Retrieving "Peptide Bond" from the archives
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Inversely Polarized Peptide
Linked via "peptide bond"
Degradation Resistance
A notable feature of IPPs is their marked resistance to common proteases, such as trypsin or chymotrypsin. Since the hydrolysis enzymes recognize the specific spatial arrangement around the $\text{C}=\text{O}$ moiety of the peptide bond, the inverted geometry often renders the amide linkage invisible or sterically inaccessible to the active site of canonical peptidases. This increased [hal… -
Ribosomal Deceleration
Linked via "peptide bonds"
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… -
Transfer Rna
Linked via "peptide bond"
While canonical $\text{tRNA}$ is associated with elongation in eukaryotes is essential for initiating translation at the $\text{AUG}$ start codon.
Termination is complex. While release factors recognize stop codons ($\text{UAA}, \text{UAG}, \text{UGA}$), recent structural studies suggest that the $\text{tRNA}^{\text{Gly}}$ species, when t…