G-protein coupled receptors (GPCRs) are large protein families known to be important in many cellular processes. They are well known for their allosteric activation mechanisms. They are drug targets for several FDA-approved drugs. We have investigated the diversity of the ligand binding site for these class of proteins against their cognate ligands using computational docking, even if their structures are known in the ligand-complexed form. The cognate ligand of some of these receptors dock at allosteric binding site, with better score than the binding at the conservative site. Further, ligands obtained from GLASS database, which consists of experimentally verified GPCR ligands, also show allosteric binding to GPCRs. The allosteric binders show strong affinity to the binding site, though the residues at the binding site are not conserved across GPCR subfamilies.

The effects of cognate synonymy in L2 word learning are explored. Participants learned the names of well-known concrete concepts in a new fictional language following a picture-word association paradigm. Half of the concepts (set A) had two possible translations in the new language (i.e., both words were synonyms): one was a cognate in participants’ L1 and the other one was not. The other half of the concepts (set B) had only one possible translation in the new language, a non-cognate word. After learning the new words, participants’ memory was tested in a picture-word matching task and a translation recognition task. In line with previous findings, our results clearly indicate that cognates are much easier to learn, as we found that the cognate translation was remembered much better than both its non-cognate synonym and the non-cognate from set B. Our results also seem to suggest that non-cognates without cognate synonyms (set B) are better learned than non-cognates with cognate synonyms (set A). This suggests that, at early stages of L2 acquisition, learning a cognate would produce a poorer acquisition of its non-cognate synonym, as compared to a solely learned non-cognate. These results are discussed under the light of different theories and models of bilingual mental lexicon.

How Nature discovered genetic coding is a largely ignored question, yet the answer is key to explaining the transition from biochemical building blocks to life. Other, related puzzles also fall inside the aegis enclosing the codes themselves. The peptide bond is unstable with respect to hydrolysis. So, it requires some form of chemical free energy to drive it. Amino acid activation and acyl-transfer are also slow and call for catalysis. All living things must thus also convert free energy and synchronize cellular chemistry. Most importantly, functional proteins occupy only small, isolated regions of sequence space. Nature evolved heritable symbolic data processing to seek out and use those sequences. That system has three parts: a memory of how amino acids behave in solution and inside proteins, a set of code-keys to access that memory, and a scoring function. The code-keys themselves are the genes for cognate pairs of tRNA and aminoacyl-tRNA synthetases, AARS. I outline the surprising links between all these questions and the structural duality of the base-pairing that holds genes together and how those links arise from the experiments.