Eugene Mamontov

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  • S-H Chen, L Liu, E Fratini, P Baglioni, A Faraone, E Mamontov
  • Proceedings of the National Academy of Sciences…
  • 2006
At low temperatures, proteins exist in a glassy state, a state that has no conformational flexibility and shows no biological functions. In a hydrated protein, at temperatures greater-- similar 220 K, this flexibility is restored, and the protein is able to sample more conformational substates, thus becoming biologically functional. This "dynamical"(More)
Cyanobacteria are prokaryotes that can use photosynthesis to convert sunlight into cellular fuel. Knowledge of the organization of the membrane systems in cyanobacteria is critical to understanding the metabolic processes in these organisms. We examined the wild-type strain of Synechocystis sp. PCC 6803 and a series of mutants with altered light-harvesting(More)
Both the structure and dynamics of biomolecules are known to be essential for their biological function. In the dehydrated state, the function of biomolecules, such as proteins, is severely impeded, so hydration is required for bioactivity. The dynamics of the hydrated biomolecules and their hydration water are related - but how closely? The problem(More)
We used high-resolution quasielastic neutron scattering spectroscopy to study the single-particle dynamics of water molecules on the surface of hydrated DNA samples. Both H(2)O and D(2)O hydrated samples were measured. The contribution of scattering from DNA is subtracted out by taking the difference of the signals between the two samples. The measurement(More)
Many biosystems are complex mixtures of disparate biofluids. To study contact and transport phenomena in these mixtures, one has to apply much information on the biofluids which are components of the mixtures. A lot of the corresponding data can be extracted by means of experiments. However, it is not always easy to obtain experimental results on rather(More)
The structurally and dynamically perturbed hydration shells that surround proteins and biomolecules have a substantial influence upon their function and stability. This makes the extent and degree of water perturbation of practical interest for general biological study and industrial formulation. We present an experimental description of the dynamical(More)
Despite extensive efforts in experimental and computational studies, the microscopic understanding of dynamics of biological macromolecules remains a great challenge. It is known that hydrated proteins, DNA and RNA, exhibit a so-called "dynamic transition." It appears as a sharp rise of their mean-squared atomic displacements r2 at temperatures above(More)
We studied the dynamics of hydrated tRNA using neutron and dielectric spectroscopy techniques. A comparison of our results with earlier data reveals that the dynamics of hydrated tRNA is slower and varies more strongly with temperature than the dynamics of hydrated proteins. At the same time, tRNA appears to have faster dynamics than DNA. We demonstrate(More)
We describe the design and current performance of the backscattering silicon spectrometer (BASIS), a time-of-flight backscattering spectrometer built at the spallation neutron source (SNS) of the Oak Ridge National Laboratory (ORNL). BASIS is the first silicon-based backscattering spectrometer installed at a spallation neutron source. In addition to high(More)
Dynamics of water, especially in the temperature range of the "no man's land", remain a mystery. We present detailed study of dynamics in aqueous LiCl solution that is often considered as a model for bulk water. We employ broadband dielectric and light scattering spectroscopy in a broad frequency and temperature range. Our analysis reveals no sign of the(More)