Protein hydration in solution: experimental observation by x-ray and neutron scattering.
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 H2O and D2O 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 approximately 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.
Svergun
D I
DI
European Molecular Biology Laboratory, Hamburg Outstation, Notkestrasse 85, D-22603 Hamburg, Germany. Svergun@EMBL-Hamburg.DE
Richard
S
S
Koch
M H
MH
Sayers
Z
Z
Kuprin
S
S
Zaccai
G
G
D004926:Escherichia coli / Q000201:enzymology; D008970:Molecular Weight; D009113:Muramidase / Q000737:chemistry*; D009502:Neutrons; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D012264:Ribonucleotide Reductases / Q000737:chemistry*; D012542:Scattering, Radiation; D012996:Solutions; D012997:Solvents; D013880:Thioredoxin-Disulfide Reductase / Q000737:chemistry*; D014961:X-Ray Diffraction / Q000379:methods
D011506:Proteins; D012996:Solutions; D012997:Solvents; D012264:Ribonucleotide Reductases; D013880:Thioredoxin-Disulfide Reductase; D009113:Muramidase