ReSMAP: predictor for residue-specific membrane-association propensities of intrinsially disordered proteins

Method at a Glance

ReSMAP is a sequence-based method for predicting the Residue-Specific Membrane-Association Propensities of intrinsically disordered proteins. The prediction is made from a sequence-based partition function. Every residue i contributes a multiplicative Boltzmann factor qi; |i - n| to the statistical weight for residue n’s membrane association. qi; |i - n| depends on the amino-acid type of residue i and the sequence distance |i – n|. We only distinguish three types of amino acids: positively charged (K, R, and the N-terminus), negatively charged (D, E, and the C-terminus), and neutral (all other amino acids). The parameters of the partition function were optimized against data from molecular dynamics simulations of disordered proteins associating with acidic membranes. The images above illustrate the ChiZ protein associated with a POPG:POPE membrane (left), and the agreement between ReSMAP prediction and tthe molecular dynamics simulation data for membrane-association propensity (P) (right).

    Qin, S.; Hicks, A.; Dey, S.; Prasad, R.; Zhou, H.-X. ReSMAP: Web Server for Predicting Residue-Specific Membrane-Association Propensities of Intrinsically Disordered Proteins. Membranes 2022, 12, 773. pdf Supplementary Information

Enter the IDP (or IDR) sequence to get predicted membrane-association propensities

  • Type a name for referencing your submission:
  • Paste the amino-acid sequence (in one-letter code, ok with space and digits):

  • Is there an amphipathic helix stably bound to membrane? (Proteins with amphipathic helix have a different set of parameters.)

  • Output example

  • Download software

  • Other servers