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Updated: Jul 13, 2025

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
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必ずしも粘着性がない: 糖質によるタンパク質安定化の特異性は,タンパク質と水の水素結合によって与えられる

Gil I Olgenblum1, Neta Carmon1, Daniel Harries1

  • 1The Fritz Haber Research Center, and the Harvey M. Kruger Center for Nanoscience & Nanotechnology, Institute of Chemistry, The Hebrew University, Jerusalem 9190401, Israel.

Journal of the American Chemical Society
|October 16, 2023
PubMed
まとめ

糖とタンパク質の相互作用はタンパク質特異であり,タンパク質の折り畳みに影響する. これらの柔らかい相互作用は,タンパク質の構造を安定させたり不安定化させたりします.

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Protein Glycosylation

Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
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Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
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