ArticleChemistry (Weinheim an der Bergstrasse, Germany)2015
"Invisible" conformers of an antifungal disulfide protein revealed by constrained cold and heat unfolding, CEST-NMR experiments, and molecular dynamics calculations.
Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 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
33 citing papers in PubMed, 46 citations in OpenAlex.
- Small Disulfide Proteins with Antifungal Impact: NMR Experimental Structures as Compared to Models of Alphafold Versions.International journal of molecular sciences · 2025Article
- Dynamic Structures of Bioactive Proteins as Determined by Nuclear Magnetic Resonance.International journal of molecular sciences · 2023Article
- Hard nut to crack: Solving the disulfide linkage pattern of the Neosartorya (Aspergillus) fischeri antifungal protein 2.Protein science : a publication of the Protein Society · 2023Article
- The influence of random-coil chemical shifts on the assessment of structural propensities in folded proteins and IDPs.RSC advances · 2023Review
- DMSO-Induced Unfolding of the Antifungal Disulfide Protein PAF and Its Inactive Variant: A Combined NMR and DSC Study.International journal of molecular sciences · 2023Article
- Characterization and expression of fungal defensin inFrontiers in microbiology · 2023Article
- The Importance of MgChemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
- Protein-Calixarene Complexation: From Recognition to Assembly.Accounts of chemical research · 2022Article
- Solution Structure, Dynamics, and New Antifungal Aspects of the Cysteine-Rich Miniprotein PAFC.International journal of molecular sciences · 2021Article
- Ensemble-Based Analysis of the Dynamic Allostery in the PSD-95 PDZ3 Domain in Relation to the General Variability of PDZ Structures.International journal of molecular sciences · 2020Article
- Two small, cysteine-rich and cationic antifungal proteins from Penicillium chrysogenum: A comparative study of PAF and PAFB.Biochimica et biophysica acta. Biomembranes · 2020Review
- Characterization of a fungal competition factor: Production of a conidial cell-wall associated antifungal peptide.PLoS pathogens · 2020Article
- Nutrient Excess Triggers the Expression of theMicroorganisms · 2019Article
- Cysteine-Rich Antifungal Proteins from Filamentous Fungi are Promising Bioactive Natural Compounds in Anti-Israel journal of chemistry · 2019Review
- Article
- Membrane Sphingolipids Regulate the Fitness and Antifungal Protein Susceptibility ofFrontiers in microbiology · 2019Article
- Different modes of barrel opening suggest a complex pathway of ligand binding in human gastrotropin.PloS one · 2019Article
- Structure and Synthesis of Antifungal Disulfide β-Strand Proteins from Filamentous Fungi.Microorganisms · 2018Review
- Rational Design and Biotechnological Production of Novel AfpB-PAF26 Chimeric Antifungal Proteins.Microorganisms · 2018Article
- Multiple frequency saturation pulses reduce CEST acquisition time for quantifying conformational exchange in biomolecules.Journal of biomolecular NMR · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Transition between conformational states in proteins is being recognized as a possible key factor of function. In support of this, hidden dynamic NMR structures were detected in several cases up to populations of a few percent. Here, we show by two- and three-state analysis of thermal unfolding, that the population of hidden states may weight 20-40 % at 298 K in a disulfide-rich protein. In addition, sensitive (15) N-CEST NMR experiments identified a low populated (0.15 %) state that was in slow exchange with the folded PAF protein. Remarkably, other techniques failed to identify the rest of the NMR "dark matter". Comparison of the temperature dependence of chemical shifts from experiments and molecular dynamics calculations suggests that hidden conformers of PAF differ in the loop and terminal regions and are most similar in the evolutionary conserved core. Our observations point to the existence of a complex conformational landscape with multiple conformational states in dynamic equilibrium, with diverse exchange rates presumably responsible for the completely hidden nature of a considerable fraction.
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.