Search bioRxiv⌕ Search

bioRxiv · 10.64898/2026.10.05.756861

Frustration Quenching and Network Topology of the Energy Landscape as Primary Determinants of Protein-Ligand Binding Pose Prediction by Deep Learning Models

Abstract

Deep learning co-folding and docking models accurately predict ligand binding poses at orthosteric sites yet systematically underperform at allosteric pockets. Here, we demonstrate that this accuracy gap reflects a fundamental biophysical property of local energy landscape topology specifically, the magnitude of frustration quenching upon ligand binding rather than an intrinsic algorithmic defect. By evaluating leading co-folding and docking paradigms across curated benchmarks and large-scale uncurated datasets, we show that AI prediction success strongly tracks frustration quenching which the degree to which ligand binding relieves local energetic strain to form a steep energy funnel. Topologically, frustration-weighted residue interaction networks reveal that orthosteric pockets act as high-betweenness communication hubs embedded within contiguous, minimally frustrated pathways. In contrast, allosteric sites reside in low-betweenness peripheral regions with fragmented frustration profiles, presenting flatter, entropy-dominated landscapes that challenge structure prediction algorithms. Comparing generative diffusion with single-shot regression demonstrates that multi-pose sampling capacity is required to cross energy barriers and discover the frustration funnel, whereas joint receptor-ligand coordinate co-adaptation governs local optimization within the funnel. Collectively, this study reframes the allosteric "blind spot" as a quantitative property of energy landscape architecture rather than a defect of any specific predictive framework. We demonstrate that frustration quenching magnitude and structural network centrality serve as physical descriptors that define the intrinsic limits of AI performance, reframing AI accuracy from a benchmark metric into a physics-grounded quantitative reporter of macromolecular binding landscape architecture.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

Turano, L., Foley, B., Dennis, R., Gatlin, W., Verkhivker, G.. 2026-10-09. Frustration Quenching and Network Topology of the Energy Landscape as Primary Determinants of Protein-Ligand Binding Pose Prediction by Deep Learning Models. https://doi.org/10.64898/2026.10.05.756861

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related preprints

Cancers relax selection on charge at the mitochondrial complex I quinone cavity

Mitochondrial complex I translocates protons through hydrated channels whose connectivity and electrostatics are both defined by structure, but whether they are distinctly constrained is unknown. From a 2.39 cryo-EM structure modelling 2,945 ordered waters, we built the proton wire of the seven mtDNA-encoded ND subunits and scored all 40,166 missense substitutions on two near-orthogonal axes (r = 0.17): electrostatic shift at proton-loading sites, and topological disruption of the wire. Across 858 germline variant sites, loading sites (0.51) and cut vertices (0.67) are both depleted. In tumours only loading sites are enriched (1.42 TCGA, 1.67 PCAWG, 1.29 MSK-IMPACT), a 3.06-fold difference tested as a wire class tissue-type interaction (P = 3.6 10-). It survives adjustment for conservation, burial and coverage, and is concentrated in ND1 within 15 of the quinone cavity, not spread along the proton path. Selection separates charge from connectivity, without establishing a fitness benefit.

biophysics↗

Rugnux: from diffraction images to structure at synchrotrons and XFELs in one program

Rising data rates in macromolecular crystallography outpace multi-program pipelines on computing clusters. Rugnux, a single GPU-accelerated program, turns rotation or serial still diffraction images into merged data and an initial structure. At synchrotrons, results arrive seconds after the last image; on one workstation, 207 public datasets from 36 sources took a median of 15 s each, with deposition-quality. Serial XFEL data were processed faster than the collection rate, enabling real-time structure determination.

biophysics↗

Phase Separation of Intracellular Proteins Influences Synaptic Bistability

Synaptic bistability at the post synaptic density has been proposed to be the result of the nucleation and evaporation of receptor clusters. The exact biophysical mechanism underlying these inter-receptor attractions that can trigger nucleation remains to be elucidated. Emerging evidence demonstrates that numerous postsynaptic density submembrane proteins, that interact with various membrane receptors, can undergo phase separation, necessitating a revised conceptual model. By employing Langevin dynamics simulations of coarse-grained scaffold proteins and interacting membrane receptors, we study how phase transitions of scaffold proteins alter receptor clustering at the membrane. In our model, scaffold macromolecules can undergo phase separation and interact with receptor molecules at the model membranes. We observed that the presence of scaffold polymers across the membrane creates an attractive interaction between otherwise purely repulsive receptors. By systematically varying the number of receptors at the membrane, we dissected the coupling between receptor clustering and the phase behavior of scaffold macromolecules. We show that the propensity for receptor clustering is enhanced by the condensation of scaffold proteins. We then used two different scaffolds and systematically varied the interaction between them, to change the spatial organization of two condensed phases w.r.t. one another. Interestingly, we observed that receptor clustering can be reduced by co-phase separation of scaffold macromolecules, indicating the role of competing interactions in receptor clustering. Our work advances understanding of receptor-mediated signaling and phase separation, providing insights into cellular compartmentalization and biochemical regulation at the synapse.

biophysics↗