Chirality is present at all levels of structural hierarchy of protein and plays a significant role in
protein biosynthesis. The macromolecules involved in protein biosynthesis such as …

In the present work we report, for the first time, a novel difference in the molecular
mechanism of the activation step of aminoacylation reaction between the class I and class II …

The relationship of molecular chirality and biology is intriguing. Our curiosity prompts the
question as to why diverse natural biological molecules are overwhelmingly dissymmetric. Is …

Threonyl-tRNA synthetase (ThrRS) is a Zn (II) containing enzyme that catalyzes the
activation of threonine and its subsequent transfer to the cognate tRNA. This process is …

Aminoacylation is a vital step of natural biosynthesis of peptide. Correct aminoacylation is a
necessary prerequisite for the elimination of noncognate amino acids such as d-amino …

The present work is aimed at understanding the origin of the difference in the molecular
organization of the active site nanospaces of the class I and class II aminoacyl tRNA …

d-Amino acids are excluded at three different steps during protein synthesis: the
aminoacylation of tRNA, binding of aminoacyl-tRNAs to EF-Tu, and selection of the …

The relation between the conservation of active site residues and the molecular mechanism
of aminoacylation reaction is an unexplored problem. In the present paper, the influences of …

In this work we investigated the outside binding mode between a cationic porphyrin and a
nucleotide pair of DNA, adenine-thymine and guanine-cytosine, in a supramolecular …

The proteins belonging to different organisms as well as the natural amino acids as
incorporated into proteins occurring free in tissues and lymphatic fluids are, as a rule …