ArticleCurrent protocols in protein science2015
Analysis of protein stability and ligand interactions by thermal shift assay.
Article in Current protocols in protein science, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 296 papers.
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Who cites it
296 citing papers in PubMed.
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236 more citing papers are in PubMed but not listed here.
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Authors and funding
2 authors.
Funding
Abstract
Purification of recombinant proteins for biochemical assays and structural studies is time-consuming and presents inherent difficulties that depend on the optimization of protein stability. The use of dyes to monitor thermal denaturation of proteins with sensitive fluorescence detection enables rapid and inexpensive determination of protein stability using real-time PCR instruments. By screening a wide range of solution conditions and additives in a 96-well format, the thermal shift assay easily identifies conditions that significantly enhance the stability of recombinant proteins. The same approach can be used as an initial low-cost screen to discover new protein-ligand interactions by capitalizing on increases in protein stability that typically occur upon ligand binding. This unit presents a methodological workflow for small-scale, high-throughput thermal denaturation of recombinant proteins in the presence of SYPRO Orange dye.
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