ArticlePloS one2009
Coupling between properties of the protein shape and the rate of protein folding.
Article in PloS one, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 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
23 citing papers in PubMed.
- Computational screening of natural compounds from traditional Persian medicinal plant for the finding of potential antidepressant.Scientific reports · 2026Article
- Evaluating the ciprofloxacin potentiation efficacy of repurposed drug flupentixol through efflux pump inhibition of pathogenic bacteria.Scientific reports · 2025Article
- Importance of Inter-residue Contacts for Understanding Protein Folding and Unfolding Rates, Remote Homology, and Drug Design.Molecular biotechnology · 2025Review
- Identifying potential monkeypox virus inhibitors: anFrontiers in cellular and infection microbiology · 2024Article
- Article
- Structural insights into the binding of zoledronic acid with RANKLFrontiers in molecular biosciences · 2022Article
- Comparative analysis of non structural protein 1 of SARS-CoV2 with SARS-CoV1 and MERS-CoV: AnJournal of molecular structure · 2021Article
- Study on the Influence of mRNA, the Genetic Language, on Protein Folding Rates.Frontiers in genetics · 2021Article
- Review
- How Quickly Do Proteins Fold and Unfold, and What Structural Parameters Correlate with These Values?Biomolecules · 2020Article
- Analysis of mutations leading to para-aminosalicylic acid resistance in Mycobacterium tuberculosis.Scientific reports · 2019Article
- Structural Basis of the Subcellular Topology Landscape ofFrontiers in microbiology · 2019Article
- Empirical power laws for the radii of gyration of protein oligomers.Acta crystallographica. Section D, Structural biology · 2016Article
- Article
- Network Properties of the Ensemble of RNA Structures.PloS one · 2015Article
- Diverse metastable structures formed by small oligomers of α-synuclein probed by force spectroscopy.PloS one · 2014Article
- Computational Studies of Beta Amyloid (Aβ42) with p75NTR Receptor: A Novel Therapeutic Target in Alzheimer's Disease.Advances in bioinformatics · 2014Article
- Dissecting the critical factors for thermodynamic stability of modular proteins using molecular modeling approach.PloS one · 2014Article
- Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
There are several important questions on the coupling between properties of the protein shape and the rate of protein folding. We have studied a series of structural descriptors intended for describing protein shapes (the radius of gyration, the radius of cross-section, and the coefficient of compactness) and their possible connection with folding behavior, either rates of folding or the emergence of folding intermediates, and compared them with classical descriptors, protein chain length and contact order. It has been found that when a descriptor is normalized to eliminate the influence of the protein size (the radius of gyration normalized to the radius of gyration of a ball of equal volume, the coefficient of compactness defined as the ratio of the accessible surface area of a protein to that of an ideal ball of equal volume, and relative contact order) it completely looses its ability to predict folding rates. On the other hand, when a descriptor correlates well with protein size (the radius of cross-section and absolute contact order in our consideration) then it correlates well with the logarithm of folding rates and separates reasonably well two-state folders from multi-state ones. The critical control for the performance of new descriptors demonstrated that the radius of cross-section has a somewhat higher predictive power (the correlation coefficient is -0.74) than size alone (the correlation coefficient is -0.65). So, we have shown that the numerical descriptors of the overall shape-geometry of protein structures are one of the important determinants of the protein-folding rate and mechanism.
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.