ArticleBiophysical journal2001
The conformation of serum albumin in solution: a combined phosphorescence depolarization-hydrodynamic modeling study.
Article in Biophysical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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41 citing papers in PubMed, 262 citations in OpenAlex.
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- AC electrokinetic immobilization of organic dye molecules.Analytical and bioanalytical chemistry · 2020Article
- The Effect of Ethanol on Gelation, Nanoscopic, and Macroscopic Properties of Serum Albumin Hydrogels.Molecules (Basel, Switzerland) · 2020Article
- Hemodynamic and Systemic Effects of Albumin in Patients with Advanced Liver Disease.Current hepatology reports · 2020Review
- Protein Binding Characteristics of the Principal Green Tea Catechins: A QCM Study Comparing Crude Extract to Pure EGCG.Biochemistry research international · 2019Article
- Freely suspended perforated polymer nanomembranes for protein separations.Scientific reports · 2018Article
- Continuous Fluorescence Depletion Anisotropy Measurement of Protein Rotation.Journal of fluorescence · 2018Article
- The interactions of CdTe quantum dots with serum albumin and subsequent cytotoxicity: the influence of homologous ligands.Toxicology research · 2018Article
- Effect of Aggregation on the Hydrodynamic Properties of Bovine Serum Albumin.Pharmaceutical research · 2017Article
- Metal nanoparticles: understanding the mechanisms behind antibacterial activity.Journal of nanobiotechnology · 2017Review
- Sensitive Analysis of Protein Adsorption to Colloidal Gold by Differential Centrifugal Sedimentation.Analytical chemistry · 2017Article
- A centrifugation-based physicochemical characterization method for the interaction between proteins and nanoparticles.Nature communications · 2016Article
- Diazaoxatriangulenium: synthesis of reactive derivatives and conjugation to bovine serum albumin.Organic & biomolecular chemistry · 2016Article
- The "long tail" of the protein tumbling correlation function: observation by (1)H NMR relaxometry in a wide frequency and concentration range.Journal of biomolecular NMR · 2015Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
There is a striking disparity between the heart-shaped structure of human serum albumin (HSA) observed in single crystals and the elongated ellipsoid model used for decades to interpret the protein solution hydrodynamics at neutral pH. These two contrasting views could be reconciled if the protein were flexible enough to change its conformation in solution from that found in the crystal. To investigate this possibility we recorded the rotational motions in real time of an erythrosin-bovine serum albumin complex (Er-BSA) over an extended time range, using phosphorescence depolarization techniques. These measurements are consistent with the absence of independent motions of large protein segments in solution, in the time range from nanoseconds to fractions of milliseconds, and give a single rotational correlation time phi(BSA, 1 cP, 20 degrees C) = 40 +/- 2 ns. In addition, we report a detailed analysis of the protein hydrodynamics based on two bead-modeling methods. In the first, BSA was modeled as a triangular prismatic shell with optimized dimensions of 84 x 84 x 84 x 31.5 A, whereas in the second, the atomic-level structure of HSA obtained from crystallographic data was used to build a much more refined rough-shell model. In both cases, the predicted and experimental rotational diffusion rate and other hydrodynamic parameters were in good agreement. Therefore, the overall conformation in neutral solution of BSA, as of HSA, should be rigid, in the sense indicated above, and very similar to the heart-shaped structure observed in HSA crystals.
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