ArticleEuropean biophysics journal : EBJ2012
Bio-protective effects of homologous disaccharides on biological macromolecules.
Article in European biophysics journal : EBJ, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 35 citations in OpenAlex.
- Trehalose: a multifunctional sugar and its metabolites are biotechnological targets for crop salinity tolerance under saline conditions.Plant molecular biology · 2026Review
- The Structural and Dynamical Properties of the Hydration of SNase Based on a Molecular Dynamics Simulation.Molecules (Basel, Switzerland) · 2021Article
- Experimental demonstration of the novel "van-Hove integral method (vHI)" for measuring diffusive dynamics by elastic neutron scattering.Scientific reports · 2021Article
- The tepary bean genome provides insight into evolution and domestication under heat stress.Nature communications · 2021Article
- Comparison of Chemical Composition and Biological Activities of EightPharmaceuticals (Basel, Switzerland) · 2020Article
- Mechanisms of action of ionic liquids on living cells: the state of the art.Biophysical reviews · 2020Review
- From protein and its hydration water dynamics to controlling mechano-elasticity of cellular lipid membranes and cell migration via ionic liquids.Biophysical reviews · 2020Article
- From just physics to biophysics of biological systems.Biophysical reviews · 2020Article
- A Quantitative Comparison of the Counting Significance of van Hove Integral Spectroscopy and Quasielastic Neutron Scattering.Scientific reports · 2020Article
- Sweet cherry fruit cracking: follow-up testing methods and cultivar-metabolic screening.Plant methods · 2020Article
- Dynamics from elastic neutron-scattering via direct measurement of the running time-integral of the van Hove distribution function.Scientific reports · 2019Article
- Survival and Energy Producing Strategies of Alkane Degraders Under Extreme Conditions and Their Biotechnological Potential.Frontiers in microbiology · 2018Review
- Room-temperature ionic liquids meet bio-membranes: the state-of-the-art.Biophysical reviews · 2017Review
- Investigating Structure and Dynamics of Proteins in Amorphous Phases Using Neutron Scattering.Computational and structural biotechnology journal · 2017Review
- Fine tuning of trehalose biosynthesis and hydrolysis as novel tools for the generation of abiotic stress tolerant plants.Frontiers in plant science · 2014Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In this contribution the effects of the homologous disaccharides trehalose and sucrose on both water and hydrated lysozyme dynamics are considered by determining the mean square displacement (MSD) from elastic incoherent neutron scattering (EINS) experiments. The self-distribution function (SDF) procedure is applied to the data collected, by use of IN13 and IN10 spectrometers (Institute Laue Langevin, France), on trehalose and sucrose aqueous mixtures (at a concentration corresponding to 19 water molecules per disaccharide molecule), and on dry and hydrated (H(2)O and D(2)O) lysozyme also in the presence of the disaccharides. As a result, above the glass transition temperature of water, the MSD of the water-trehalose system is lower than that of the water-sucrose system. This result suggests that the hydrogen-bond network of the water-trehalose system is stronger than that of the water-sucrose system. Furthermore, by taking into account instrumental resolution effects it was found that the system relaxation time of the water-trehalose system is longer than that of the water-sucrose system, and the system relaxation time of the protein in a hydrated environment in the presence of disaccharides increases sensitively. These results explain the higher bioprotectant effectiveness of trehalose. Finally, the partial MSDs of sucrose/water and trehalose/water have been evaluated. It clearly emerges from the analysis that these are almost equivalent in the low-Q domain (0-1.7 Å(-1)) but differ substantially in the high-Q range (1.7-4 Å(-1)). These findings reveal that the lower structural sensitivity of trehalose to thermal changes is connected with the local spatial scale.
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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.