Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Alexei M. Kopylov"'
Autor:
Olga I. Rassokhina, Philipp O. Tsvetkov, Jiri Sponer, Alexander A. Makarov, Andrey V. Golovin, Alexei M. Kopylov, Roman V. Reshetnikov
Publikováno v:
Nucleic Acids Research
A combination of explicit solvent molecular dynamics simulation (30 simulations reaching 4 µs in total), hybrid quantum mechanics/molecular mechanics approach and isothermal titration calorimetry was used to investigate the atomistic picture of ion
Publikováno v:
Journal of Chemical Theory and Computation. 6:3003-3014
The thrombin-binding aptamer (15-TBA) is a 15-mer DNA oligonucleotide with sequence d(GGTTGGTGTGGTTGG). 15-TBA folds into a quadruplex DNA (G-DNA) structure with two planar G-quartets connected by three single-stranded loops. The arrangement of the 1
Publikováno v:
FEBS Letters. 580:5858-5862
In E. coli, S7 initiates 30S ribosome assembly by binding to 16S rRNA. It also regulates translation of the S12 and S7 cistrons of the ‘streptomycin’ operon transcript by binding to the S12–S7 intercistronic region. Here, we describe the contac
Autor:
Wolfram Saenger, Brigitte Wittmann-Liebold, Eugeny N. Dobrov, Alexei M. Kopylov, Maria M. Anokhina, V. A. Spiridonova, Tsezi A. Egorov, Peter Orth, Maria M. Beliakova
Publikováno v:
FEBS Letters. 477:263-267
Results of a first successful application of a direct photo-induced affinity modification of Tet repressor (TetR(D)) protein with tetracycline within a complex of known three-dimensional structure are described. The conditions of the modification hav
Publikováno v:
FEBS Letters. 460:353-356
A study of the ability of His6-tagged ribosomal protein S7 of Thermus thermophilus to interact with the truncated S12–S7 intercistronic region of str mRNA of Escherichia coli has been described. A minimal S7 binding mRNA fragment is a part of the c
Publikováno v:
IUBMB Life. 44:1141-1146
Direct determination of RNA-protein complex structures is often facilitated by the use of thermophilic proteins; however E. coli is the most investigated system so far. A hybrid approach is to form heterologous complexes of E. coli RNA with thermophi
Tetracycline blocks stable binding of aminoacyl-tRNA to the bacterial ribosomal A-site. Various tetracycline binding sites have been identified in crystals of the 30S ribosomal small subunit of Thermus thermophilus. Here we describe a direct photo- a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::94d18480356a357f41a4126bb2bf8741
https://europepmc.org/articles/PMC419471/
https://europepmc.org/articles/PMC419471/
Publikováno v:
FEBS Letters. 369:158-160
Researchers still have great difficulty in isolating individual ribosomal proteins from the ribosome in quantities high enough for structural research. To this end, when studying protein S7, we created an E. coli overproducer of the recombinant prote
By chemical and enzymatic probing, we have analyzed the secondary structure of rodent BC1 RNA, a small brain-specific non-messenger RNA. BC1 RNA is specifically transported into dendrites of neuronal cells, where it is proposed to play a role in regu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6a7a75c60e91ee8d3c43ca259c6078f0
https://europepmc.org/articles/PMC1370124/
https://europepmc.org/articles/PMC1370124/
Publikováno v:
Current genetics. 24(1-2)
Expression of a neomycin phosphotransferase II (NPTII) gene has been designed to be regulated by an FLP-mediated switching of the orientation of the NPTII coding region located on the invertible DNA segment in episomal yeast plasmids. Inversion of th