ArticlePloS one2012
Evidence for water-tuned structural differences in proteins: an approach emphasizing variations in local hydrophilicity.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
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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.
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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.
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Who cites it
16 citing papers in PubMed, 79 citations in OpenAlex.
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- Human Serum Albumin Loaded with Fatty Acids Reveals Complex Protein-Ligand Thermodynamics and Boleadora-Type Solution Dynamics Leading to Gelation.The journal of physical chemistry. B · 2025Article
- Periodate-Mediated Cross-Linking for the Preparation of Catechol Conjugated Albumin Nanoparticles Used for in Vitro Drug Delivery.ACS applied bio materials · 2025Article
- Ru(II) Complexes with 3,4-Dimethylphenylhydrazine: Exploring In Vitro Anticancer Activity and Protein Affinities.Biomolecules · 2025Article
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- Macro- and Nanoscale Effect of Ethanol on Bovine Serum Albumin Gelation and Naproxen Release.International journal of molecular sciences · 2022Article
- Optimization of the Physical, Optical and Mechanical Properties of Composite Edible Films of Gelatin, Whey Protein and Chitosan.Molecules (Basel, Switzerland) · 2022Article
- Evaluating the Merit of a Syringol Derived Fluorophore as a Charge Transfer Probe for Detection of Serum Albumins.Journal of photochemistry and photobiology. A, Chemistry · 2022Article
- Molecular-Level Release of Coumarin-3-Carboxylic Acid and Warfarin-Derivatives from BSA-Based Hydrogels.Pharmaceutics · 2021Article
- Identification of Patients with Pancreatic Cancer by Electron Paramagnetic Resonance Spectroscopy of Fatty Acid Binding to Human Serum Albumin.ACS pharmacology & translational science · 2020Article
- Dual luminescent charge transfer probe for quantitative detection of serum albumin in aqueous samples.Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy · 2020Article
- The Effect of Ethanol on Gelation, Nanoscopic, and Macroscopic Properties of Serum Albumin Hydrogels.Molecules (Basel, Switzerland) · 2020Article
- Novel Tamoxifen Nanoformulations for Improving Breast Cancer Treatment: Old Wine in New Bottles.Molecules (Basel, Switzerland) · 2020Review
- Maleimido-proxyl as an EPR spin label for the evaluation of conformational changes of albumin.European biophysics journal : EBJ · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We present experimental evidence for the significant effect that water can have on the functional structure of proteins in solution. Human (HSA) and Bovine Serum Albumin (BSA) have an amino acid sequence identity of 75.52% and are chosen as model proteins. We employ EPR-based nanoscale distance measurements using double electron-electron resonance (DEER) spectroscopy and both albumins loaded with long chain fatty acids (FAs) in solution to globally (yet indirectly) characterize the tertiary protein structures from the bound ligands' points of view. The complete primary structures and crystal structures of HSA and as of recently also BSA are available. We complement the picture as we have recently determined the DEER-derived solution structure of HSA and here present the corresponding BSA solution structure. The characteristic asymmetric FA distribution in the crystal structure of HSA can surprisingly be observed by DEER in BSA in solution. This indicates that the BSA conformational ensemble in solution seems to be narrow and close to the crystal structure of HSA. In contrast, for HSA in solution a much more symmetric FA distribution was found. Thus, conformational adaptability and flexibility dominate in the HSA solution structure while BSA seems to lack these properties. We further show that differences in amino acid hydropathies of specific structural regions in both proteins can be used to correlate the observed difference in the global (tertiary) solution structures with the differences on the primary structure level.
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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.