Zobrazeno 1 - 10
of 83
pro vyhledávání: '"Maria J. Jezewska"'
Publikováno v:
Biophysical Chemistry. 222:7-24
Obtaining a detailed knowledge about energetics of ligand–macromolecule interactions is a prerequisite for elucidation of the nature, behavior, and activities of the formed complexes. The most commonly used methods in characterizing molecular inter
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::adccff6795c895884383fa34f1b77140
https://doi.org/10.1016/j.bpc.2016.12.006
https://doi.org/10.1016/j.bpc.2016.12.006
Publikováno v:
Journal of Molecular Structure. 1077:40-50
Elucidation of ligand - macromolecule interactions requires detailed knowledge of energetics of the formed complexes. Spectroscopic methods are most commonly used in characterizing molecular interactions in solution. The methods do not require large
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9e0ed4326dac3b3ab4c391581423cecc
https://doi.org/10.1016/j.molstruc.2014.04.041
https://doi.org/10.1016/j.molstruc.2014.04.041
Publikováno v:
Biochemistry. 52:1845-1857
The oligomerization reaction of the Escherichia coli DnaT protein has been quantitatively examined using fluorescence anisotropy and analytical ultracentrifugation methods. In solution, DnaT exists as a monomer-trimer equilibrium system. At the estim
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c2dbc15bd1f613bc27c66937bc80b779
https://doi.org/10.1021/bi301568w
https://doi.org/10.1021/bi301568w
Publikováno v:
Biophysical chemistry. 222
Physico-chemical titration techniques are the most commonly used methods in characterizing molecular interactions. These methods are mainly based on spectroscopic, calorimetric, hydrodynamic, etc., measurements. However, truly quantitative physico-ch
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::88fd39a3ded2766073c7038de6cdef0c
https://pubmed.ncbi.nlm.nih.gov/28095332
https://pubmed.ncbi.nlm.nih.gov/28095332
Autor:
Maria J. Jezewska, Paul J. Bujalowski, Kyung H. Choi, Michal R. Szymanski, Cecile Bussetta, Wlodzimierz Bujalowski, Mengyi Ye
Publikováno v:
Journal of Biological Chemistry. 286:33095-33108
Fundamental aspects of interactions of the Dengue virus type 3 full-length polymerase with the single-stranded and double-stranded RNA and DNA have been quantitatively addressed. The polymerase exists as a monomer with an elongated shape in solution.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4aa3f7e68755295effba36229da9f2cf
https://doi.org/10.1074/jbc.m111.255034
https://doi.org/10.1074/jbc.m111.255034
Publikováno v:
Biophysical Chemistry. 158:26-37
Interactions of the polymerase X from the African Swine Fever Virus with the ssDNA have been studied, using quantitative fluorescence titration and fluorescence resonance energy transfer techniques. The primary DNA-binding subsite of the enzyme, inde
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::817bc8194dd2e93901dc3a191c30d0d4
https://doi.org/10.1016/j.bpc.2011.04.012
https://doi.org/10.1016/j.bpc.2011.04.012
Publikováno v:
Journal of Molecular Biology. 411:123-142
A direct quantitative analysis of the initial steps in primosome assembly, involving PriA and PriB proteins and the minimal primosome assembly site (PAS) of phage ϕX174, has been performed using fluorescence intensity, fluorescence anisotropy titrat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::57b0a5cd08485e063f8925e658eba56c
https://doi.org/10.1016/j.jmb.2011.05.029
https://doi.org/10.1016/j.jmb.2011.05.029
Publikováno v:
Biophysical Chemistry. 156:115-127
Interactions of the 8-kDa domain of the rat pol β and the intact enzyme with the ssDNA have been studied, using the quantitative fluorescence titration technique. The 8-kDa domain induces large topological changes in the bound DNA structure and enga
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5f65030015a47df45be4b177b9fe0118
https://doi.org/10.1016/j.bpc.2011.01.006
https://doi.org/10.1016/j.bpc.2011.01.006
Publikováno v:
Biochemistry. 49:3555-3566
The Escherichia coli single-stranded DNA binding protein (SSB) plays a central role in DNA metabolism through its high affinity interactions with ssDNA, as well as its interactions with numerous other proteins via its unstructured C-termini. Although
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4d907ecce8ad3b8b3118331dcda32889
https://doi.org/10.1021/bi100069s
https://doi.org/10.1021/bi100069s
Publikováno v:
Journal of Biological Chemistry. 285:9683-9696
The primosome is a multi-protein-DNA complex that catalyzes the priming of the DNA during the replication process. In Escherichia coli, PriA helicase plays a fundamental role in the initiation of the ordered assembly of the primosome. PriA is involve
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2924fb5aa023da5b158760056bc92412
https://doi.org/10.1074/jbc.m109.094789
https://doi.org/10.1074/jbc.m109.094789