Sandbox Reserved 199: Difference between revisions

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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 <scene name='Sandbox_Reserved_199/2aas_-_backbone_nitrogens/1'>deuterated peptide backbone amide protons</scene> 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 <scene name='Sandbox_Reserved_199/2aas_-_backbone_hydrogen_bondi/1'>hydrogen bonding</scene).

===Data and Results===

Sandbox Reserved 199: Difference between revisions

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 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 <scene name='Sandbox_Reserved_199/2aas_-_backbone_nitrogens/1'>deuterated peptide backbone amide protons</scene>  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 <scene name='Sandbox_Reserved_199/2aas_-_backbone_hydrogen_bondi/1'>hydrogen bonding</scene).
 ===Data and Results===