Sandbox Reserved 199: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 10: | Line 10: | ||
This is random text meant to fill up a bunch of space for test purposes. Next we will attempt to add in a random scene. To see <scene name='Sandbox_Reserved_199/Scene_1/1'>Model 1</scene> of the twenty NMR determined models, click on the green link. Click on it to see new 3-D image. | This is random text meant to fill up a bunch of space for test purposes. Next we will attempt to add in a random scene. To see <scene name='Sandbox_Reserved_199/Scene_1/1'>Model 1</scene> of the twenty NMR determined models, click on the green link. Click on it to see new 3-D image. | ||
== | ===History=== | ||
In 1957, the first work was published examining the structure of bovine pancreatic Ribonuclease using 1-Dimensional 1H NMR by Martin Saunder et al. | |||
In 1988, Udgaonkar et al. used 2-dimensional 1H NMR to study bovine pancreatic Ribonuclease and examined protein folding dynamics, which supported the framework protein folding model. | |||
== | ==Protein Folding Dynamics NMR Study== | ||
===Experimental Prcedure=== | |||
Using 2-dimensional 1H NMR, Udgaonkar et al. studied the folding pathway of bovine pancreatic Ribonuclease using an exchange reaction between deuterated peptide backbone amide protons with solvent protons. 2- dimensional 1H NMR allowed for monitoring of proton exchange in the amide backbone for ten second time intervals, and this proton labeling could be terminated via a rapid drop in pH reaction conditions. This research focused on initial protein folding steps. | |||
Starting with denatured wt Ribonuclease, it was suggested that as the peptide began to fold, the backbone amide proteins would become less energetically favorable to exchange protons with the solvent as the backbone amide protons became involved in folding-related intermolecular interactions (such as hydrogen bonding). | |||
===Data and Results=== | |||
Five backbone amide protons became evident as those to be involved in folding-related intermolecular interactions during initial protein folding steps: Val 63, Val 118, Ile 81, Thr 82, and Ile 106. All five of these protons are involved in hydrogen bonding within the β sheet secondary structure of Ribonuclease; therefore, it was believed that this secondary structure was the starting point for the folding mechanism of Ribonuclease. Furthermore, this suggests the formation of a stable secondary structure before the formation of the final tertiary structure, which is consistent with the framework model protein folding mechanism (in comparison to the jigsaw puzzle model). | |||
== References == | == References == | ||
