Ontology highlight
ABSTRACT:
SUBMITTER: Svergun DI
PROVIDER: S-EPMC19315 | biostudies-literature | 1998 Mar
REPOSITORIES: biostudies-literature
Svergun D I DI Richard S S Koch M H MH Sayers Z Z Kuprin S S Zaccai G G
Proceedings of the National Academy of Sciences of the United States of America 19980301 5
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 ...[more]