Arash Firouzbakht, Austin Haider, Kari Gaalswyk, Sepehr Alaeen, Kingshuk Ghosh, Martin Gruebele
Intrinsically disordered proteins (IDPs) that lie close to the empirical boundary separating IDPs and folded proteins in Uversky's charge-hydropathy plot may behave as "marginal IDPs" and sensitively switch conformation upon changes in environment (temperature, crowding, and charge screening), sequence, or both. In our search for such a marginal IDP, we selected Huntingtin-interacting protein K (HYPK) near that boundary as a candidate; PKIα, also near that boundary, has lower secondary structure propensity; and Crk1, just across the boundary on the folded side, has higher secondary structure propensity...
April 30, 2024: Proceedings of the National Academy of Sciences of the United States of America