Spin-1/2 orthogonal-dimer chain composed of regularly alternating Ising and Heisenberg dimers is exactly solved in a presence of the magnetic field by the transfer-matrix method. It is shown that the ground-state phase diagram involves in total six different phases. Besides the ferromagnetic phase with fully polarized spins one encounters the singlet antiferromagnetic and modulated antiferromagnetic phases manifested in zero-temperature magnetization curves as zero magnetization plateau, the frustrated ferrimagnetic and singlet ferrimagnetic phases causing existence of an intermediate one-half magnetization plateau, and finally, the intriguing modulated ferrimagnetic phase with a translationally broken symmetry leading to an unconventional one-quarter magnetization plateau. The quantum character of individual ground states is quantified via the concurrence, which measures a strength of the bipartite entanglement within the pure and mixed states of the Heisenberg dimers at zero as well as nonzero temperatures. The parameter region, where the bipartite entanglement may be in contrast to general expectations reinforced upon increasing of temperature and/or magnetic field, is elucidated. ith six-spin cluster J H ( ) J I ' J I J I J I J I S 2,i-1
The interactions of epoxiconazole and prothioconazole with human serum albumin and bovine serum albumin were investigated using spectroscopic methods complemented with molecular modeling. Spectroscopic techniques showed the formation of pesticide/serum albumin complexes with the static type as the dominant mechanism. The association constants ranged from 3.80 × 104–6.45 × 105 L/mol depending on the pesticide molecule (epoxiconazole, prothioconazole) and albumin type (human or bovine serum albumin). The calculated thermodynamic parameters revealed that the binding of pesticides into serum albumin macromolecules mainly depended on hydrogen bonds and van der Waals interactions. Synchronous fluorescence spectroscopy and the competitive experiments method showed that pesticides bind to subdomain IIA, near tryptophan; in the case of bovine serum albumin also on the macromolecule surface. Concerning prothioconazole, we observed the existence of an additional binding site at the junction of domains I and III of serum albumin macromolecules. These observations were corroborated well by molecular modeling predictions. The conformation changes in secondary structure were characterized by circular dichroism, three-dimensional fluorescence, and UV/VIS absorption methods.
Studies of interactions between pesticides and target mammalian proteins are important steps toward understanding the pesticide′s toxicity. Using calorimetric and spectroscopic methods, the interaction between triazole fungicide tebuconazole and human serum albumin has been investigated. The spectroscopic techniques showed that fluorescence quenching of human serum albumin by tebuconazole was the result of the formation of tebuconazole/human serum albumin complex with the static type as the dominant mechanism. The association constant was found to be 8.51 × 103 L/mol. The thermodynamic parameters were obtained as ΔH = −56.964 kJ/mol, ΔS = −115.98 J/mol·K. The main active interactions forming the tebuconazole/human serum albumin complex were identified as the interplay between hydrogen bonds and/or van der Waals forces, based on thermodynamic experiments. These binding modes were corroborated well by the predictions of molecular modeling. Hydrogen bonding of tebuconazole with Arg222, Ala215 and Ala291 of human serum albumin played a relevant role in binding. The conformation changes in secondary structure were characterized by circular dichroism and 3D fluorescence spectra.
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