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Protein hydration in solution: Experimental observation by x-ray and neutron scattering
Open accessAbstract
The structure of the protein–solvent interface is the subject of controversy in theoretical studies and requires direct experimental characterization. Three proteins with known atomic resolution crystal structure (lysozyme, Escherichia coli thioredoxin reductase, and protein R1 of E. coli ribonucleotide reductase) were investigated in parallel by x-ray and neutron scattering in H 2 O and D 2 O solutions. The analysis of the protein–solvent interface is based on the significantly different contrasts for the protein and for the hydration shell. The results point to the existence of a first hydration shell with an average density ≈10% larger than that of the bulk solvent in the conditions studied. Comparisons with the results of other studies suggest that this may be a general property of aqueous interfaces.
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Citations
Cited by
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Ball, P. (2008) · Chemical Reviews · doi:10.1021/cr068037a · Cited by 2,177
Ballabio, F., Paissoni, C., Bollati, M., de Rosa, M., Capelli, R., & Camilloni, C. (2023) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.3c00864 · Cited by 23
Fitting high-resolution electron density maps from atomic models to solution scattering data
Chamberlain, S. R., Moore, S., & Grant, T. D. (2023) · Biophysical Journal · doi:10.1016/j.bpj.2023.10.034 · Cited by 10
Human myelin proteolipid protein structure and lipid bilayer stacking
Ruskamo, S., Raasakka, A., Pedersen, J. S., Martel, A., Škubník, K., Darwish, T., Porcar, L., & Kursula, P. (2022) · doi:10.1101/2022.03.14.484199 · Cited by 1
Metadata
- Authors
- Svergun, D. I., Richard, S., Koch, M. H. J., Sayers, Z., Kuprin, S., & Zaccai, G.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1998-03-03
- Volume
- 95
- Issue
- 5
- Pages
- 2267-2272
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2031091369
- Cited by
- 912
- References
- 0
- FWCI
- 5.18
- Type
- journal article
- Language
- en
- Open access
- green
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