ArticleProteomics insights2013
Mutational effect of structural parameters on coiled-coil stability of proteins.
Article in Proteomics insights, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed.
- Determining the minimal amount of DMSO necessary to stabilize the Angiomotin lipid binding domain.Indiana University journal of undergraduate research · 2024Article
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2 authors.
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Abstract
Understanding the parameters that influence the melting temperature of coiled-coils (CC) and their stability is very important. We have analyzed 45 CC mutants of DNA binding protein, electron transport protein, hydrolase, oxidoreductase, and transcription factors. Many mutants have been observed at Tm = 40 °C-60 °C with ΔS = 9-11 kcal/°C mol, ΔG = -400 to -450 kcal/mol, and Keq = 0.98-1.03. The multiple regression analysis of Tm reveals that influences of thermodynamic parameters are strong (R = 0.97); chemical parameters are moderate (R = 0.63); and the geometrical parameters are negligible (R = 0.19). The combination of all these three parameters exhibits a little higher influence on Tm (R = 0.98). From the analysis, it has been concluded that the thermodynamic parameters alone are very important in stability studies on protein coil mutants. Besides, the derived regression model would have been useful for the reliable prediction of the melting temperature of coil mutants.
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