Zobrazeno 1 - 10
of 39
pro vyhledávání: '"I.V. Kurinov"'
Publikováno v:
Protein Science. 8:2399-2405
Pokeweed antiviral protein (PAP) is a ribosome-inactivating protein (RIP), which enzymatically removes a single adenine base from a conserved, surface exposed loop sequence of ribosomal rRNA. We now present unprecedented experimental evidence that PA
Publikováno v:
Biochemical and Biophysical Research Communications. 275:549-552
Pokeweed antiviral protein II (PAP-II) is a naturally occurring protein isolated from early summer leaves of the pokeweed plant (Phytolacca americana). PAP-II belongs to a family of ribosome-inactivating proteins which catalytically deadenylate ribos
Autor:
Robert W. Harrison, I.V. Kurinov
Publikováno v:
Protein Science. 5:752-758
Three-dimensional structures of trypsin with the reversible inhibitor leupeptin have been determined in two different crystal forms. The first structure was determined at 1.7 A resolution with R-factor = 17.7% in the trigonal crystal space group P3(1
Autor:
I.V. Kurinov, Robert W. Harrison
Publikováno v:
Nature Structural & Molecular Biology. 1:735-743
We describe here the use of a rapid computational method to predict the relative binding strengths of a series of small-molecule ligands for the serine proteinase trypsin. Flexible molecular models of the ligands were docked to the proteinase using a
Publikováno v:
Journal of Physics and Chemistry of Solids. 55:127-137
A new approach for the investigation of intramolecular motions in proteins, based on the study of spin-lattice relaxation of ferric iron in the protein active centres, has been developed. The Mossbauer spectra of dry and hydrated transferrin enriched
The pokeweed antiviral protein (PAP) belongs to a family of ribosome-inactivating proteins (RIP), which depurinate ribosomal RNA through their site-specific N-glycosidase activity. We report low temperature, three-dimensional structures of PAP co-cry
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b8901113d25f6e2fa76c642f1fc3f036
https://europepmc.org/articles/PMC2144398/
https://europepmc.org/articles/PMC2144398/
Autor:
Robert W. Harrison, I.V. Kurinov
Publikováno v:
Acta crystallographica. Section D, Biological crystallography. 51(Pt 1)
Lysozyme structures at six different temperatures in the range 95-295 K have been determined using X-ray crystallography at a resolution of 1.7 A. The crystals at lower temperatures had a 7.4% decrease in the unit-cell volume. The volume change was d
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