In order to realize the tram's low-floor structure, most of the trams that have been recently introduced adopt an independently rotating wheelset. In the case of trains driving in two regions with different gauges, an independently rotating wheelset may be applied to utilize the variable track technology. Since the independent rotation type wheelset has no rotational restraint of the left and right wheels, the difference in rotational speed between the outer and inner wheels occurs naturally during curved driving, and it is applied to railroad vehicles traveling in steep curve sections because it smoothly drives curved driving. However, the longitudinal creep force and the lateral restoring force are weakened as the left and right rotational constraints disappear. Lack of transverse direction restoring force weakens stability while causing continuous flange contact driving or zigzag phenomenon against disturbance. Under the conditions of driving in a steep curve, these railway vehicles generate excessive wear, noise, and lateral pressure, as well as deterioration of ride comfort and derailment. In order to overcome these drawbacks, a method has been proposed in which the torque of a motor mounted on each wheel is individually controlled to generate lateral restoring force or to improve driving performance through lateral displacement control using a yaw moment. In this paper, development using HILs was performed to check the performance and stability of the individual motor torque control technology before verifying by applying the individual motor torque control to the actual vehicle. HILs were constructed by combining a real-time dynamic analysis model of a railway vehicle with a drive motor to which real individual motor control was applied. Under the conditions of driving the test track where the actual test vehicle was tested, the analysis of the driving characteristics and the control characteristics of the disturbance was performed to confirm the proposed individual motor torque control performance.

The formation of inclusion complexes between alkylsulfonate guests and a cationic pillar[5]arene receptor in water was investigated by NMR and ITC techniques. The results show the formation of host-guest complexes stabilized by electrostatic interactions and hydrophobics effects with binding constants of up to 107 M-1 for the guest with higher hydrophobic character. Structurally, the alkyl chain of the guest is included in the hydrophobic aromatic cavity of the macrocycle while the sulfonate groups are hold in the multicationic portal by ionic interactions.

The affinity constant, also known as the equilibrium constant, binding constant, equilibrium association constant, or the reciprocal value, the equilibrium dissociation constant (K_d), can be considered as one of the most important characteristics for any antibody-antigen pair. Many methods based on different technologies have been proposed and used to determine this value. However, since a very large number of publications and commercial datasheets do not include this information, significant obstacles in performing such measurements seem to exist. In other cases where such data are reported, the results have often proved to be unreliable. This situation may indicate that most of the technologies available today require a high level of expertise that does not seem to be available in many laboratories. In this paper, we present a simple approach based on standard immunoassay technology that is easy and quick to perform. It relies on the effect that the molar IC₅₀ approaches the K_d value in the case of infinitely small concentrations of the reagent concentrations. A two-dimensional dilution of the reagents leads to an asymptotic convergence to K_d. The approach has some similarity to the well-known checkerboard titration used for the optimization of immunoassays. A well-known antibody against the FLAG peptide, clone M2, was used as a model system and the results were compared with other methods. This approach could be used in any case where a competitive assay is available or can be developed. The determination of an affinity constant should belong to the crucial parameters in any quality control of antibody-related products and assays and should be mandatory in papers using immunochemical protocols.