Unveiling the structural mechanisms behind high affinity and selectivity in phosphorylated epitope-specific rabbit antibodies.

Protein phosphorylation is a crucial process in various cellular functions, and its irregularities have been implicated in several diseases, including cancer. Antibodies are commonly employed to detect protein phosphorylation in research. However, unlike the extensive studies on recognition mechanisms of the phosphate group by proteins such as kinases and phosphatases, only a few studies have explored antibody mechanisms.

Programmable generation of counterrotating bicircular light pulses in the multi-terahertz frequency range.

The manipulation of solid states using intense infrared or terahertz light fields is a pivotal area in contemporary ultrafast photonics research. While conventional circular polarization has been well explored, the potential of counterrotating bicircular light remains widely underexplored, despite growing interest in theory. In the mid-infrared or multi-terahertz region, experimental challenges lie in difficulties in stabilizing the relative phase between two-color lights and the lack of available polarization elements.

Ultra-broadband detection of coherent infrared pulses by sum-frequency generation spectroscopy in reflection geometry.

We have newly developed, to the best of our knowledge, a detection method for broadband infrared pulses based on sum-frequency generation spectroscopy in reflection geometry, which can avoid a restriction of the detection bandwidth originating from the phase mismatch that is inevitable for the upconversion in transmission geometry. Using a GaAs crystal, we successfully demonstrated the ultra-broadband detection of the infrared pulses generated from a two-color laser-induced air plasma filament in a region from 300 to 3300 cm. With the advantage of ultra-short infrared pulses, the present detection method holds promise for application to time-resolved, ultra-broadband vibrational spectroscopy.

Impact of single-residue mutations on protein thermal stability: The case of threonine 83 of BC2L-CN lectin.

The thermal stability of trimeric lectin BC2L-CN was investigated and found to be considerably altered when mutating residue 83, originally a threonine, located at the fucose-binding loop. Mutants were analyzed using differential scanning calorimetry and isothermal microcalorimetry. Although most mutations decreased the affinity of the protein for oligosaccharide H type 1, six mutations increased the melting temperature (T) by >5 °C; one mutation, T83P, increased the T value by 18.