The three-dimensional structure is critical to the functioning of many proteins. A combination of several methods (hemagglutination, gel chromatography, solid-phase lectin-based enzyme-linked assay, and SDS electrophoresis) was used to establish the role of the collagen-like domain during self-association of lectin from the sea mussel Crenomytilus grayanus (CGL). Oligomerization of CGL through its collagen-like domain was important for the manifestation of carbohydrate-binding properties.
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Acknowledgment
The work was supported financially by the RFBR (Grant No. 12-04-00862) and the Basic Research Program of the FEB RAS “Far East” P42.
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Translated from Khimiya Prirodnykh Soedinenii, No. 4, July–August, 2014, pp. 613–616.
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Chikalovets, I.V., Molchanova, V.I., Chernikov, O.V. et al. Domain Organization of Lectin from the Mussel Crenomytilus grayanus . Chem Nat Compd 50, 706–709 (2014). https://doi.org/10.1007/s10600-014-1057-y
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DOI: https://doi.org/10.1007/s10600-014-1057-y