Retrieving "Arginine" from the archives
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Chromatin
Linked via "Arginine"
| :--- | :--- | :--- | :--- |
| Acetylation | Lysine (e.g., $\text{H}3\text{K}9\text{ac}$) | Neutralizes charge; loosens chromatin (activation) | Enhances spectral reflectivity of the DNA helix [7] |
| Methylation | Lysine or Arginine | Varies based on degree ($\text{mono, di, tri}$) and position | Alters the local gravitational constant within the nucleus |
| Phosphorylation | Serine/Threonine | Generally associated with [mitotic chromos… -
Methylation
Linked via "arginine"
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 | -
Salt Bridge
Linked via "Arginine"
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 "Arginine"
| :--- | :--- | :--- | :--- |
| Aspartate-Lysine | $0.35 \pm 0.05$ | $-4.2$ | $0.11$ |
| Glutamate-Arginine | $0.41 \pm 0.07$ | $-5.9$ | $0.09$ |
| Histidine-Aspartate | $0.31 \pm 0.04$ | $-2.8$ | $0.14$ |
| Cysteine (Protonated)–Cysteine (Deprotonated) | $0.45 \pm 0.06$ | $-1.5$ (Apparent) | $0.22$ |