Basic amino-acid side chains regulate transmembrane integrin signalling. Nature. 481:209-213. https://doi.org/1 0.1038/nature10697Kim, C., Schmidt, T., Cho, E.-G., Ye, F., Ulmer, T. S., and Ginsberg, M. H. (2011). Basic amino-acid side chains regulate ...
No-flow concentration compartments give the possibility to concentrate amino acid solutions. Concentration factors have been obtained in a wide range of current density for basic amino acids with various side chains (lysine, arginine, histidine). The feed solution concentration influence on concentration...
Association of neighboring β-Strands to form the β-barrel structure of the voltage-dependent anion channel, human isoform 1 (hVDAC1) precedes membrane insertion and is largely driven by polar interactions between basic and acidic amino acid side-chains ...
Our observations show that blocked arginine- and arginine-containing peptides bound more tightly to GAGs than the analogous lysine species and suggest that the difference was due to the intrinsic properties of the arginine and lysine side chains. The greater affinity of the guanidino cation for ...
Moreover, recent evidence reveals other redox-sensitive sites apart from cysteine modifications, including protein carbonylation, methionine oxidation, and hydroxylation. For example, protein carbonylation occurs through direct oxidation of side chains of lysine, arginine, prolines, and threonine or by cova...
In addition, comparison of 3D structures of two peptides showed significantly different structural motifs near the N-terminal regions, where MCa but not IpTxa has a β-strand and makes the hydrophobic core by connecting to the side chains of four cysteine residues, Cys10, Cys16, Cys21, and...
The peptides with C-terminal phosphonate residues related to phenylalanine, other aromatic amino acids or amino acids with long aliphatic side chains are potent and specific inhibitors of chymotrypsin and chymotrypsin-like enzymes. The peptides with C-terminal phosphonate residues related to ornithine, ...
B, compares the derCD23 and 2H2R Ca2+-free sCD23 structures (15), with Arg172 (red) and Lys173 (blue) high-lighted and the positions of the extended side chains shown in panels ii and iv. C, compares as a ribbon diagram twenty individual NMR structures close to the RKC motif (14...
the side chains of Arg/Lys are longer than Leu/Ile, making them more accessible to the graphene surface. Second and more importantly, while Arg/Lys are usually exposed to solvent in the native structure of the protein, Leu/Ile are highly packed in the hydrophobic environment of the interior...
In contrast, the two Ca2+ sites seen in the PsbO possess at least three ligands from amino acid side chains (Fig. 6, B and C) and thus are potentially of high affinity. In the homologous PsbO from spinach, which has also been reported to bind Ca2+ (69, 70, 71), Asn-197 and ...