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Creators/Authors contains: "Singh, Jitendra"

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  1. Abstract

    With continued fossil‐fuel dependence, anthropogenic aerosols over South Asia are projected to increase until the mid‐21st century along with greenhouse gases (GHGs). Using the Community Earth System Model (CESM1) Large Ensemble, we quantify the influence of aerosols and GHGs on South Asian seasonal precipitation patterns over the 21st century under a very high‐emissions (RCP 8.5) trajectory. We find that increasing local aerosol concentrations could continue to suppress precipitation over South Asia in the near‐term, delaying the emergence of precipitation increases in response to GHGs by several decades in the monsoon season and a decade in the post‐monsoon season. Emergence of this wetting signal is expected in both seasons by the mid‐21st century. Our results demonstrate that the trajectory of local aerosols together with GHGs will shape near‐future precipitation patterns over South Asia. Therefore, constraining precipitation response to different trajectories of both forcers is critical for informing near‐term adaptation efforts.

     
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  2. Abstract

    Understanding the molecular evolution of the SARS‐CoV‐2 virus as it continues to spread in communities around the globe is important for mitigation and future pandemic preparedness. Three‐dimensional structures of SARS‐CoV‐2 proteins and those of other coronavirusess archived in the Protein Data Bank were used to analyze viral proteome evolution during the first 6 months of the COVID‐19 pandemic. Analyses of spatial locations, chemical properties, and structural and energetic impacts of the observed amino acid changes in >48 000 viral isolates revealed how each one of 29 viral proteins have undergone amino acid changes. Catalytic residues in active sites and binding residues in protein–protein interfaces showed modest, but significant, numbers of substitutions, highlighting the mutational robustness of the viral proteome. Energetics calculations showed that the impact of substitutions on the thermodynamic stability of the proteome follows a universal bi‐Gaussian distribution. Detailed results are presented for potential drug discovery targets and the four structural proteins that comprise the virion, highlighting substitutions with the potential to impact protein structure, enzyme activity, and protein–protein and protein–nucleic acid interfaces. Characterizing the evolution of the virus in three dimensions provides testable insights into viral protein function and should aid in structure‐based drug discovery efforts as well as the prospective identification of amino acid substitutions with potential for drug resistance.

     
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