The Influence of Solvent Composition on Global Dynamics of Human Butyrylcholinesterase Powders: A Neutron-Scattering Study
Biophysical Journal, ISSN: 0006-3495, Vol: 86, Issue: 5, Page: 3152-3165
2004
- 20Citations
- 22Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations20
- Citation Indexes20
- 20
- CrossRef19
- Captures22
- Readers22
- 22
Article Description
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 ∼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 Ångstrom-nanosecond scale by the solvent depends not only on the presence of salt ions but also on their type.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0006349504743635; http://dx.doi.org/10.1016/s0006-3495(04)74363-5; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=11144353839&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/15111428; http://linkinghub.elsevier.com/retrieve/pii/S0006349504743635; http://api.elsevier.com/content/article/PII:S0006349504743635?httpAccept=text/xml; http://api.elsevier.com/content/article/PII:S0006349504743635?httpAccept=text/plain; https://linkinghub.elsevier.com/retrieve/pii/S0006349504743635
Elsevier BV
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