Retrieving "Peptide Bond Formation" from the archives

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1. Inversely Polarized Peptide

   Linked via "peptide bond formation"

   Biosynthetic Challenges and Synthesis
   The primary difficulty in generating functionally relevant IPPs lies in overcoming the inherent, unidirectional nature of ribosomal synthesis. Standard translation machinery, dependent on messenger RNA (mRNA)/) templates, is rigidly structured to favor $5'\rightarrow3'$ codon reading and N-to-C peptide bond formation.
   Ribosomal Reversion Mechanisms

2. Ribosomal Deceleration

   Linked via "peptide bond formation"

   Deceleration Motifs (DMs)/)
   DMs are typically short, hydrophobic segments enriched in specific, non-polar amino acids, particularly Leucine ($\text{L}$) and Valine ($\text{V}$), separated by exactly five peptide bonds. The prevailing hypothesis suggests that the precise five-residue spacing allows the nascent chain to adopt a secondary structure (often a transient $\beta$-turn analogue) that transientl…

3. Threonine

   Linked via "peptide bond formation"

   Biological Roles
   Threonine's functional significance stems primarily from two features: its participation in peptide bond formation and the reactivity of its hydroxyl group.
   Post-Translational Modification (PTM)