Interaction between aspartic acid and D-glucose, D-galactose, and D-fructose has been studied by isothermal titration calorimetry, calorimetry of dissolution, and densimetry. It has been found that D-glucose and D-fructose form thermodynamically stable associates with aspartic acid, in contrast to D-galactose. The selectivity in the interaction of aspartic acid with monosaccharides is affected ...

Detailed stopped-flow studies in combination with site-directed mutagenesis, isothermal titration calorimetry data and x-ray crystallographic knowledge have revealed that the biphasic pre-equilibrium fluorescence changes reported for a single Ig-binding domain of protein L from Peptostreptococcus magnus binding to kappa light chain are due to the binding of the kappa light chain at two separate...

Two [60]fullerene dumbbell-like molecules with a single or double perylene-3,4,9,10-tetracarboxylic acid bisimide (PBI) linker were synthesized to study the structural and photophysical properties in addition complex formation [10]cycloparaphenylene ([10]CPP). Due their special optical properties, it is possible describe complexation using conventional spectroscopic methods such as NMR fluoresc...

Ultrasmall gold nanoparticles with a metallic core diameter of 2 nm were surface-conjugated peptides that selectively target epitopes on the surface WW domain model protein hPin1 (hPin1-WW). The binding to was accomplished via thiol group terminal cysteine. particles analyzed by NMR spectroscopy, high-resolution transmission electron microscopy, and differential centrifugal sedimentation. loadi...

Internalization of G-protein-coupled receptors is mediated by phosphorylation of the C-terminus, followed by binding with the cytosolic protein arrestin. To explore structural factors that may play a role in internalization of cannabinoid receptor 1 (CB1), we utilize a phosphorylated peptide derived from the distal C-terminus of CB1 (CB1(5P)(454-473)). Complexes formed between the peptide and h...

Dipeptidyl peptidase III (DPP III, EC 3.4.14.4) is a monozinc metalloexopeptidase that hydrolyzes dipeptides from the N-terminus of peptides consisting three or more amino acids. Recently, DPP has attracted great interest scientists, and numerous studies have been conducted showing it involved in regulation various physiological processes. Since only metalloenzyme among dipeptidyl peptidases, w...