Intrinsically Disordered Protein: Difference between revisions

It appears that hundreds of IDPs that remain soluble after boiling protect folded proteins against heat-denaturation, aggregation, and loss of activity from dessication or organic solvents<ref name="hero">PMID: 32163402</ref>. They also appear to suppress neurodegeneration and extend lifespan<ref name="hero" />. They have been termed "heat-resistant obscure" (hero) proteins<ref name="hero" />. Their isoelectric pH's (pI's) form a bimodal distribution, so that most are negatively or positively charged at neutral pH<ref name="hero" />. Examples include six human proteins that were studied in detail: [https://www.uniprot.org/uniprot/Q8NC51 SERF2] (length 59), [https://www.uniprot.org/uniprot/Q9BUW7 C9orf16] (length 83), [https://www.uniprot.org/uniprot/Q9UNZ5 C19ofr53] (length 99), [https://www.uniprot.org/uniprot/Q00994 BEX3] (length 111), [https://www.uniprot.org/uniprot/O00193 C11orf58] (length 183), and [https://www.uniprot.org/uniprot/Q8NC51 SERBP1] (length 408)<ref name="hero" />. In several test cases, scrambling the sequences of these proteins did not diminish their protective effects<ref name="hero" />. Their protective activity appears to depend on their high charge density and length, but not on a specific sequence.