Download Curriculum Vitae

Lukasz Joachimiak received his B.S. in Biochemistry from the University of Wisconsin-Madison in 2000.  He received his Ph.D. in 2007 working in the lab of David Baker at University of Washington where he established computational tools to define the energetic and structural principles that underlie protein-protein interactions.  He completed his postdoctoral work with Judith Frydman at Stanford University where he developed innovative approaches to understand the structure and mechanics of substrate interaction by the eukaryotic chaperonin TRiC/CCT.

At UT Southwestern Medical Center, Dr. Joachimiak's laboratory will utilize structural and biochemical approaches to dissect the role of chaperones and protein misfolding in neurodegenerative diseases.  His group is also interested in integrating experimental and computational methods to predict the structures of protein complexes not tractable by classical structural biology techniques.





University of Wisconsin - Madi (2001), Biochemistry
Graduate School
University of Washington (2007), Biochemistry

Research Interest

  • Chaperone structual biology
  • Molecular recognition and specificity
  • Neurodegeneration


Featured Publications LegendFeatured Publications

xTract: software for characterizing conformational changes of protein complexes by quantitative cross-linking mass spectrometry.
Walzthoeni T, Joachimiak LA, Rosenberger G, Röst HL, Malmström L, Leitner A, Frydman J, Aebersold R Nat. Methods 2015 Dec 12 12 1185-90
The structural basis of substrate recognition by the eukaryotic chaperonin TRiC/CCT.
Joachimiak LA, Walzthoeni T, Liu CW, Aebersold R, Frydman J Cell 2014 Nov 159 5 1042-55
Chemical cross-linking/mass spectrometry targeting acidic residues in proteins and protein complexes.
Leitner A, Joachimiak LA, Unverdorben P, Walzthoeni T, Frydman J, Förster F, Aebersold R Proc. Natl. Acad. Sci. U.S.A. 2014 Jul 111 26 9455-60
Exogenous delivery of chaperonin subunit fragment ApiCCT1 modulates mutant Huntingtin cellular phenotypes.
Sontag EM, Joachimiak LA, Tan Z, Tomlinson A, Housman DE, Glabe CG, Potkin SG, Frydman J, Thompson LM Proc. Natl. Acad. Sci. U.S.A. 2013 Feb 110 8 3077-82
A gradient of ATP affinities generates an asymmetric power stroke driving the chaperonin TRIC/CCT folding cycle.
Reissmann S, Joachimiak LA, Chen B, Meyer AS, Nguyen A, Frydman J Cell Rep 2012 Oct 2 4 866-77
The molecular architecture of the eukaryotic chaperonin TRiC/CCT.
Leitner A, Joachimiak LA, Bracher A, Mönkemeyer L, Walzthoeni T, Chen B, Pechmann S, Holmes S, Cong Y, Ma B, Ludtke S, Chiu W, Hartl FU, Aebersold R, Frydman J Structure 2012 May 20 5 814-25
Cryo-EM structure of a group II chaperonin in the prehydrolysis ATP-bound state leading to lid closure.
Zhang J, Ma B, DiMaio F, Douglas NR, Joachimiak LA, Baker D, Frydman J, Levitt M, Chiu W Structure 2011 May 19 5 633-9
A de novo protein binding pair by computational design and directed evolution.
Karanicolas J, Corn JE, Chen I, Joachimiak LA, Dym O, Peck SH, Albeck S, Unger T, Hu W, Liu G, Delbecq S, Montelione GT, Spiegel CP, Liu DR, Baker D Mol. Cell 2011 Apr 42 2 250-60
Experimental and computational analyses of the energetic basis for dual recognition of immunity proteins by colicin endonucleases.
Keeble AH, Joachimiak LA, Maté MJ, Meenan N, Kirkpatrick N, Baker D, Kleanthous C J. Mol. Biol. 2008 Jun 379 4 745-59
Computational design of a new hydrogen bond network and at least a 300-fold specificity switch at a protein-protein interface.
Joachimiak LA, Kortemme T, Stoddard BL, Baker D J. Mol. Biol. 2006 Aug 361 1 195-208

Honors & Awards

  • Endowed Scholar Award