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Biology Chemistry

4
Open Unknowns
0
Cross-Domain Bridges
4
Active Hypotheses

Open Unknowns (4)

Unknown Do lipid rafts exist as stable, nanoscale liquid-ordered domains in living cell membranes, and if so, what is their functional role in receptor clustering and signal transduction? u-lipid-raft-functional-role-signaling
Unknown How rugged are protein fitness landscapes — what fraction of beneficial mutations are epistatic (context-dependent), and can the landscape topology be predicted from protein structure well enough to guide directed evolution without exhaustive experimental measurement? u-protein-fitness-landscape-epistasis-ruggedness
Unknown What minimum replication fidelity is required for non-enzymatic RNA replication to sustain a functional RNA world — and can plausible prebiotic chemistry achieve this fidelity threshold under realistic environmental conditions? u-rna-world-nonenzymatic-replication-fidelity
Unknown What fraction of silent biosynthetic gene clusters in soil actinobacteria encode genuinely novel antibiotic scaffolds with activity against multidrug-resistant pathogens — and what are the minimal conditions (growth signals, co-culture, epigenetic modification) needed to reliably activate silent clusters in situ? u-silent-bgc-activation-novel-antibiotics

Active Hypotheses

Hypothesis Lipid raft phase separation concentrates GPI-anchored proteins and receptor tyrosine kinases into signaling-competent nanoclusters, with raft lifetime and size controlled by the 2D Cahn-Hilliard free energy parameters — specifically, cholesterol concentration sets the proximity to the phase boundary. high
Hypothesis Machine learning models trained on deep mutational scanning (DMS) data can predict the fitness of multi-mutation combinations with accuracy sufficient to identify the global fitness maximum in a protein landscape with up to 5 simultaneous mutations, replacing 3-5 rounds of directed evolution with a single round of computational screening. high
Hypothesis The ribosome is a frozen accident of the RNA world: the peptidyl transferase center evolved as a ribozyme before proteins existed, and the gradual replacement of ribozyme catalysts by protein enzymes occurred via a Darwinian takeover in which RNA retained only the reactions it could not be displaced from. high
Hypothesis The modular architecture of PKS and NRPS assembly lines evolves primarily by horizontal gene transfer and domain shuffling rather than point mutation — and the combinatorial space of viable module orderings is much larger than currently sampled by evolution, making synthetic PKS/NRPS libraries a rich source of novel bioactive scaffolds with predicted structural diversity. high

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Generated 2026-05-10 · USDR Dashboard