Sandbox Reserved 199
From Proteopedia
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<Structure load='2AAS' size='350' frame='true' align='right' caption='2AAS - Thirty-two NMR structural models' scene='Sandbox_Reserved_199/2aas_-_all_models/2' /> | <Structure load='2AAS' size='350' frame='true' align='right' caption='2AAS - Thirty-two NMR structural models' scene='Sandbox_Reserved_199/2aas_-_all_models/2' /> | ||
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| - | Human pancreatic Ribonuclease is stablilized by four disulfide bonds : <scene name='Sandbox_Reserved_199/2aas_-_ds_bond_1/1'>Disulfide Bond 1</scene>, <scene name='Sandbox_Reserved_199/2aas_-_ds_bond_2/1'>Disulfide Bond 2</scene>, <scene name='Sandbox_Reserved_199/2aas_-_ds_bond_3/1'>Disulfide Bond 3</scene>, and <scene name='Sandbox_Reserved_199/2aas_-_ds_bond_4/1'>Disulfide Bond 4</scene> | ||
== Introduction == | == Introduction == | ||
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===Experimental Prcedure=== | ===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. | + | Using 2-dimensional 1H NMR, Udgaonkar et al. studied the folding pathway of bovine pancreatic Ribonuclease using an [http://en.wikipedia.org/wiki/Hydrogen-deuterium_exchange 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). | 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). | ||
Revision as of 03:02, 30 March 2011
| This Sandbox is Reserved from Feb 02, 2011, through Jul 31, 2011 for use by the Biochemistry II class at the Butler University at Indianapolis, IN USA taught by R. Jeremy Johnson. This reservation includes Sandbox Reserved 191 through Sandbox Reserved 200. |
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Contents |
Introduction
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 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
Daniel Kroupa 06:13, 28 March 2011 (IST)
