Zobrazeno 1 - 6
of 6
pro vyhledávání: '"K M, Poliakov"'
Autor:
Konstantin G. Skryabin, Mikhail V. Kovalchuk, Nikolai V. Ravin, Andrey V. Mardanov, Ekaterina Yu. Bezsudnova, Vladimir Popov, V. A. Smagin, Tamara V. Tikhonova, K. M. Poliakov, T.N. Stekhanova
Publikováno v:
Acta Crystallographica Section F Structural Biology and Crystallization Communications. 65:368-371
DNA ligases catalyze the sealing of 5'-phosphate and 3'-hydroxyl termini at single-strand breaks in double-stranded DNA and their function is essential to maintain the integrity of the genome in DNA metabolism. An ATP-dependent DNA ligase from the ar
Autor:
K M, Poliakov, D A, Goncharuk, A A, Trofimov, T N, Safonova, V A, Mit'kevich, E N, Tkach, A A, Makarov, A A, Shul'ga
Publikováno v:
Molekuliarnaia biologiia. 44(5)
The structures of two crystal modifications of the W34F mutant ribonuclease from the bacterium Bacillus intermedius (binase) were solved and refined at 1.7 and 1.1 A resolution. The kinetic parameters of the hydrolysis of substrates of different leng
Autor:
M V, Anisimova, A A, Shul'ga, I V, Levichkin, M P, Kirpichnikov, K M, Poliakov, K G, Skriabin, M A, Vijayalakshmi, V P, Varlamov
Publikováno v:
Bioorganicheskaia khimiia. 27(1)
The zinc(II)-binding affinities of recombinant human growth hormone and two its mutants, 14-33 and 14-95, were studied using Immobilized Metal Ion Affinity Gel-electrophoresis (IMAG). The mutant hormones, composed of polypeptide chain segments of the
Autor:
I I, Protasevich, F O, Tsvetkov, A A, Shul'ga, K M, Poliakov, V M, Lobachev, M P, Kirpichnikov, A A, Makarov
Publikováno v:
Molekuliarnaia biologiia. 33(3)
Autor:
E Iu, Kolbanovskaia, A L, Okorokov, K I, Panov, K M, Poliakov, R W, Hartley, M Ia, Karpeĭskiĭ
Publikováno v:
Molekuliarnaia biologiia. 28(3)
Barnase, an extracellular ribonuclease produced by Bacillus amyloliquefaciens, belongs to a family of small microbial ribonucleases with similar structure and properties. These enzymes hydrolyze phosphodiester bonds on the 3' side of guanosine nucleo
Publikováno v:
Biokhimiia (Moscow, Russia). 53(6)
Extracellular guanyl-specific RNAase of the fungus Aspergillus pallidus (RNAase ApI) was isolated in preparative amounts with a 40% yield and purified to homogeneity (938-fold). The complete amino acid sequence of the protein (104 amino acid residues