88 research outputs found

    On the Long Lasting “C‐Type” Structures in the Sodium Lidargram: The Lifetime of Kelvin‐Helmholtz Billows in the Mesosphere and Lower Thermosphere Region

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    In order to understand the characteristics of long‐lasting “C‐type” structure in the Sodium (Na) lidargram, six cases from different observational locations have been analyzed. The Na lidargram, collected from low‐, middle‐, and high‐latitude sites, show long lifetime of the C‐type structures which is believed to be the manifestation of Kelvin‐Helmholtz (KH) billows in the Mesosphere and Lower Thermosphere (MLT) region. In order to explore the characteristics of the long‐lasting C‐type structures, the altitude profile of square of Brunt‐Väisälä frequency in the MLT region has been derived using the temperature profile collected from the Na lidar instruments and the SABER instrument onboard TIMED satellite. It is found to be positive in the C‐type structure region for all the six cases which indicates that the regions are convectively stable. Simultaneous wind measurements, which allowed us to calculate the Richardson numbers and Reynolds numbers for three cases, suggest that the regions where the C‐type structure appeared were dynamically stable and nonturbulent. This paper brings out a hypothesis wherein the low temperature can increase the magnitude of the Prandtl number and convectively stable atmospheric region can cause the magnitude of Reynolds number to decrease. As a consequence, the remnant of previously generated KH billows in nearly “frozen‐in” condition can be advected through this conducive region to a different location by the background wind where they can sustain for a long time without much deformation. These long‐lived KH billows in the MLT region will eventually manifest the long‐lasting C‐type structures in the Na lidargram

    Mutation D816V Alters the Internal Structure and Dynamics of c-KIT Receptor Cytoplasmic Region: Implications for Dimerization and Activation Mechanisms

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    The type III receptor tyrosine kinase (RTK) KIT plays a crucial role in the transmission of cellular signals through phosphorylation events that are associated with a switching of the protein conformation between inactive and active states. D816V KIT mutation is associated with various pathologies including mastocytosis and cancers. D816V-mutated KIT is constitutively active, and resistant to treatment with the anti-cancer drug Imatinib. To elucidate the activating molecular mechanism of this mutation, we applied a multi-approach procedure combining molecular dynamics (MD) simulations, normal modes analysis (NMA) and binding site prediction. Multiple 50-ns MD simulations of wild-type KIT and its mutant D816V were recorded using the inactive auto-inhibited structure of the protein, characteristic of type III RTKs. Computed free energy differences enabled us to quantify the impact of D816V on protein stability in the inactive state. We evidenced a local structural alteration of the activation loop (A-loop) upon mutation, and a long-range structural re-organization of the juxta-membrane region (JMR) followed by a weakening of the interaction network with the kinase domain. A thorough normal mode analysis of several MD conformations led to a plausible molecular rationale to propose that JMR is able to depart its auto-inhibitory position more easily in the mutant than in wild-type KIT and is thus able to promote kinase mutant dimerization without the need for extra-cellular ligand binding. Pocket detection at the surface of NMA-displaced conformations finally revealed that detachment of JMR from the kinase domain in the mutant was sufficient to open an access to the catalytic and substrate binding sites

    Topological vitali measure spaces

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    Using a tightRope ®

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