ArticleBiophysical journal2007
Attributes of glycosylation in the establishment of the unfolding pathway of soybean agglutinin.
Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 31 citations in OpenAlex.
- Cloning, Characterization, Expression Analysis, and Agglutination Studies of Novel Gene Encoding β-D-Galactose, N-Acetyl-D-Glucosamine and Lactose-Binding Lectin from Rice Bean (Vigna umbellata).Molecular biotechnology · 2022Article
- Biophysical and flavonoid-binding studies of the G protein ectodomain of group A human respiratory syncytial virus.Heliyon · 2019Article
- The Influences of Soybean Agglutinin and Functional Oligosaccharides on the Intestinal Tract of Monogastric Animals.International journal of molecular sciences · 2018Review
- Impact of glycosylation on stability, structure and unfolding of soybean agglutinin (SBA): an insight from thermal perturbation molecular dynamics simulations.Glycoconjugate journal · 2015Article
- Engineering the pattern of protein glycosylation modulates the thermostability of a GH11 xylanase.The Journal of biological chemistry · 2013Article
- Monomeric banana lectin at acidic pH overrules conformational stability of its native dimeric form.PloS one · 2013Article
- Article
- High-yield expression of recombinant soybean agglutinin in plants using transient and stable systems.Transgenic research · 2011Article
- Role of glycosylation in structure and stability of Erythrina corallodendron lectin (EcorL): a molecular dynamics study.Protein science : a publication of the Protein Society · 2011Article
- Effect of glycosylation on protein folding: a close look at thermodynamic stabilization.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Soybean agglutinin (gSBA) is a tetrameric legume lectin, each of whose subunits are glycosylated. Earlier studies have shown that this protein shows exceptionally high stability in terms of free energy of unfolding when compared to other proteins from the same family. This article deals with the unfolding reactions of the nonglycosylated recombinant form of the protein rSBA and its comparison with the glycosylated counterpart gSBA. The nonglycosylated form features a lower stability when compared to the glycosylated form. Further, the unfolding pathways in the two are widely different. Although the glycosylated form undergoes a simple two-state unfolding, the nonglycosylated species unfolds via a compact monomeric intermediate that is not a molten globule. Representative isothermal and thermal denaturation profiles show that glycosylation accounts for a stabilization of approximately 9 kcal/mol of the tetramer, whereas the difference in T(m) between the two forms is 26 degrees C. Computational studies on the glycan-protein interactions at the noncanonical interface of the protein show that quite a number of hydrogen bond and hydrophobic interactions stabilize the glycoprotein tetramer.
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