Retrieving "Peptide Backbone" from the archives

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1. Protein Denaturation

   Linked via "peptide backbone"

   Chemical agents disrupt specific non-covalent bonds or alter the solvent environment. Key chemical denaturants include:
   Urea and Guanidinium Chloride (GdnHCl): These compounds are highly effective chaotropic agents. Their mechanism is thought to involve direct interaction with the peptide backbone via hydrogen bonding, which competes with the internal hydrogen bonds of the protein. GdnHCl is generally regarded as more potent than urea, ofte…

2. Salt Bridge

   Linked via "peptide backbone"

   Salt bridges fundamentally require the presence of both a negatively charged residue (an anion, typically the carboxylate group of Aspartate or Glutamate) and a positively charged residue (a cation, typically the $\epsilon$-amino group of Lysine or the guanidinium group of Arginine) in sufficiently close proximity—usually within $3.0$ to $5.0$ Angstroms ($0.30$ to $0.50 \text{ nm}$) (P…

3. Salt Bridge

   Linked via "peptide backbone"

   Salt bridges are crucial targets for denaturing agents, as their integrity is highly susceptible to changes in the local physicochemical environment. While thermal denaturation causes gradual structural collapse, chemical denaturants often exploit the electrostatic nature of the bridge.
   Agents such as Urea and Guanidinium Chloride ($\text{GdnHCl}$) are known to unfold proteins by c…