bioRxivBiochemistryPreprint
Sticky salts: overbinding of monovalent cations to phosphorylations in all-atom forcefields
Jules MarieniD, Julie Puyo-FourtineiD, Chantal PrévostiD, Sophie Sacquin‐MoraiD, Élise Duboué-DijoniD
Abstract
Phosphorylation is a major post-translational modification, which is involved in the regulation of the dynamics and function of Intrinsically Disordered Proteins (IDPs). We recently characterized a phenomenon, which we termed n-Phosphate collaborations (nP-collabs), where bulk cations form stable bridges between several phosphoresidues in all-atom molecular dynamic simulations. nP-collabs were found to be sensitive to the combination of forcefields and cation types. Here, we attempt to assess the physical relevance of these nP-collabs by evaluating the strength of the cation/phosphate interaction through osmotic coefficient ({phi}) calculations on the model [Formula] and [Formula] salts, using different classical forcefields for phosphorylations. All force-fields were found to overestimate the strength of the interaction to various degrees. We thus designed new parameters for CHARMM36m and AmberFF99SB-ILDN using the Electronic Continuum Correction (ECC) approach, which provide remarkable agreement for{phi} values for both cation types and over a range of concentrations. We provide a preliminary test of these ECC parameters for phosphorylations by simulating the sevenfold-phosphorylated rhodopsin peptide 7PP and comparing secondary chemical shifts to experimental data. Conformational ensembles resulting from the ECC-derived phosphorylated forcefields display both qualitative and quantitative improvements with regard to full-charge forcefields. We thus conclude that long-lasting nP-collabs are artifacts for classical forcefields born from the lack of explicit polarization, and propose a possible computational strategy for the extensive parameterization of phosphorylations. The presence of long-lived nP-collabs in simulations produced using classical forcefields is therefore a serious concern for the accurate modelling of multiphosphorylated peptides and IDPs, which are at the center of research questions regarding neurodegenerative diseases such as Alzheimers or Parkinsons.
- assay: proteomics
- research focus: protein folding & dynamics
- approach: statistical model
- approach: mechanistic / dynamical model
- Citations
- 0
Reproducibility ledger
Nobody has reported trying to reproduce this paper yet. Did you replicate an experiment or run the code? Your report saves the next lab a week.
Sign in to file a reproducibility report.
Related papers
- nP-collabs: Investigating counterion mediated bridges in the multiply phosphorylated tau-R2 repeat
Jules Marien, Chantal Prévost, Sophie Sacquin‐Mora·Journal of Chemical Information and ModelingPeer-reviewed·Aug 2, 2024
- Force Field Limitations of All-Atom Continuous Constant pH Molecular Dynamics
Craig A. Peeples, Ruibin Liu, Jana Shen·The Journal of Physical Chemistry BPeer-reviewed·Nov 12, 2024
- Phosphorylation of disordered proteins tunes local and global intramolecular interactions
Emery T. Usher, Martin J. Fossat, Alex S. Holehouse·Biophysical JournalPeer-reviewed·Nov 13, 2024
- Effects of phosphorylation on protein backbone dynamics and conformational preferences
David Bickel, Wim Vranken·Journal of Chemical Theory and ComputationPeer-reviewed·Jun 3, 2024
- α-Helix stabilization by co-operative side chain charge-reinforced interactions to phosphoserine in a basic kinase-substrate motif
M. Batchelor, R. S. Dawber, … R. Bayliss·bioRxiv·Nov 27, 2021
- Effect of Phosphorylation on the Collision Cross Sections of Peptide Ions in Ion Mobility Spectrometry
K. Ogata, C.-H. Chang, Y. Ishihama·bioRxiv·Jun 15, 2020