ArticleProteins2022
The dynamic basis of structural order in proteins.
Article in Proteins, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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.
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.
Who cites it
3 citing papers in PubMed, 6 citations in OpenAlex.
- The Spatial Distribution of Local Mobility in Folded Proteins.The journal of physical chemistry. B · 2026Article
- Techniques for Bioinformatic Applications in Protein Dynamics.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Application of artificial intelligence and machine learning techniques to the analysis of dynamic protein sequences.Proteins · 2024Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
We compare the sequences of folded and intrinsically disordered proteins (IDPs), using bioinformatic methods recently developed to study protein dynamic properties. We demonstrate that the two classes of sequences are organized in diametrically opposite ways with respect to long-length-scale dynamic properties. We further demonstrate a statistically significant difference between the amino acid compositions of folded and disordered proteins, which is expressed in dynamic properties. Our results indicate that the long-length-scale properties of sequences are critical in determining whether proteins are able to fold, and, more generally, that they are central to an understanding of protein physics. They further provide a physical basis for the empirically observed differences in amino acid composition between folded and IDPs.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.