Articolele autorului Bogdan Bancia
Link la profilul stiintific al lui Bogdan Bancia

Analysis of selectively 15N labelled PpiB, C-peptide and DnaG-C by NMR: NMR approach to protein structure analysis BOOK Lambert Academic Publishing

The three-dimensional structure determination of proteins represents an important step towards understanding their biological function and thus their roles in living organisms. Using a combination of multidimensional NMR techniques three different biomolecules were analyzed in the present study, E. coli peptidyl – prolyl cis-trans isomerase PpiB, proinsulin connecting peptide and DnaG-C. 15N-HSQC spectra were recorded of PpiB which had been expressed

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Functionalization of PMMA surfaces by dielectric barrier discharge treatments
Biomembrane excitability studied within a wide-band frequency of an interacting exogenous electric field

There does exist increasing experimental and theoretical evidence that supports the existence of a coupling between exogenous electromagnetic fields and ion channels located within the membrane of excitable cells. One of the most tantalizing consequences of such interactions points to a resonant-like behavior of this class of electrical non-linear systems leading to an optimized information transfer along excitable membranes. Herein, we present novel

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Bsc Atipically manifestation of the nervous excitability in the presence of an exogenous electric field

There does exist increasing experimental and theoretical evidence that supports the existence of a coupling between exogenous electromagnetic fields and ion channels located within the membrane of excitable cells. One of the most tantalizing consequences of such interactions points to a resonant-like behavior of this class of electrical non-linear systems leading to an optimized information transfer along excitable membranes. Herein, we present novel

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MSc Analysis of selectively 15N labelled Ppib, proinsulin connecting peptide and DnaG-C by NMR

The three-dimensional structure determination of proteins represents an important step towards understanding their biological function and thus their roles in living organisms. Using a combination of multidimensional NMR techniques three different biomolecules were analyzed in the present study, E. coli peptidyl – prolyl cis-trans isomerase PpiB, proinsulin connecting peptide and DnaG-C. 15N-HSQC spectra were recorded of PpiB which had been expressed

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Expression, purification, crystallization, and NMR studies of the helicase interaction domain of Escherichia coli DnaG primase

In Escherichia coli, the DnaG primase is the RNA polymerase that synthesizes RNA primers at replication forks. It is composed of three domains, a small N-terminal zinc-binding domain, a larger central domain responsible for RNA synthesis, and a C-terminal domain comprising residues 434-581 [DnaG(434-581)] that interact with the hexameric DnaB helicase. Presumably because of this interaction, it had not been possible previously to express the C-terminal

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