Journal
MEMBRANES
Volume 12, Issue 8, Pages -Publisher
MDPI
DOI: 10.3390/membranes12080773
Keywords
membrane binding; intrinsically disordered proteins; membrane-association propensity; amphipathic helix; intrinsically disordered regions
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Funding
- National Institutes of Health [GM118091, AI119178]
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This study identified the membrane-association characteristics of intrinsically disordered regions (IDRs) in proteins and developed a web server called ReSMAP for predicting residue-specific membrane-association propensities from IDR sequences.
The functional processes of many proteins involve the association of their intrinsically disordered regions (IDRs) with acidic membranes. We have identified the membrane-association characteristics of IDRs using extensive molecular dynamics (MD) simulations and validated them with NMR spectroscopy. These studies have led to not only deep insight into functional mechanisms of IDRs but also to intimate knowledge regarding the sequence determinants of membrane-association propensities. Here we turned this knowledge into a web server called ReSMAP, for predicting the residue-specific membrane-association propensities from IDR sequences. The membrane-association propensities are calculated from a sequence-based partition function, trained on the MD simulation results of seven IDRs. Robustness of the prediction is demonstrated by leaving one IDR out of the training set. We anticipate there will be many applications for the ReSMAP web server, including rapid screening of IDR sequences for membrane association.
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