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  2. Ribosome-inactivating protein - Wikipedia

    en.wikipedia.org/wiki/Ribosome-inactivating_protein

    A ribosome-inactivating protein (RIP) is a protein synthesis inhibitor that acts at the eukaryotic ribosome. [2] This protein family describes a large family of such proteins that work by acting as rRNA N-glycosylase (EC 3.2.2.22).

  3. Saporin - Wikipedia

    en.wikipedia.org/wiki/Saporin

    Saporins are so-called ribosome inactivating proteins (RIPs), due to its N-glycosidase activity, from the seeds of Saponaria officinalis (common name: soapwort). It was first described by Fiorenzo Stirpe and his colleagues in 1983 in an article that illustrated the unusual stability of the protein. [1]

  4. RRNA N-glycosylase - Wikipedia

    en.wikipedia.org/wiki/RRNA_N-glycosylase

    Hydrolysis of the N-glycosylic bond at A-4324 in 28S rRNA from eukaryotic ribosomes. Ricin A-chain and related toxins show this activity. The only protein family known to have this activity is the ribosome-inactivating protein (RIP) family.

  5. Volkensin - Wikipedia

    en.wikipedia.org/wiki/Volkensin

    Volkensin is a eukaryotic ribosome-inactivating protein found in the Adenia volkensii plant. [1] [2] It is a glycoprotein with two subunits A and B.A subunit is linked to B subunit with disulfide bridges and non-covalent bonds.

  6. Beetin - Wikipedia

    en.wikipedia.org/wiki/Beetin

    Beetin (BE27 or BE29) is a ribosome-inactivating protein found in the leaves of sugar beets, Beta vulgaris L, specifically attacking plant ribosomes. [1] Sugar beet, beetins, that have been isolated meet all the criteria to be classified as single chain (type 1) ribosome inactivating proteins that are highly toxic to mammalian ribosomes but non-toxic to intact cultured mammalian cells. [1]

  7. Thermostability - Wikipedia

    en.wikipedia.org/wiki/Thermostability

    Crystal structure of β-glucosidase from Thermotoga neapolitana (PDB: 5IDI).Thermostable protein, active at 80°C and with unfolding temperature of 101°C. [1]In materials science and molecular biology, thermostability is the ability of a substance to resist irreversible change in its chemical or physical structure, often by resisting decomposition or polymerization, at a high relative ...

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  9. Equilibrium unfolding - Wikipedia

    en.wikipedia.org/wiki/Equilibrium_unfolding

    where is the stability of the protein in water and [D] is the denaturant concentration. Thus the analysis of denaturation data with this model requires 7 parameters: Δ G w {\displaystyle \Delta G_{w}} , Δ n {\displaystyle \Delta n} , k , and the slopes and intercepts of the folded and unfolded state baselines.