ArticleBiophysical journal2007
C-phycocyanin hydration water dynamics in the presence of trehalose: an incoherent elastic neutron scattering study at different energy resolutions.
Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Exploring Cyclodextrin-Based Nanosponges as Drug Delivery Systems: Evaluation of Spectroscopic Methods for Examining Structure and Dynamics of Nanosponges.International journal of molecular sciences · 2025Review
- Neutrons describe ectoine effects on water H-bonding and hydration around a soluble protein and a cell membrane.Scientific reports · 2016Article
- Water Determines the Structure and Dynamics of Proteins.Chemical reviews · 2016Review
- Bio-protective effects of homologous disaccharides on biological macromolecules.European biophysics journal : EBJ · 2012Article
- Dynamics of biological macromolecules: not a simple slaving by hydration water.Biophysical journal · 2010Article
- Dynamics of apomyoglobin in the alpha-to-beta transition and of partially unfolded aggregated protein.European biophysics journal : EBJ · 2009Article
- Protein dynamics and stability: the distribution of atomic fluctuations in thermophilic and mesophilic dihydrofolate reductase derived using elastic incoherent neutron scattering.Biophysical journal · 2008Article
- Differences in internal dynamics of actin under different structural states detected by neutron scattering.Biophysical journal · 2008Article
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2 authors.
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Abstract
We present a study of C-phycocyanin hydration water dynamics in the presence of trehalose by incoherent elastic neutron scattering. By combining data from two backscattering spectrometers with a 10-fold difference in energy resolution we extract a scattering law S(Q,omega) from the Q-dependence of the elastic intensities without sampling the quasielastic range. The hydration water is described by two dynamically different populations--one diffusing inside a sphere and the other diffusing quasifreely--with a population ratio that depends on temperature. The scattering law derived describes the experimental data from both instruments excellently over a large temperature range (235-320 K). The effective diffusion coefficient extracted is reduced by a factor of 10-15 with respect to bulk water at corresponding temperatures. Our approach demonstrates the benefits and the efficiency of using different energy resolutions in incoherent elastic neutron scattering over a large angular range for the study of biological macromolecules and hydration water.
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