Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Martin Klvana"'
Autor:
Martin Klvana, Urban Bren
Publikováno v:
Molecules, Vol 24, Iss 1, p 150 (2019)
Thermal stabilities of DNA duplexes containing Gua (g), α- (a) or β-anomer of formamidopyrimidine-N7-9-hydroxy-aflatoxin B1 (b) differ markedly (Tm: a < g < b ), but the underlying molecular origin of this experimentally observed phenomenon is yet
Externí odkaz:
https://doaj.org/article/b1146cb636e943568ece2ce72d269a43
Autor:
Eva Chovancova, Antonin Pavelka, Petr Benes, Ondrej Strnad, Jan Brezovsky, Barbora Kozlikova, Artur Gora, Vilem Sustr, Martin Klvana, Petr Medek, Lada Biedermannova, Jiri Sochor, Jiri Damborsky
Publikováno v:
PLoS Computational Biology, Vol 8, Iss 10, p e1002708 (2012)
Tunnels and channels facilitate the transport of small molecules, ions and water solvent in a large variety of proteins. Characteristics of individual transport pathways, including their geometry, physico-chemical properties and dynamics are instrume
Externí odkaz:
https://doaj.org/article/291f1b72633147e3a03d80fd1180ac09
Autor:
Martin, Klvana, Urban, Bren
Publikováno v:
Molecules
Thermal stabilities of DNA duplexes containing Gua (g), α- (a) or β-anomer of formamidopyrimidine-N7-9-hydroxy-aflatoxin B1 (b) differ markedly (Tm: a
Autor:
Yuji Nagata, Michal Otyepka, Martina Pavlová, Rebecca C. Wade, Pavel Banáš, Jiri Damborsky, Radka Chaloupková, Masataka Tsuda, Zbynek Prokop, Martin Klvana
Publikováno v:
Nature Chemical Biology. 5:727-733
Engineering enzymes to degrade anthropogenic compounds efficiently is challenging. We obtained Rhodococcus rhodochrous haloalkane dehalogenase mutants with up to 32-fold higher activity than wild type toward the toxic, recalcitrant anthropogenic comp
Autor:
Petr Kulhánek, Alena Stsiapanava, Zbynek Prokop, Jan Dohnálek, Ivana Kuta-Smatanova, Jiri Damborsky, Martina Pavlová, Tana Koudelakova, Martin Klvana, Radka Chaloupková, Rebecca C. Wade, Michal Kuty, Pavel Dvorak
Publikováno v:
Journal of molecular biology. 392(5)
Eight mutants of the DhaA haloalkane dehalogenase carrying mutations at the residues lining two tunnels, previously observed by protein X-ray crystallography, were constructed and biochemically characterized. The mutants showed distinct catalytic eff