Abstract：
:The Anfinsen hypothesis, the demonstration of which led to the Nobel prize in Chemistry, posits that all information required to determine a proteins' three dimensional structure is contained within its amino acid sequence. This suggests that it should be possible, in theory, to fold any protein in vitro. In practice, however, protein production by refolding is challenging because suitable refolding conditions must be empirically determined for each protein and can be painstaking. Here we demonstrate, using a variety of proteins, that differential scanning fluorimetry (DSF) can be used to determine and optimize conditions that favor proper protein folding in a rapid and high-throughput fashion. The resulting method, which we deem DSF guided refolding (DGR), thus enables the production of aggregation-prone and disulfide-containing proteins by refolding from E. coli inclusion bodies, which would not normally be amenable to production in bacteria.
journal_name
Sci Repjournal_title
Scientific reportsauthors
Biter AB,de la Peña AH,Thapar R,Lin JZ,Phillips KJdoi
10.1038/srep18906subject
Has Abstractpub_date
2016-01-19 00:00:00pages
18906issn
2045-2322pii
srep18906journal_volume
6pub_type
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