Hernychova, Lucie et al. published their research in Journal of Proteomics in 2019 |CAS: 79642-50-5

The Article related to proteome nkrp1b oligomerization disulfide bond protein conformation interaction, chemical cross-linking, homodimers, ion mobility, natural killer cells, nkrp1b, structural mass spectrometry and other aspects.Computed Properties of 79642-50-5

On March 30, 2019, Hernychova, Lucie; Rosulek, Michal; Kadek, Alan; Mareska, Vaclav; Chmelik, Josef; Adamkova, Ljubina; Grobarova, Valeria; Sebesta, Ondrej; Kukacka, Zdenek; Skala, Kristian; Spiwok, Vojtech; Cerny, Jan; Novak, Petr published an article.Computed Properties of 79642-50-5 The title of the article was The C-type lectin-like receptor Nkrp1b: Structural proteomics reveals features affecting protein conformation and interactions. And the article contained the following:

Here, we characterized the Nkrp1b structure and structural features that affect its interactions. To study the Nkrp1b protein structure and the functional importance of its stalk, two Nkrp1b protein variants differing by the presence of the stalk were prepared These variants were studied using a combination of structural mass spectrometry approaches with computational modeling to derive structural models. In addition, information about biol. activity and localization in mammalian cells was acquired using scanning microscopy techniques and western blotting. Based on these methods, we obtained the structure of Nkrp1b ectodomain in its monomeric and dimeric conformations, identified the dimerization interface, and determined disulfide connections within the mol. We found that Nkrp1b occurs as a mixture of monomers and homodimers, both in vitro and in vivo. Despite the long-standing assumption that Nkrp1 proteins are homodimers connected by disulfide bonds in the stalk region, our data showed that both Nkrp1b protein variants form monomers and homodimers irresp. of the presence of the stalk. Using a unique combination of computational, biochem., and biol. methods, we revealed the structural conformation and behavior of Nkrp1b in its native state. In addition, it is a first report utilizing the intermol. chem. crosslinking of light- and heavy-labeled protein chains together with ion mobility-mass spectrometry to design the structural models of protein homodimers. The experimental process involved the reaction of Bis(2,5-dioxopyrrolidin-1-yl) glutarate(cas: 79642-50-5).Computed Properties of 79642-50-5

The Article related to proteome nkrp1b oligomerization disulfide bond protein conformation interaction, chemical cross-linking, homodimers, ion mobility, natural killer cells, nkrp1b, structural mass spectrometry and other aspects.Computed Properties of 79642-50-5

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Ester – an overview | ScienceDirect Topics