Bio
Professor Rajni Kant, Ph.D FRSC, is a distinguished academician and researcher in the field of Physics, specializing in Condensed Matter Physics and X-ray Crystallography. He is affiliated with the Chemical Crystallography Laboratory, Department of Physics, University of Jammu, India. With over 30 publications and 189 citations, his h-index stands at 9 and i10-index at 9. He has supervised 26 Ph.D and 51 M.Phil scholars and completed 18 research projects. He also holds a Ph.D in Chemistry from Dr. B. R. Ambedkar National Institute of Technology Jalandhar (2021) and currently serves as an Assistant Professor at Baba Farid College, Bathinda. His research contributions include synthesis, crystal structure analysis, and molecular docking studies.
Educational Journey
Dr. B. R. Ambedkar National Institute of Technology Jalandhar
Ph.D in Chemistry • Chemistry
2021University of Jammu
Ph.D, Post-Ph.D, M.Phil, M.Sc, B.Sc • Physics (Condensed Matter Physics/X-ray Crystallography)
Experience
Baba Farid College
Assistant Professor
2024 - Present • ChemistryResearch
Synthesis, Crystal Structure, Hirshfeld Surface, Energy Framework and Molecular Docking of 2-(((6-Methoxy pyridin-3-yl)imino)methyl)Phenol
The structure of 2-(((6-methoxypyridin-3- yl)imino)methyl)phenol (MPIMP) (C13H12N2O2) has been determined by X-ray diffraction methods. It crystallizes in the tetragonal crystal system with space group P42/n and unit cell dimensions a = 14.2958(3) Å, b = 14.2958(3) Å, c = 11.0179(3) Å, V = 2251.73(12) Å3, Z = 8. The structure has been refined by full-matrix least square procedure to a final R-value of 0.0518(wR2 = 0.1312) for 1709 observed reflections. The molecules linked via two intermolecular (CH… N and C-H…O) hydrogen bonds. The crystal structure was further stabilized by a strong intramolecular N-H…O hydrogen bond. The Hirshfeld surface analysis reveals the interaction contacts of the molecule and the strength of molecular packing in the crystal. The energy framework has been performed through different intermolecular interaction energies for structural stability. The molecular docking of MPIMP was performed against tuberculosis enzyme Decaprenylphosphoryl- b-Dribose 20-epimerase (DprE1, PDB code: 4KW5) to reconnoiter the binding interactions at the active sites.
