Zobrazeno 1 - 10
of 20
pro vyhledávání: '"L T, Delbaere"'
Publikováno v:
Photochemistry and photobiology. 73(6)
M-DNA is a novel duplex conformation in which metal ions such as Co2+, Ni2+ or Zn2+ replace the imino protons of every base pair. An ethidium fluorescence assay was used to estimate lesions in M-DNA induced by gamma- and UV radiation. General damage
Autor:
G F, Audette, R, Engelmann, W, Hengstenberg, J, Deutscher, K, Hayakawa, J W, Quail, L T, Delbaere
Publikováno v:
Journal of molecular biology. 303(4)
The histidine-containing phosphocarrier protein HPr is a central component of the phosphoenolpyruvate:sugar phosphotransferase system (PTS), which transfers metabolic carbohydrates across the cell membrane in many bacterial species. In Gram-positive
Publikováno v:
Biochemistry and cell biology = Biochimie et biologie cellulaire. 77(6)
The structure of the N-terminal domain of enzyme I complexed with histidine-containing protein (HPr) has been described by multi-dimensional NMR. Residues in HPr involved in binding were identified by intermolecular nuclear Overhauser effects (Garret
Publikováno v:
The Journal of biological chemistry. 274(31)
The active site residue, His(15), in histidine-containing protein, HPr, can be replaced by aspartate and still act as a phosphoacceptor and phosphodonor with enzyme I and enzyme IIA(glucose), respectively. Other substitutions, including cysteine, glu
Publikováno v:
Journal of molecular biology. 280(5)
The tertiary structure of Jel42 Fab fragment complexed with HPr, a phosphocarrier protein of the phosphoenolpyruvate:sugar phosphotransferase system of Escherichia coli, has been determined at 2.5 A resolution. X-ray diffraction from a larger crystal
Publikováno v:
The Journal of biological chemistry. 268(30)
The x-ray structure of Escherichia coli HPr has been redetermined at 2.0-A resolution. In contrast to the previous study (El-Kabbani, O. A. L., Waygood, E. B., and Delbaere, L. T. J. (1987) J. Biol. Chem. 262, 12926-12929), the overall structure is,
Autor:
L, Prasad, S, Sharma, M, Vandonselaar, J W, Quail, J S, Lee, E B, Waygood, K S, Wilson, Z, Dauter, L T, Delbaere
Publikováno v:
The Journal of biological chemistry. 268(15)
The location and description of epitopes on proteins describe the basis of immunological specificity. The 2.8-A structure of the phosphocarrier protein, HPr from Escherichia coli, complexed to the Fab fragment of the monoclonal antibody, Jel42, has b
Publikováno v:
Ciba Foundation symposium. 158
As predicted by inhibition studies the X-ray crystal structure of the complex formed between the tetrasaccharide alpha-L-Fuc(1----2)-beta-D-Gal(1----3) [alpha-L-Fuc-(1----4)]-beta-D-GlcNAc- OMe (Leb-OMe) and the lectin IV of Griffonia simplicifolia (
Publikováno v:
Journal of molecular biology. 124(1)
Publikováno v:
The Journal of biological chemistry. 264(31)
Single crystals of the complex of a monoclonal Fab fragment with the histidine-containing protein of the phosphoenolpyruvate:sugar phosphotransferase system of Escherichia coli have been grown. This represents one of the first Fab-protein antigen com