RV
Rajan Vyas
Shiv Nadar University, Central University of Punjab, Panjab University, Case Western Reserve University
About
My research interest includes the use of X-ray crystallography as a major technique to determine the structure and function of proteins such as membrane proteins, DNA polymerases, and other soluble proteins. The structural studies are coupled to the other biochemical and biophysical methods in order to establish the mechanisms of the respective proteins.
Employment
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Shiv Nadar University Assistant Professor2020 - Present
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Central University of Punjab Assistant Professor/Ramalingaswami Fellow2018 - 2020
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Case Western Reserve University Postdoctoral Fellow2015 - 2017
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Ohio State University Postdoctoral Fellow2012 - 2014
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National Institute of Immunology Postdoctoral Fellow2010 - 2012
Education
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Panjab University Ph.D2004 - 2010
Projects & Funding
Projects & funding information is unavailable.
Publications (20)
- An Aerobic in Vitro Cell Lysate-based Method for Fe-S Cluster Reconstitution in Recombinant Rv1460 Protein from Mycobacterium tuberculosis H37Rv Save
- Unveiling the silent defenders: mycobacterial stress sensors at the forefront to combat tuberculosis Save
- Structural insights into the substrate specificity of SP_0149, the substrate-binding protein of a methionine ABC transporter from Streptococcus pneumoniae Save
- The voltage-gated sodium channel pore exhibits conformational flexibility during slow inactivation Save
- Structural basis for the D-stereoselectivity of human DNA polymerase β Save
- Structural Insights into the Post-Chemistry Steps of Nucleotide Incorporation Catalyzed by a DNA Polymerase Save
- Crystal structures of Mycobacterium tuberculosis HspAT and ArAT reveal structural basis of their distinct substrate specificities Save
- VCP recruitment to mitochondria causes mitophagy impairment and neurodegeneration in models of Huntington's disease Save
- Mechanistic Basis for the Bypass of a Bulky DNA Adduct Catalyzed by a Y-Family DNA Polymerase Save
- Viewing human DNA polymerase β faithfully and unfaithfully bypass an oxidative lesion by time-dependent crystallography Save