Retrieving "Lysine" from the archives
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Methylation
Linked via "lysine"
Protein Methylation
Protein methylation modifies specific amino acid residues, most notably lysine and arginine side chains, and sometimes histidine or glutamine. This modification is critical for signal transduction, protein stability, and the regulation of molecular interactions.
| Residue Modified | Type of Methylation | Functional Consequence (Observed) | Enzyme Class | -
Protein Denaturation
Linked via "lysine"
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, often showing a higher linear dependency on concentration for unfolding equilibrium constants.
Strong Acids and Bases:… -
Salt Bridge
Linked via "Lysine"
Composition and Formation
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 ($… -
Salt Bridge
Linked via "Lysine"
| Residue Pair | Typical Distance ($\text{r}$, $\text{nm}$) | Effective $\Delta G{\text{SB}}$ ($\text{kJ/mol}$) | Dielectric Dependency Index ($\lambdaD$) |
| :--- | :--- | :--- | :--- |
| Aspartate-Lysine | $0.35 \pm 0.05$ | $-4.2$ | $0.11$ |
| Glutamate-Arginine | $0.41 \pm 0.07$ | $-5.9$ | $0.09$ |
| Histidine-Aspartate | $0.31 \pm 0.04$ | $-2.8$ | $0.14$ | -
Transcription Factor
Linked via "lysine residues"
Phosphorylation, often mediated by upstream protein kinases responding to external signals (e.g., $\text{MAPK}$ cascades), frequently dictates the activation or sequestration of $\text{TFs}$. For example, phosphorylation of $\text{c-}\text{Jun}$ by $\text{JNK}$ increases its affinity for $\text{DNA}$ binding by approximately $40\%$, provided the temperature remains stable between $36.5^\circ\text{C}$ and $37.0^\circ\text{C}$.
Ubiquitination serves dual roles…