Rescaling protein-protein interactions improves Martini 3 for flexible proteins in solution

F. Emil Thomasen (), Tórur Skaalum, Ashutosh Kumar, Sriraksha Srinivasan, Stefano Vanni () and Kresten Lindorff-Larsen ()
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F. Emil Thomasen: University of Copenhagen
Tórur Skaalum: University of Copenhagen
Ashutosh Kumar: University of Fribourg
Sriraksha Srinivasan: University of Fribourg
Stefano Vanni: University of Fribourg
Kresten Lindorff-Larsen: University of Copenhagen

Nature Communications, 2024, vol. 15, issue 1, 1-17

Abstract: Abstract Multidomain proteins with flexible linkers and disordered regions play important roles in many cellular processes, but characterizing their conformational ensembles is difficult. We have previously shown that the coarse-grained model, Martini 3, produces too compact ensembles in solution, that may in part be remedied by strengthening protein–water interactions. Here, we show that decreasing the strength of protein–protein interactions leads to improved agreement with experimental data on a wide set of systems. We show that the ‘symmetry’ between rescaling protein–water and protein–protein interactions breaks down when studying interactions with or within membranes; rescaling protein-protein interactions better preserves the binding specificity of proteins with lipid membranes, whereas rescaling protein-water interactions preserves oligomerization of transmembrane helices. We conclude that decreasing the strength of protein–protein interactions improves the accuracy of Martini 3 for IDPs and multidomain proteins, both in solution and in the presence of a lipid membrane.

Date: 2024
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DOI: 10.1038/s41467-024-50647-9

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