ArticlePloS one2011
A protein aggregation based test for screening of the agents affecting thermostability of proteins.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 17 citations in OpenAlex.
- Conserved Calcium-Binding Residues at the Ca-I Site Involved in Fructooligosaccharide Synthesis byACS omega · 2020Article
- Effect of Arginine on Chaperone-Like Activity of HspB6 and Monomeric 14-3-3ζ.International journal of molecular sciences · 2020Article
- Temperature stability of proteins: Analysis of irreversible denaturation using isothermal calorimetry.Proteins · 2017Article
- Structural implications of CaScientific reports · 2016Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To search for agents affecting thermal stability of proteins, a test based on the registration of protein aggregation in the regime of heating with a constant rate was used. The initial parts of the dependences of the light scattering intensity (I) on temperature (T) were analyzed using the following empiric equation: I = K(agg)(T-T(0))(2), where K(agg) is the parameter characterizing the initial rate of aggregation and T(0) is a temperature at which the initial increase in the light scattering intensity is registered. The aggregation data are interpreted in the frame of the model assuming the formation of the start aggregates at the initial stages of the aggregation process. Parameter T(0) corresponds to the moment of the origination of the start aggregates. The applicability of the proposed approach was demonstrated on the examples of thermal aggregation of glycogen phosphorylase b from rabbit skeletal muscles and bovine liver glutamate dehydrogenase studied in the presence of agents of different chemical nature. The elaborated approach to the study of protein aggregation may be used for rapid identification of small molecules that interact with protein targets.
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