ArticleJournal of molecular modeling2014
Analysis of the structure and dynamics of human serum albumin.
Article in Journal of molecular modeling, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Observing Picomolar Protein Unfolding Using Resonance Light Scattering.Biomolecules · 2025Article
- Ligand-human serum albumin analysis: the near-UV CD and UV-Vis spectroscopic studies.Naunyn-Schmiedeberg's archives of pharmacology · 2025Article
- Optimizing Excipient Properties to Prevent Aggregation in Biopharmaceutical Formulations.Journal of chemical information and modeling · 2024Article
- Investigating the Interaction of an Anticancer Nucleolipidic Ru(III) Complex with Human Serum Proteins: A Spectroscopic Study.Molecules (Basel, Switzerland) · 2023Article
- Characterization of Synovial Fluid Components: Albumin-Chondroitin Sulfate Interactions Seen through Molecular Dynamics.Materials (Basel, Switzerland) · 2022Article
- Effect of Ion and Binding Site on the Conformation of Chosen Glycosaminoglycans at the Albumin Surface.Entropy (Basel, Switzerland) · 2022Article
- Lipoic Acid Restores Binding of Zinc Ions to Human Serum Albumin.Frontiers in chemistry · 2022Article
- Fusion of engineered albumin with factor IX Padua extends half-life and improves coagulant activity.British journal of haematology · 2021Article
- A comparative study of synthetic winged peptides for absolute protein quantification.Scientific reports · 2021Article
- The Binding of Free and Sulfated Androstenone in the Plasma of the Boar.Animals : an open access journal from MDPI · 2021Article
- Oxidized Albumin as a Mediator of Kidney Disease.Antioxidants (Basel, Switzerland) · 2021Review
- Article
- Radiolabeling of Human Serum Albumin With Terbium-161 Using Mild Conditions and Evaluation ofFrontiers in medicine · 2021Article
- Article
- Toxicity profile of honey and ghee, when taken together in equal ratio.Toxicology reports · 2020Article
- Multiple binding modes of ibuprofen in human serum albumin identified by absolute binding free energy calculations.Physical chemistry chemical physics : PCCP · 2016Article
- Article
- Albumin in chronic liver disease: structure, functions and therapeutic implications.Hepatology international · 2016Review
Corrections and comments
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Authors and funding
1 author.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human serum albumin (HSA) is a biologically relevant protein that binds a variety of drugs and other small molecules. No less than 50 structures are deposited in the RCSB Protein Data Bank (PDB). Based on these structures, we first performed a clustering analysis. Despite the diversity of ligands, only two well defined conformations are detected, with a deviation of 0.46 nm between the average structures of the two clusters, while deviations within each cluster are smaller than 0.08 nm. Those two conformations are representative of the apoprotein and the HSA-myristate complex already identified in previous literature. Considering the structures within each cluster as a representative sample of the dynamical states of the corresponding conformation, we scrutinize the structural and dynamical differences between both conformations. Analysis of the fluctuations within each cluster set reveals that domain II is the most rigid one and better matches both structures. Then, taking this domain as reference, we show that the structural difference between both conformations can be expressed in terms of twist and hinge motions of domains I and III, respectively. We also characterize the dynamical difference between conformations by computing correlations and principal components for each set of dynamical states. The two conformations display different collective motions. The results are compared with those obtained from the trajectories of short molecular dynamics simulations, giving consistent outcomes. Let us remark that, beyond the relevance of the results for the structural and dynamical characterization of HAS conformations, the present methodology could be extended to other proteins in the PDB archive.
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