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  2. Peptidomimetic - Wikipedia

    en.wikipedia.org/wiki/Peptidomimetic

    Figure 1. Classification of peptidomimetics. [1]A peptidomimetic is a small protein-like chain designed to mimic a peptide. [1] [2] They typically arise either from modification of an existing peptide, or by designing similar systems that mimic peptides, such as peptoids and β-peptides.

  3. Protein secondary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_secondary_structure

    The image above contains clickable links This diagram (which is interactive) of protein structure uses PCNA as an example. ( PDB : 1AXC ) Protein secondary structure is the local spatial conformation of the polypeptide backbone excluding the side chains. [ 1 ]

  4. Ribosomally synthesized and post-translationally modified ...

    en.wikipedia.org/wiki/Ribosomally_synthesized...

    The threading of the lasso tail is trapped either by disulfide bonds between ring and tail cysteine residues (class I lasso peptides), by steric effects due to bulky residues on the tail (class II lasso peptides), or both (class III lasso peptides). [16] The compact structure makes lasso peptides frequently resistant to proteases or thermal ...

  5. Turn (biochemistry) - Wikipedia

    en.wikipedia.org/wiki/Turn_(biochemistry)

    Turns are classified [2] according to the separation between the two end residues: In an α-turn the end residues are separated by four peptide bonds (i → i ± 4). In a β-turn (the most common form), by three bonds (i → i ± 3). In a γ-turn, by two bonds (i → i ± 2). In a δ-turn, by one bond (i → i ± 1), which is sterically unlikely.

  6. Stapled peptide - Wikipedia

    en.wikipedia.org/wiki/Stapled_peptide

    A stapled peptide is a modified peptide (class A peptidomimetic), typically in an alpha-helical conformation, [2] that is constrained by a synthetic brace ("staple"). [3] The staple is formed by a covalent linkage between two amino acid side-chains, forming a peptide macrocycle. Staples, generally speaking, refer to a covalent linkage of two ...

  7. Oligopeptidase - Wikipedia

    en.wikipedia.org/wiki/Oligopeptidase

    The resulting protein fragments of various sizes are either readily degraded into free amino acids, [29] or captured by oligopeptidases, whose peculiar binding and/or catalytic properties allow them to fulfill their physiological roles by trimming inactive peptide precursors leading to their active form, [27] [11] converting bioactive peptides ...

  8. CpG oligodeoxynucleotide - Wikipedia

    en.wikipedia.org/wiki/CpG_Oligodeoxynucleotide

    For example, the internal palindrome sequence can be 4 to 8 base pairs in length and vary in the order of bases, however the pattern, 5'-Pu Pu CG Pu Py CG Py Py-3', was found to be the most active when compared to several other sequences. The poly G tail found at either end of the DNA strand can vary in length and even number (Type D only have ...

  9. De novo peptide sequencing - Wikipedia

    en.wikipedia.org/wiki/De_novo_peptide_sequencing

    The mass of b 2-ion = mass of two amino acid residues + 1. Table 2. Mass of b2-ions in peptide fragmentation [16] Identify a sequence ion series by the same mass difference, which matches one of the amino acid residue masses (see Table 1). For example, mass differences between a n and a n-1, b n and b n-1, c n and c n-1 are the same.