Lee Lab Protein Research

Selected Publications

  • Sapienza PJ, Bonin JP, Jinasena DHP, Li K, Dieckhaus H, Popov KI, Aubé J, and Lee AL, Mixed, non-classical behavior in a classic allosteric protein, Proc. Natl. Acad. Sci. 120, e2308338120 (2023).
  • Jain, A, Dokholyan, NV and Lee, AL, Allosteric inactivation of an engineered optogenetic GTPase, Proc. Natl. Acad. Sci. 120, e2219254120 (2023).
  • Bonin, JP, Sapienza, PJ & Lee, AL (2022). Dynamic allostery in substrate binding by human thymidylate synthase. eLife, 11, e79915.
  • Sapienza PJ, Currie MM, Lancaster NM, Li K, Aubé J, Goldfarb D, Cloer EW, Major MB, and Lee AL, Visualizing an Allosteric Intermediate Using CuAAC Stabilization of an NMR Mixed Labeled Dimer, ACS Chem Biol (2021), 16(12):2766-2775. doi: 10.1021/acschembio.1c00617.
  • Wang J, Jain A, McDonald LR, Gambogi C, Lee AL, and Dokholyan NV, Mapping allosteric communications within individual proteins, Nature Communications (2020), 11, 3862.
  • Bonin JP, Sapienza PJ, Wilkerson E, Goldfarb D, Wang L, Herring L, Chen X, Major MB, and Lee AL, Positive cooperativity in substrate binding by human thymidylate synthase, Biophysical Journal (2019), 117, 1074-1084.
  • Sapienza PJ, Popov KI, Mowrey DD, Falk BT, Dokholyan NV, and Lee AL, Inter-active site communication mediated by the dimer interface beta-sheet in the half-the-sites enzyme, thymidylate synthase, Biochemistry (2019), 58, 3302-3313.
  • Lee AL and Sapienza PJ,  Thermodynamic and NMR assessment of ligand cooperativity and intersubunit communication in symmetric dimers:  application to thymidylate synthase, Frontiers in Molecular Biosciences (2018), 5, article 47.  doi: 10.3389/fmolb.2018.00047.
  • Sapienza PJ and Lee AL, Widespread perturbation of function, structure, and dynamics by a conservative single atom substitution in thymidylate synthase, Biochemistry (2016), 55, 5702-5713.
  • Falk BT, Sapienza PJ, and Lee AL, Chemical shift imprint of intersubunit communication in a symmetric homodimer, Proc. Natl. Acad. Sci. U.S.A. (2016), 113, 9533-9538.  (Commentary in same issue, pp. 9407-9409).