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https://www.selleckchem.com/products/mrtx0902.html The COVID-19 pandemic is caused by SARS-CoV-2. Currently, most of the research efforts towards the development of vaccines and antibodies against SARS-CoV-2 were mainly focused on the spike (S) protein, which mediates virus entry into the host cell by binding to ACE2. As the virus SARS-CoV-2 continues to spread globally, variants have emerged, characterized by multiple mutations of the S glycoprotein. Herein, we employed microsecond-long molecular dynamics simulations to study the impact of the mutations of the S glycoprotein in SARS-CoV-2 Variant of Concern 202012/01 (B.1.1.7), termed the "UK variant", in comparison with the wild type, with the aim to decipher the structural basis of the reported increased infectivity and virulence. The simulations provided insights on the different dynamics of UK and wild-type S glycoprotein, regarding in particular the Receptor Binding Domain (RBD). In addition, we investigated the role of glycans in modulating the conformational transitions of the RBD. The overall results showed that the UK mutant experiences higher flexibility in the RBD with respect to wild type; this behavior might be correlated with the increased transmission reported for this variant. Our work also adds useful structural information on antigenic "hotspots" and epitopes targeted by neutralizing antibodies.The ballasted track superstructure is characterized by a relative quick deterioration of track geometry due to ballast settlements and the accumulation of sleeper voids. The track zones with the sleeper voids differ from the geometrical irregularities with increased dynamic loading, high vibration, and unfavorable ballast-bed and sleeper contact conditions. This causes the accelerated growth of the inhomogeneous settlements, resulting in maintenance-expensive local instabilities that influence transportation reliability and availability. The recent identification and evaluation of the sleeper support condit

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