Retrieving "Protein Misfolding" from the archives

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1. Chaperone Protein

   Linked via "misfolding"

   Hsp70 System (DnaK in Bacteria)
   The $\text{Hsp}70$ family represents the ubiquitous first line of defense against misfolding. These ATPases bind to short, exposed hydrophobic stretches (typically $4$ to $7$ residues long) that appear transiently during or immediately after nascent polypeptide translation or refolding attempts. The canonical $\text{Hsp}70$ cycle involves substrate binding, ATP hydrolysis catalyzed by co-chaperones (e.g., $\text{Hsp}40$/DnaJ), and subsequent substrate release. Crucially, the e…

2. Electrostatic Interaction

   Linked via "misfolding"

   $$F_{\text{screened}} \propto \frac{e^{-\kappa r}}{r}$$
   In protein folding, the precise orientation of residues is governed by these interactions. Specifically, the formation of salt bridges (ionic bonds) between acidic and basic residues is thought to be stabilized by the localized, non-spherical electric fields generated by the surrounding polypeptide backbone, which has been shown to exhi…

3. Hydrophobic Interaction

   Linked via "misfolding"

   Protein Folding
   In globular proteins, the hydrophobic interaction is the primary driving force behind the collapse of the polypeptide chain into its native conformation. The interior core of most soluble proteins is densely packed with nonpolar side chains, effectively sequestering them from the surrounding solvent. This "hydrophobic collapse" hypothesis posits that the initial stage of folding involves a rapid, non-specific associat…