Zobrazeno 1 - 10
of 32
pro vyhledávání: '"M L, Ludwig"'
Autor:
F. Unger, M. Rothe, M.-L. Ludwig, Torsten Semmler, Ursula Leidner, Christa Ewers, Ellen Prenger-Berninghoff, Tobias Eisenberg
Publikováno v:
International journal of antimicrobial agents. 49(1)
Autor:
M J, Hunter, M L, Ludwig
Publikováno v:
Methods in enzymology. 25
Publikováno v:
Revista gaucha de enfermagem.
This article was originated by a request of some professors of the Masters Course in Nursing. The theme "bath", as an act of care, was developed, initially, on the meaning of moves. The esthetic of body movement, to the sound of music, was represente
Publikováno v:
Journal of molecular biology. 294(3)
Flavodoxin from Anacystis nidulans (Synechococcus PCC 7942) was the first member of the flavodoxin family to be characterized, and is the structural prototype for the "long-chain" flavodoxins that have molecular masses of approximately 20 kDa. Crysta
Publikováno v:
Journal of molecular biology. 294(3)
The long-chain flavodoxins, with 169-176 residues, display oxidation-reduction potentials at pH 7 that vary from -50 to -260 mV for the oxidized/semiquinone (ox/sq) equilibrium and are -400 mV or lower for the semiquinone/hydroquinone (sq/hq) equilib
Publikováno v:
Revista gaucha de enfermagem. 17(1)
The present study describes the antimicrobiological methods used for ooscopic instruments and also recommends a routine of material caring, methods and products to be employed. These orientations were also based on the author's experience with those
Publikováno v:
Journal of molecular biology. 219(2)
The structure of Mn(III) superoxide dismutase (Mn(III)SOD) from Thermus thermophilus, a tetramer of chains 203 residues in length, has been refined by restrained least-squares methods. The R-factor [formula: see text] for the 54,056 unique reflection
Autor:
G. N. Reeke, Jean A. Hartsuck, M. L. Ludwig, Thomas A. Steitz, William N. Lipscomb, Florante A. Quiocho
Publikováno v:
Proceedings of the National Academy of Sciences. 58:2220-2226
Bovine carboxypeptidase A, (CPA) is a zinc-containing enzyme of mol wt 34,600 which catalyzes the hydrolysis of polypeptides at the C-terminal peptide bond, especially if the terminal residue of the substrate is aromatic. We have extended our X-ray d
Publikováno v:
Proceedings of the National Academy of Sciences. 50:282-285
Autor:
M. J. Hunter, M. L. Ludwig
Publikováno v:
Journal of the American Chemical Society. 84:3491-3504