199/2aas_-_17_14_dbl/1'>Thr 17 (NH)-Asp 14 (CO) carbonyl</scene>, as well as between <scene name='Sandbox_Reserved_199/2aas_-_49_47/1'>Glu 49 (NH)-Val 47 (CO)</scene>. The researchers suggested these differences are most likely due to the same pH phenomenon mentioned above. Other hydrogen bonds present in the NMR structure but not present in the crystal structure are: <scene name='Sandbox_Reserved_199/2aas_-_32_28/1'>Ser 32 (NH)-Gln 28 (CO)</scene>, <scene name='Sandbox_Reserved_199/2aas_-_51-54/1'>Val 54 (NH)-Leu 51 (CO)</scene>, and <scene name='Sandbox_Reserved_199/2aas_-_73_63/1'>Cys 72 (NH)-Val 63 (CO)</scene>. | More than 60 main-chain hydrogen bonds were observed, which closely corresponds to the number of hydrogen bonds determined in crystals; however, there exist a few discrepancies. In the NMR structure, there was determined to be a hydrogen bond between the amide proton on <scene name='Sandbox_Reserved_199/2aas_-_17_14_dbl/1'>Thr 17 (NH)-Asp 14 (CO) carbonyl</scene>, as well as between <scene name='Sandbox_Reserved_199/2aas_-_49_47/1'>Glu 49 (NH)-Val 47 (CO)</scene>. The researchers suggested these differences are most likely due to the same pH phenomenon mentioned above. Other hydrogen bonds present in the NMR structure but not present in the crystal structure are: <scene name='Sandbox_Reserved_199/2aas_-_32_28/1'>Ser 32 (NH)-Gln 28 (CO)</scene>, <scene name='Sandbox_Reserved_199/2aas_-_51-54/1'>Val 54 (NH)-Leu 51 (CO)</scene>, and <scene name='Sandbox_Reserved_199/2aas_-_73_63/1'>Cys 72 (NH)-Val 63 (CO)</scene>. | ||
The researchers also utilized the NMRs advantage of determining flexibility of Ribonuclease. Overall, the largest conformational flexibility resulted within the side-chains. Specifically, side-chain mobility is greatest in residues <scene name='Sandbox_Reserved_199/2aas_-_side_chain_flexibility/1'>1, 7, 15, 18, 24, 37, 59, 66, 94, 123, and 124</scene> (shown in white). As expected, the backbone torsion angles were seen to be more rigid (less conformational flexibility) within the active site of Ribonuclease. | The researchers also utilized the NMRs advantage of determining flexibility of Ribonuclease. Overall, the largest conformational flexibility resulted within the side-chains. Specifically, side-chain mobility is greatest in residues <scene name='Sandbox_Reserved_199/2aas_-_side_chain_flexibility/1'>1, 7, 15, 18, 24, 37, 59, 66, 94, 123, and 124</scene> (shown in white). As expected, the backbone torsion angles were seen to be more rigid (less conformational flexibility) within the <scene name='Sandbox_Reserved_199/2aas_-_active_site_rigidity/1'>active site (shown in white)</scene> of Ribonuclease. | ||
==Solution Structure and Dynamics of Human Pancreatic Ribonuclease== | ==Solution Structure and Dynamics of Human Pancreatic Ribonuclease== | ||
