How Binding Affinity and Binding Specificity Map to Sequence Space.

Abstract read

In one paragraph

Article in Journal of molecular evolution, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it

0cells of the map it votes in

0citing papers in PubMed

–field-weighted citation impact

1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

David A LiberlesDepartment of Biology and Center for Computational Genetics and Genomics, Temple University, Philadelphia, PA, 19122, USA. daliberles@temple.edu.ORCID http://orcid.org/0000-0003-3487-8826

Michelle M MeyerDepartment of Biology, Boston College, Chestnut Hill, MA, 02467, USA.

Funding

Investigating Evolutionary Constraints on Regulatory RNAR35GM158403 · NIGMS · BOSTON COLLEGE · PI Michelle Margaret Meyer · 2025 to 2026

$775k

NIGMS NIH HHS R35 GM158403

6 · The paper itself

Abstract

Evidence suggests that molecular interactions may evolve differently for proteins compared to functional RNA. We suggest that for RNA interacting with other nucleic acid molecules, the selection of higher affinity interactions leads to greater specificity, whereas for proteins interacting with other proteins, there is a trade-off between selection for greater affinity vs. greater specificity. This difference arises from the nature of the molecular contacts driving intra- and inter-molecular interactions, with crucial roles for non-specific hydrophobic interactions driving affinity in proteins and for specific hydrogen bonds driving affinity and specificity in RNA. The implications of this difference are discussed.

Indexed as

ProteinsRNABinding SitesHydrogen BondingHydrophobic and Hydrophilic InteractionsModels, MolecularProtein BindingRNA-Binding ProteinsProteinsRNARNA-Binding ProteinsAptamerBinding affinityBinding specificityProtein foldingProtein interactionRNA interaction

Identifiers

PMID41910602

DOI10.1007/s00239-026-10308-5

PMCPMC13076558

What OpenQuestion holds

Textmetadata

LicenceCC BY

Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.