BENDER, a dataset of 11,533 IDP sequences spanning 13 taxonomic groups, each simulated under CALVADOS-2 molecular dynamics and annotated with ensemble-level geometric and novel contact-network properties, suggests that hub topology in disordered protein contact networks is a conserved physical feature of sequence-encoded disorder rather than an evolutionary contingency.
Abstract
Intrinsically disordered proteins and regions are found across all kingdoms of life, yet the computational characterisation of their conformational ensembles has remained almost entirely confined to the human proteome. Whether the force fields used to generate them remain accurate for taxonomically distant organisms, and whether the sequence-ensemble relationships they reveal transfer across taxa well enough to improve prediction on phylogenetically held-out organisms, are open questions. Here we introduce BENDER, a dataset of 11,533 IDP sequences spanning 13 taxonomic groups, each simulated under CALVADOS-2 molecular dynamics and annotated with ensemble-level geometric and novel contact-network properties, together with per-sequence pi–pi and cation–pi contact frequencies linked to phase-separation propensity. We show that CALVADOS-2 ensembles agree strongly with an orthogonal structural reference across the full dataset, with both held-out taxa performing above the dataset median, and that direct comparison against a second independently parameterized force field reveals no systematic scaling-exponent bias. We find that cross-taxon training data improves out-of-distribution ensemble prediction in two independent architectures despite training on one-third the data. Positive degree assortativity is conserved across all taxonomic groups, suggesting that hub topology in disordered protein contact networks is a conserved physical feature of sequence-encoded disorder rather than an evolutionary contingency.
Although protein toxins represent valuable pharmacological templates, predicting toxicity directly from primary sequences is inherently challenging because of their evolutionary dynamics. Active toxins and their benign homologues frequently share identical structural scaffolds and differ by only a few key residue subst...
Seongmin Kim, Min-Seok Kim, Chungoo Park· bioRxiv· 0 citations
BindCORE is introduced, an ensemble-aware deep learning framework that integrates global, local, and pairwise biophysical descriptors to predict interaction sites within IDRs and shows that conformational ensembles contain interpretable determinants of LIP and MoRF binding residues.
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The discordance persists: pLDDT correlates positively with PUNCH2 disorder in random and de novo proteins and negatively with β-strand fraction, opposite to the conserved and disordered baselines, a concrete failure mode that protein designers and other working on sequences remote in sequence space should be aware of w...
Lars A. Eicholt, Lasse Middendorf· bioRxiv· 0 citations
Pi-Ensemble (Predicting Interpolated Ensemble), a sequence-guided framework for generating protein conformational ensembles interpolating between two structural anchor states, provides an extensible framework for studying protein flexibility, guiding adaptive sampling, and accelerating mechanistic investigations of pro...
Hassan Nadeem, D. Kleiman, Yu-Ming Zhou et al.· bioRxiv· 0 citations
An improved force field is developed, derived from its parent, Amber ff24EXP-GA, and its evaluation against Amber ff14SB and other contemporary force fields, such as CHARMM36m, in capturing the empirically determined conformational properties of unfolded systems: short peptides that serve as model systems for IDPs, and...
Protein fitness prediction is essential for protein engineering. Recent fitness-landscape benchmarks such as FLIP2 have shown that methods performing well under conventional train–test splits can fail when the test set is shifted out of distribution (OOD), including mutations at unseen positions and variants from unsee...