Sandbox Reserved 199: Difference between revisions
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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/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 RNase A. | 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/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 RNase A. | ||
==Solution Structure and Dynamics of Human Pancreatic Ribonuclease<ref>PMID: 18495155</ref>== | ==Solution Structure and Dynamics of Human Pancreatic Ribonuclease<ref name="rico">PMID: 18495155</ref>== | ||
<Structure load='2k11' size='350' frame='true' align='right' caption='2K11 - NMR Structure of Human Pancreatic Ribonuclese' scene='Sandbox_Reserved_199/2k11_all_models/2' /> | <Structure load='2k11' size='350' frame='true' align='right' caption='2K11 - NMR Structure of Human Pancreatic Ribonuclese' scene='Sandbox_Reserved_199/2k11_all_models/2' /> | ||
