ArticleBiophysical journal2005
Oligomerization endows enormous stability to soybean agglutinin: a comparison of the stability of monomer and tetramer of soybean agglutinin.
Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed, 44 citations in OpenAlex.
- JA-responsive R2R3-type MYB transcription factor OsMYB4P confers broad-spectrum antiviral immunity in rice.Plant biotechnology journal · 2025Article
- CRISPR/Cas9-mediated inactivation of the soybean agglutininFrontiers in plant science · 2025Article
- Computational insights into the circular permutation roles on ConA binding and structural stability.Current research in structural biology · 2024Article
- Nanoscale materials for probing the biological functions of the glycocalyx.Glycobiology · 2016Review
- Impact of glycosylation on stability, structure and unfolding of soybean agglutinin (SBA): an insight from thermal perturbation molecular dynamics simulations.Glycoconjugate journal · 2015Article
- A quaternary mechanism enables the complex biological functions of octameric human UDP-glucose pyrophosphorylase, a key enzyme in cell metabolism.Scientific reports · 2015Article
- Urea Unfolding Study of E. coli Alanyl-tRNA Synthetase and Its Monomeric Variants Proves the Role of C-Terminal Domain in Stability.Journal of amino acids · 2015Article
- Square-wave voltammetry assays for glycoproteins on nanoporous gold.Journal of electroanalytical chemistry (Lausanne, Switzerland) · 2014Article
- Thermal, chemical and pH induced unfolding of turmeric root lectin: modes of denaturation.PloS one · 2014Article
- Monomeric banana lectin at acidic pH overrules conformational stability of its native dimeric form.PloS one · 2013Article
- Density variant glycan microarray for evaluating cross-linking of mucin-like glycoconjugates by lectins.Journal of the American Chemical Society · 2012Article
- High-yield expression of recombinant soybean agglutinin in plants using transient and stable systems.Transgenic research · 2011Article
- Camptosemin, a tetrameric lectin of Camptosema ellipticum: structural and functional analysis.European biophysics journal : EBJ · 2010Article
- Rational design of multiple TB antigens TB10.4 and TB10.4-Ag85B as subunit vaccine candidates against Mycobacterium tuberculosis.Pharmaceutical research · 2010Article
- Attributes of glycosylation in the establishment of the unfolding pathway of soybean agglutinin.Biophysical journal · 2007Article
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2 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Soybean agglutinin is a tetrameric legume lectin, each of whose subunits are glycosylated. This protein shows a very high degree of stability when compared to the other proteins of the same family. In a previous work, it was shown that the unusual stability of the protein is due to a high degree of subunit interactions. In this study we present the thermodynamic parameters for the stability of soybean agglutinin monomer. The monomeric species is found at pH 2 and below which it is most populated at pH 1.9, as evident from size-exclusion chromatographic and dynamic light scattering studies. The analyses of circular dichroism and fluorescence spectroscopy suggest that the monomer is well folded, and that it has certain characteristic features when compared to its tetrameric counterpart. The conformational stabilities of the tetramer and the monomer at the temperature of their maximum stabilities (310 K) are 59.2 kcal/mol and 9.8 kcal/mol, respectively, indicating that oligomerization contributes significantly to the stability of the native molecule. Also, the T(g) difference for the two forms of the protein is approximately 40 K, whereas the difference in DeltaC(p) is only 1.6 kcal/mol/K. This suggests that the major hydrophobic core is present in the monomer itself, and that oligomerization involves mainly ionic interactions.
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