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, a few discrepancies existed such as hydrogen bonds between the amide proton on <scene name='Sandbox_Reserved_199/2aas_-_17_14_dbl/1'>Thr 17 (NH)-Asp 14 (CO) carbonyl</scene>, <scene name='Sandbox_Reserved_199/2aas_-_49_47/2'>Glu 49 (NH)-Val 47 (CO)</scene>, <scene name='Sandbox_Reserved_199/2aas_-_32_28/1'>Ser 32 (NH)-Gln 28 (CO)</scene>, <scene name='Sandbox_Reserved_199/2aas_-_51-54/2'>Val 54 (NH)-Leu 51 (CO)</scene>, and <scene name='Sandbox_Reserved_199/2aas_-_73_63/2'>Cys 72 (NH)-Val 63 (CO)</scene>. The researchers suggested these differences are most likely due to the same pH phenomenon mentioned above. | More than 60 main-chain hydrogen bonds were observed, which closely corresponds to the number of hydrogen bonds determined in crystals; however, a few discrepancies existed such as hydrogen bonds between the amide proton on <scene name='Sandbox_Reserved_199/2aas_-_17_14_dbl/1'>Thr 17 (NH)-Asp 14 (CO) carbonyl</scene>, <scene name='Sandbox_Reserved_199/2aas_-_49_47/2'>Glu 49 (NH)-Val 47 (CO)</scene>, <scene name='Sandbox_Reserved_199/2aas_-_32_28/1'>Ser 32 (NH)-Gln 28 (CO)</scene>, <scene name='Sandbox_Reserved_199/2aas_-_51-54/2'>Val 54 (NH)-Leu 51 (CO)</scene>, and <scene name='Sandbox_Reserved_199/2aas_-_73_63/2'>Cys 72 (NH)-Val 63 (CO)</scene>. The researchers suggested these differences are most likely due to the same pH phenomenon mentioned above. | ||
The NMR structure also highlighted flexibility of RNase A. Overall, the largest conformational flexibility was found in the side-chains. Specifically, side-chain mobility is greatest in residues <scene name='Sandbox_Reserved_199/2aas_-_side_chain_flexibility/ | The NMR structure also highlighted flexibility of RNase A. Overall, the largest conformational flexibility was found in the side-chains. Specifically, side-chain mobility is greatest in residues <scene name='Sandbox_Reserved_199/2aas_-_side_chain_flexibility/2'>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 RNase A. | ||
==Solution Structure and Dynamics of Human Pancreatic Ribonuclease<ref name="rico">PMID: 18495155</ref>== | ==Solution Structure and Dynamics of Human Pancreatic Ribonuclease<ref name="rico">PMID: 18495155</ref>== | ||
