Publications by authors named "B Stec"
To shed light onto the activation mechanism of vinculin, we carried out a detailed refinement of chicken vinculin and compared it to the human protein which is greater than 95% identical. Refinement resulted in a complete and significantly improved model. This model includes important elements such as a pro-rich strap region (PRR) and C-terminus.
View Article and Find Full Text PDFThe universally conserved N6-threonylcarbamoyladenosine (t6A) modification of tRNA is essential for translational fidelity. In bacteria, t6A biosynthesis starts with the TsaC/TsaC2-catalyzed synthesis of the intermediate threonylcarbamoyl adenylate (TC-AMP), followed by transfer of the threonylcarbamoyl (TC) moiety to adenine-37 of tRNA by the TC-transfer complex comprised of TsaB, TsaD and TsaE subunits and possessing an ATPase activity required for multi-turnover of the t6A cycle. We report a 2.
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- The study highlights the potential of using metal-ligand interactions to control protein complex formation, which is important for developing advanced biomaterials.
- The researchers designed three protein dimers that are monomeric without metal and form stable dimers when zinc sulfate is present, emphasizing their high-affinity and symmetric characteristics.
- The dimers exhibit notable thermal stability and can dissociate in the presence of EDTA, with structural analysis confirming effective zinc binding and desired dimer configurations.
Determination of the signal power-to-noise power ratio on the input and output of reception systems is essential to the estimation of their quality and signal reception capability. This issue is especially important in the case when both signal and noise have the same characteristic as Gaussian white noise. This article considers the problem of how a signal-to-noise ratio is changed as a result of signal processing in the correlation receiver of a noise radar in order to determine the ability to detect weak features in the presence of strong clutter-type interference.
View Article and Find Full Text PDFThe universal N(6)-threonylcarbamoyladenosine (t6A) modification at position 37 of ANN-decoding tRNAs is central to translational fidelity. In bacteria, t6A biosynthesis is catalyzed by the proteins TsaB, TsaC/TsaC2, TsaD and TsaE. Despite intense research, the molecular mechanisms underlying t6A biosynthesis are poorly understood.
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