Kanazawa University, report in Small, on how short peptides self-assemble linearly on atomically-thick solid surfaces, such ...

The researchers designed short and simple dipeptides, mainly consisting of alternating amino acids with aromatic side groups, tyrosine (Y) and histidine (H) (Fig. 2). The former is hydrophobic residue ...

Here we use cryogenic electron microscopy to determine the structure of TbAQP2 from Trypanosoma brucei, bound to either the substrate glycerol or to the sleeping sickness drugs, pentamidine or ...

Researchers reveal how hydration shapes peptide assembly on 2D materials, offering new insights for bioelectronics and ...

Proteins are biopolymers of amino acids (polypeptides), joined by peptide bonds, that are generated by ribosomes. The amino acid sequence, encoded by its gene, determines a protein’s structure ...

Each amino acid is assigned a value reflecting its tendency to be found in hydrophobic (water-avoiding) or hydrophilic (water-attracting) environments. Despite certain limitations, the Kyte–Doolittle ...

Therefore, the rQTY variants could become partially hydrophobic proteins at specific sites. If the rQTY code can replace amino acids Q, T, Y to L, V and F, respectively, it can then increase the ...

Researchers at the universities of Amsterdam and Utrecht have observed the formation of nanocavities in montmorillonite clay ...

Stuff ...

The company has integrated the AI model into its internal discovery pipeline and aims to use it in collaborative drug ...

How do we determine how healthy our food is? We know now that our nutrition shouldn't just be measured in calories, or even ...