Richard Gillilan

Richard Gillilan
Visiting Scientist
607-255-0917
reg8@cornell.edu
Education/Experience:

 2021             Fellow of the American Crystallographic Association

2024-presentVisiting Scientist, Cornell High Energy Synchrotron Source, Cornell University
2000-2024Sr Staff Scientist, Cornell High Energy Synchrotron Source, Cornell University
1992-2000Research Scientist, Visualization Specialist, Sr Tech Advisor, Cornell Theory Center
1990-1992Postgraduate Research Chemist, University of California, San Diego
1988-1990Postdoctoral Research Associate, Cornell University
1988Ph.D. Chemistry, University of Pennsylvania
1983B.A. Chemistry (honors), Mathematics, University of Maryland, Baltimore County
Research Interests:

Extreme biophysics, structural proteomics, high pressure biology and deep life, small-angle X-ray solution scattering, biophysical instrumentation and separation science, x-ray optics, protein-protein interactions (simulation and experiment), aggregation, stability and phase separation, origin of life.

Article about my recent research (Physics Magazine): https://physics.aps.org/articles/v17/132
Recent Publications:
  • H. M. Moran, E. Manriquez-Sandoval, P. Sharma, S. D. Fried, and R. E. Gillilan, Proteome-Wide Assessment of Protein Structural Perturbations under High Pressure, PRX Life 2, 033011 (2024).
  • Winnikoff, J. R. et al. Homeocurvature adaptation of phospholipids to pressure in deep-sea invertebrates. Science 384, 1482–1488 (2024).
  • Li, Y., Li, Q., Gillilan, R. E. & Abbaspourrad, A. Reversible disassembly-reassembly of C-phycocyanin in pressurization-depressurization cycles of high hydrostatic pressure. International Journal of Biological Macromolecules 253, 127623 (2023).
  • Chowdhury, A. A. et al. Characterizing Protein–Protein Interactions and Viscosity of a Monoclonal Antibody from Low to High Concentration Using Small-Angle X-ray Scattering and Molecular Dynamics Simulations. Mol. Pharmaceutics (2023) doi:10.1021/acs.molpharmaceut.3c00484.
  • Biswas, S. et al. Understanding the Impacts of Molecular and Macromolecular Crowding Agents on Protein–Polymer Complex Coacervates. Biomacromolecules (2023) doi:10.1021/acs.biomac.3c00545.
  • Illava, G., Gillilan, R. & Ando, N. Development of in-line anoxic small-angle X-ray scattering and structural characterization of an oxygen-sensing transcriptional regulator. J Biol Chem 105039 (2023) doi:10.1016/j.jbc.2023.105039.
  • Peters, E. et al. Defining the role of the N-terminal helix in the Arf1 nucleotide switch transition using pressure perturbation. Biophysical Journal 122, 329a (2023).
  • Zhang, M. et al. pH-Dependent Solution Micellar Structure of Amphoteric Polypeptoid Block Copolymers with Positionally Controlled Ionizable Sites. Biomacromolecules acs.biomac.3c00407 (2023) doi:10.1021/acs.biomac.3c00407.
  • Wang, J. et al. Pressure pushes tRNALys3 into excited conformational states. Proceedings of the National Academy of Sciences 120, e2215556120 (2023).
  • Ford, R. R. et al. Micelle Formation and Phase Separation of Poloxamer 188 and Preservative Molecules in Aqueous Solutions Studied by Small Angle X-ray Scattering. Journal of Pharmaceutical Sciences 112, 731–739 (2023).
  • *Miller, R. C., Cummings, C., Huang, Q., Ando, N. & Gillilan, R. E. Inline small-angle X-ray scattering-coupled chromatography under extreme hydrostatic pressure. Protein Science 31, e4489 (2022). doi:10.1002/pro.4489
  • *Gillilan, R. E. High-pressure SAXS, deep life, and extreme biophysics. in Methods in Enzymology (Academic Press, 2022). doi:10.1016/bs.mie.2022.08.025.
  • Zhang, S., McCallum, S. A., Gillilan, R. E., Wang, J. & Royer, C. A. High Pressure CPMG and CEST Reveal That Cavity Position Dictates Distinct Dynamic Disorder in the PP32 Repeat Protein. J. Phys. Chem. B (2022) doi:10.1021/acs.jpcb.2c05498.
  • Trewhella J, Vachette P, Bierma J, Blanchet C, Brookes E, Chakravarthy S, Chatzimagas L, Cleveland TE IV, Cowieson N, Crossett B, et al. (2022) A round-robin approach provides a detailed assessment of biomolecular small-angle scattering data reproducibility and yields consensus curves for benchmarking. Acta Crystallographica Section D [Internet] 78. Available from: https://doi.org/10.1107/S2059798322009184
  • Allsopp, R. et al. Antimicrobial Peptide Mechanism Studied by Scattering-Guided Molecular Dynamics Simulation. J. Phys. Chem. B (2022) doi:10.1021/acs.jpcb.2c03193.
  • Lokareddy, R. K. et al. Terminase Subunits from the Pseudomonas-Phage E217. Journal of Molecular Biology 434, 167799 (2022).
  • Florio, T. J. et al. Differential recognition of canonical NF-κB dimers by Importin α3. Nature Communications 13, 1207 (2022).
  • Doll SG, Meshkin H, Bryer AJ, Li F, Ko Y-H, et al. 2022. Recognition of the TDP-43 nuclear localization signal by importin α1/β. Cell Reports. 39(13):111007
  • Zovo, K. et al. Substitution of the Methionine Axial Ligand of the T1 Copper for the Fungal-like Phenylalanine Ligand (M298F) Causes Local Structural Perturbations that Lead to Thermal Instability and Reduced Catalytic Efficiency of the Small Laccase from Streptomyces coelicolor A3(2). ACS Omega (2022) doi:10.1021/acsomega.1c06668.

Full publication list on Google Scholar: https://scholar.google.com/citations?hl=en&user=nj2c0oEAAAAJ&view_op=list_works&sortby=pubdate 

Scopus: https://www.scopus.com/authid/detail.uri?authorId=6701426897

Recent Recorded Lectures: 
Youtube channel: https://www.youtube.com/user/rgill333

CV: CV_09_10_24.pdf