ArticleBiophysical journal2004
The influence of solvent composition on global dynamics of human butyrylcholinesterase powders: a neutron-scattering study.
Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Characterizing Protein Structure, Dynamics and Conformation in Lyophilized Solids.Current pharmaceutical design · 2015Review
- Internal motions of actin characterized by quasielastic neutron scattering.European biophysics journal : EBJ · 2011Article
- Nanosecond motions in proteins impose bounds on the timescale distributions of local dynamics.Biophysical journal · 2009Article
- From powder to solution: hydration dependence of human hemoglobin dynamics correlated to body temperature.Biophysical journal · 2009Article
- Direct correlation between molecular dynamics and enzymatic stability: a comparative neutron scattering study of native human butyrylcholinesterase and its "aged" soman conjugate.Biophysical journal · 2009Article
- Dynamics of C-phycocyanin in various deuterated trehalose/water environments measured by quasielastic and elastic neutron scattering.European biophysics journal : EBJ · 2008Article
- Solvent isotope effect on macromolecular dynamics in E. coli.European biophysics journal : EBJ · 2008Article
- Differences in internal dynamics of actin under different structural states detected by neutron scattering.Biophysical journal · 2008Article
- Coupling of protein and hydration-water dynamics in biological membranes.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- C-phycocyanin hydration water dynamics in the presence of trehalose: an incoherent elastic neutron scattering study at different energy resolutions.Biophysical journal · 2007Article
- Effects of soman inhibition and of structural differences on cholinesterase molecular dynamics: a neutron scattering study.Biophysical journal · 2005Article
- Influence of the water structure on the acetylcholinesterase efficiency.Biophysical journal · 2005Article
- Protein dynamics in solution and powder measured by incoherent elastic neutron scattering: the influence of Q-range and energy resolution.European biophysics journal : EBJ · 2005Article
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10 authors.
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Abstract
A major result of incoherent elastic neutron-scattering experiments on protein powders is the strong dependence of the intramolecular dynamics on the sample environment. We performed a series of incoherent elastic neutron-scattering experiments on lyophilized human butyrylcholinesterase (HuBChE) powders under different conditions (solvent composition and hydration degree) in the temperature range from 20 to 285 K to elucidate the effect of the environment on the enzyme atomic mean-square displacements. Comparing D(2)O- with H(2)O-hydrated samples, we were able to investigate protein as well as hydration water molecular dynamics. HuBChE lyophilized from three distinct buffers showed completely different atomic mean-square displacements at temperatures above approximately 200 K: a salt-free sample and a sample containing Tris-HCl showed identical small-amplitude motions. A third sample, containing sodium phosphate, displayed highly reduced mean-square displacements at ambient temperature with respect to the other two samples. Below 200 K, all samples displayed similar mean-square displacements. We draw the conclusion that the reduction of intramolecular protein mean-square displacements on an Angstrom-nanosecond scale by the solvent depends not only on the presence of salt ions but also on their type.
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