Abstract
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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Dates
Type | When |
---|---|
Created | 23 years, 1 month ago (July 26, 2002, 10:40 a.m.) |
Deposited | 3 years, 4 months ago (April 13, 2022, 4:32 p.m.) |
Indexed | 2 days, 14 hours ago (Aug. 30, 2025, 12:20 p.m.) |
Issued | 27 years, 5 months ago (March 3, 1998) |
Published | 27 years, 5 months ago (March 3, 1998) |
Published Online | 27 years, 5 months ago (March 3, 1998) |
Published Print | 27 years, 5 months ago (March 3, 1998) |
@article{Svergun_1998, title={Protein hydration in solution: Experimental observation by x-ray and neutron scattering}, volume={95}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.95.5.2267}, DOI={10.1073/pnas.95.5.2267}, number={5}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Svergun, D. I. and Richard, S. and Koch, M. H. J. and Sayers, Z. and Kuprin, S. and Zaccai, G.}, year={1998}, month=mar, pages={2267–2272} }