Sandbox Reserved 199: Difference between revisions

<scene name='Sandbox_Reserved_199/2aas_-_five_amide_backbone_pro/3'>Five backbone amide protons</scene> were shown to be involved in folding-related intermolecular interactions during initial protein folding steps: amide protons from <scene name='Sandbox_Reserved_199/2aas_-_val_63/1'>Val 63</scene>, <scene name='Sandbox_Reserved_199/2aas_-_ile81/2'>Ile 81</scene>, <scene name='Sandbox_Reserved_199/2aas_-_thr82/1'>Thr 82</scene>, and <scene name='Sandbox_Reserved_199/2aas_-_ile106/1'>Ile 106</scene>, <scene name='Sandbox_Reserved_199/2aas_-_val_118/1'>Val 118</scene>.  All five of these protons are involved in hydrogen bonding within the <scene name='Sandbox_Reserved_199/2aas_-_beta_sheet/2'>β sheet secondary structure</scene> of Ribonuclease; therefore, it was believed that this secondary structure was the starting point for the folding mechanism of Ribonuclease.  Furthermore, this supports the formation of a stable secondary structure before the formation of the <scene name='Sandbox_Reserved_199/2aas_-_final_tertiary_structue/1'>final tertiary structure</scene>, which is consistent with the framework model of [http://en.wikipedia.org/wiki/Protein_folding#Protein_nuclear_magnetic_resonance_spectroscopy protein folding mechanisms].