ArticleProceedings of the National Academy of Sciences of the United States of America2013
Stabilization of a protein conferred by an increase in folded state entropy.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. 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.
- Evolution of alcohol oxidase for improved methanol bioconversion and formaldehyde tolerance.Synthetic and systems biotechnology · 2027Article
- Molecular analysis of 3D domain swapping in the acylphosphatase from Escherichia coli.Acta crystallographica. Section D, Structural biology · 2026Article
- Structural and energetic analysis of stabilizing indel mutations.bioRxiv : the preprint server for biology · 2024Article
- Analyzing Current Trends and Possible Strategies to Improve Sucrose Isomerases' Thermostability.International journal of molecular sciences · 2023Review
- Structural Dynamics Predominantly Determine the Adaptability of Proteins to Amino Acid Deletions.International journal of molecular sciences · 2023Article
- Enhancing response of a protein conformational switch by using two disordered ligand binding domains.Frontiers in molecular biosciences · 2023Article
- Ionic Liquid-Based Strategy for Predicting Protein Aggregation Propensity and Thermodynamic Stability.JACS Au · 2022Article
- A topological refactoring design strategy yields highly stable granulopoietic proteins.Nature communications · 2022Article
- Article
- Modeling of the thermal properties of SARS-CoV-2 S-protein.Frontiers in molecular biosciences · 2022Article
- The Importance of Weakly Co-Evolving Residue Networks in Proteins is Revealed by Visual Analytics.Frontiers in bioinformatics · 2022Article
- Deletion of the Loop Linking Two Domains of Exo-Inulinase InuAMN8 Diminished the Enzymatic Thermo-Halo-Alcohol Tolerance.Frontiers in microbiology · 2022Article
- Mechanistic basis for ubiquitin modulation of a protein energy landscape.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Benefits and constrains of covalency: the role of loop length in protein stability and ligand binding.Scientific reports · 2020Article
- Gradual compaction of the nascent peptide during cotranslational folding on the ribosome.eLife · 2020Article
- Exploring conformational preferences of proteins: ionic liquid effects on the energy landscape of avidin.Chemical science · 2020Article
- Catalytic and structural effects of flexible loop deletion in organophosphorus hydrolase enzyme: A thermostability improvement mechanism.Journal of biosciences · 2020Article
- Site-specific amino acid substitution in dodecameric peptides determines the stability and unfolding of c-MYC quadruplex promoting apoptosis in cancer cells.Nucleic acids research · 2018Article
- Entropic stabilization of a deubiquitinase provides conformational plasticity and slow unfolding kinetics beneficial for functioning on the proteasome.Scientific reports · 2017Article
- Impacts of the charged residues mutation S48E/N62H on the thermostability and unfolding behavior of cold shock protein: insights from molecular dynamics simulation with Gō model.Journal of molecular modeling · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Entropic stabilization of native protein structures typically relies on strategies that serve to decrease the entropy of the unfolded state. Here we report, using a combination of experimental and computational approaches, on enhanced thermodynamic stability conferred by an increase in the configurational entropy of the folded state. The enhanced stability is observed upon modifications of a loop region in the enzyme acylphosphatase and is achieved despite significant enthalpy losses. The modifications that lead to increased stability, as well as those that result in destabilization, however, strongly compromise enzymatic activity, rationalizing the preservation of the native loop structure even though it does not provide the protein with maximal stability or kinetic foldability.
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.