ArticleBiophysical journal2009
Interfacial water at protein surfaces: wide-line NMR and DSC characterization of hydration in ubiquitin solutions.
Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Phase Diagrams as a DOE Tool in Biomolecular Crystallization.Advances in biochemical engineering/biotechnology · 2026Review
- General Characterization of Properties of Ordered and Disordered Proteins by Wide-LineACS omega · 2024Article
- The 75-99 C-Terminal Peptide of URG7 Protein Promotes α-Synuclein Disaggregation.International journal of molecular sciences · 2024Article
- Wide-Line NMR Melting Diagrams, Their Thermodynamic Interpretation, and Secondary Structure Predictions for A30P and E46K α-Synuclein.ACS omega · 2022Article
- The Role of Cyclodextrins against Interface-Induced Denaturation in Pharmaceutical Formulations: A Molecular Dynamics Approach.Molecular pharmaceutics · 2021Article
- THE IMS PARADOX: A PERSPECTIVE ON STRUCTURAL ION MOBILITY-MASS SPECTROMETRY.Mass spectrometry reviews · 2021Review
- Hydration shell differentiates folded and disordered states of a Trp-cage miniprotein, allowing characterization of structural heterogeneity by wide-line NMR measurements.Scientific reports · 2019Article
- The Melting Diagram of Protein Solutions and Its Thermodynamic Interpretation.International journal of molecular sciences · 2018Article
- Synchrotron X-ray footprinting as a method to visualize water in proteins.Journal of synchrotron radiation · 2016Article
- Wide-line NMR and DSC studies on intrinsically disordered p53 transactivation domain and its helically pre-structured segment.BMB reports · 2016Article
- Effect of subdomain interactions on methyl group dynamics in the hydrophobic core of villin headpiece protein.Protein science : a publication of the Protein Society · 2014Article
- Structure and dynamics of protein waters revealed by radiolysis and mass spectrometry.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Article
- Distinct hydration properties of wild-type and familial point mutant A53T of α-synuclein associated with Parkinson's disease.Biophysical journal · 2011Article
- Protein-ice interaction of an antifreeze protein observed with solid-state NMR.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Multiple fuzzy interactions in the moonlighting function of thymosin-β4.Intrinsically disordered proteinsArticle
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6 authors.
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Abstract
Wide-line 1H-NMR and differential scanning calorimetry measurements were done in aqueous solutions and on lyophilized samples of human ubiquitin between -70 degrees C and +45 degrees C. The measured properties (size, thermal evolution, and wide-line NMR spectra) of the protein-water interfacial region are substantially different in the double-distilled and buffered-water solutions of ubiquitin. The characteristic transition in water mobility is identified as the melting of the nonfreezing/hydrate water. The amount of water in the low-temperature mobile fraction is 0.4 g/g protein for the pure water solution. The amount of mobile water is higher and its temperature dependence more pronounced for the buffered solution. The specific heat of the nonfreezing/hydrate water was evaluated using combined differential scanning calorimetry and NMR data. Considering the interfacial region as an independent phase, the values obtained are 5.0-5.8 J x g(-1) x K(-1), and the magnitudes are higher than that of pure/bulk water (4.2 J x g(-1) x K(-1)). This unexpected discrepancy can only be resolved in principle by assuming that hydrate water is in tight H-bond coupling with the protein matrix. The specific heat for the system composed of the protein molecule and its hydration water is 2.3 J x g(-1) x K(-1). It could be concluded that the protein ubiquitin and its hydrate layer behave as a highly interconnected single phase in a thermodynamic sense.
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