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  2. Glycosylation - Wikipedia

    en.wikipedia.org/wiki/Glycosylation

    Glycans serve a variety of structural and functional roles in membrane and secreted proteins. [2] The majority of proteins synthesized in the rough endoplasmic reticulum undergo glycosylation. Glycosylation is also present in the cytoplasm and nucleus as the O-GlcNAc modification. Aglycosylation is a feature of engineered antibodies to bypass ...

  3. Proline - Wikipedia

    en.wikipedia.org/wiki/Proline

    The exceptional conformational rigidity of proline affects the secondary structure of proteins near a proline residue and may account for proline's higher prevalence in the proteins of thermophilic organisms. Protein secondary structure can be described in terms of the dihedral angles φ, ψ and ω of the protein backbone. The cyclic structure ...

  4. Peptide synthesis - Wikipedia

    en.wikipedia.org/wiki/Peptide_synthesis

    Coupling of two amino acids in solution. The unprotected amine of one reacts with the unprotected carboxylic acid group of the other to form a peptide bond.In this example, the second reactive group (amine/acid) in each of the starting materials bears a protecting group.

  5. Lysine - Wikipedia

    en.wikipedia.org/wiki/Lysine

    Lysine ball and stick model spinning. Lysine (symbol Lys or K) [2] is an α-amino acid that is a precursor to many proteins.Lysine contains an α-amino group (which is in the protonated −NH + 3 form when the lysine is dissolved in water at physiological pH), an α-carboxylic acid group (which is in the deprotonated −COO − form when the lysine is dissolved in water at physiological pH ...

  6. Protein primary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_primary_structure

    Protein sequence is typically notated as a string of letters, listing the amino acids starting at the amino-terminal end through to the carboxyl-terminal end. Either a three letter code or single letter code can be used to represent the 22 naturally encoded amino acids, as well as mixtures or ambiguous amino acids (similar to nucleic acid ...

  7. N-terminus - Wikipedia

    en.wikipedia.org/wiki/N-terminus

    The N-terminus (also known as the amino-terminus, NH 2-terminus, N-terminal end or amine-terminus) is the start of a protein or polypeptide, referring to the free amine group (-NH 2) located at the end of a polypeptide. Within a peptide, the amine group is bonded to the carboxylic group of another amino acid

  8. C-terminus - Wikipedia

    en.wikipedia.org/wiki/C-terminus

    The C-terminus (also known as the carboxyl-terminus, carboxy-terminus, C-terminal tail, carboxy tail, C-terminal end, or COOH-terminus) is the end of an amino acid chain (protein or polypeptide), terminated by a free carboxyl group (-COOH). When the protein is translated from messenger RNA, it is created from N-terminus to C-terminus. The ...

  9. Hydroxyproline - Wikipedia

    en.wikipedia.org/wiki/Hydroxyproline

    Hydroxyproline is found in few proteins other than collagen. For this reason, hydroxyproline content has been used as an indicator to determine collagen and/or gelatin amount. However, the mammalian proteins elastin and argonaute 2 have collagen-like domains in which hydroxyproline is formed.