Dr. Jordan Chill

Senior Lecturer
Dr. Jordan Chill


Proteins, the molecular machinery of cells, are involved in all aspects of cellular biochemistry and biology. A comprehensive understanding of how proteins perform their biological roles and how these are regulated in the context of tissues and organisms requires the three-dimensional structure of these fascinating polymers to be known. An important method for studying the structure of proteins is nuclear magnetic resonance (NMR), which measures spectroscopic parameters of magnetic nuclei (protons and certain isotopes of nitrogen and carbon) in order to glean information about their spatial coordinates.

During his PhD studies (with Prof. Jacob Anglister, Weizmann Institute) Dr. Chill studied the structure of the cellular receptor for interferon (IFN) in humans, resulting in the first available structure of the IFN receptor, as well as a map of hydrophobic and electrostatic interactions by which the receptor recognizes its ligand and begins the IFN signaling pathway. These findings can now be utilized by pharmaceutical companies to search for more effective IFN-based therapies. During his post-doctoral studies (with Dr. Ad Bax, NIDDK/NIH, USA) Dr, Chill focused on membrane-associated proteins (MPs), hydrophobic proteins which are embedded in the cellular membrane and are involved in transport, recognition and membrane structure. At the NIH Chill learned and designed new NMR methods sufficiently sensitive to obtain structural information for a 68-kDa ion channel, an incredible size for an NMR study.

Dr, Chill arrived at Bar-Ilan University in October 2007 and formed the bio-NMR lab. His research group applies NMR methods to study the structure, dynamics and function of proteins with an emphasis on MPs, and with possible applications to health and disease. In June 2008 the Ultra-shielded 700-MHz Bruker spectrometer was successfully installed, including a cryogenic probe optimized for 13C detection. This experimental setup allows the group to run state-of-the-art experiments for studying proteins. The group includes a research assistant and six graduate students. Since milligram quantities of proteins are required for acquisition of NMR data, the group invests significant efforts in optimization of protein overexpression in bacterial systems, and purification using analytical and biochemical methods so that sufficiently pure protein samples can be prepared. NMR measurements conducted on these samples offer structural and dynamic information which uncovers the structural basis of the functions observed for proteins.   

Particular research areas (projects)

1. The KcsA potassium channel - structural basis for channel inhibition by toxins

2. Intrinsically disordered proteins, methods for their study by NMR

3. Protein-protein interactions affecting the cytoskeleton and actin polymerization

4. Membrane spanning peptides – how viral invasion of the membrane occurs.




  1. Bermel, W.; Bertini, I.; Chill, J.H.; Felli, I.C.; Haba, N.Y.; Kumar, M.V.; Pierattelli, R. 13C-direct detection amino acid selective NMR experiments to simplify the assignment of IDPs. ChemBioChem, 2012,.13(16), 2425-2432.
  2. Novacek, J.; Haba, N.; Chill, J.H.; Zidek, L.; Sklenar, V.; 4D non-uniformly sampled HabCabCON/intra-HabCabNCO experiments for the sequential assignment and chemical shift analysis of intrinsically disordered proteins. J. Biomol. NMR. 2012, 53(2), 139-148.
  3. Kamnesky, G.; Shaked, H.; Chill, J.H.; The distal C-terminal region of the KcsA potassium channel is a pH-dependent tetramerization domain. J. Mol. Biol. 2012, 418(3-4), 237-247.
  4. Chill, J.H.; Naider, F.N. A solution NMR view of protein dynamics in the biological membrane. Curr. Opin. Struc. Biol. 2011, 21, 627-633.
  5. Chill, J.H.; Louis, J.M.; Delaglio, F.; Bax A. Local and global structure of the monomeric subunit of the potassium channel KcsA probed by NMR. Biochim. Biophys. Acta  2007, 1768(12), 3260-3270.
  6. Ying, J.; Chill, J.H.; Louis, J.M.; Bax A. Mixed-time parallel evolution and multiple quantum NMR experiments: sensitivity and resolution enhancement in heteronuclear NMR. J. Biomol. NMR, 2007, 37(3), 195-204.
  7. Quadt-Akabayov, S.R.; Chill, J.H.; Levy, R.; Kessler, N.; Anglister J. Determination of the human type I interferon receptor binding site on human interferon a2 by cross saturation and an NMR-based model of the complex. Protein Sci., 2006, 15(11), 2656-2668.
  8. Chill, J.H.; Louis, J.M.; Baber, J.L.; Bax A. Measurement of 15N relaxation in the detergent-solubilized tetrameric KcsA potassium channel. J. Biomol NMR, 2006, 36(2), 123-136.
  9. Chill, J.H.; Louis, J.M.; Miller, C.; Bax A. NMR study of the tetrameric KcsA potassium channel in detergent micelles. Protein Sci, 2006, 15(4), 684-698.
  10. Samson, A.O.; Chill, J.H.; Anglister J. 2D-measurement of proton T1ρ relaxation in unlabeled proteins: Mobility changes in a-bungarotoxin upon binding of an acetylcholine receptor peptide. Biochemistry, 2005, 44(32), 10926-10934. 
  11. Rozen, O.; Chill, J.H.; Kessler, N.; Mester, B.; Sharon, M.; Zolla-Pazner, S.; Anglister J. Induced fit in HIV-neutralizing antibody complexes: evidence for alternative conformations of the gp120 V3 loop and the molecular basis for broad neutralization. Biochemistry, 2005, 44(19), 7250-7258.
  12. Chill, J.H.; Quadt, S.R.; Anglister J. Backbone dynamics of the human type I interferon receptor, a representative α-helical cytokine receptor. Biochemistry, 2004, 43(31), 10127-10137. (Corresponding author).
  13. Chill, J.H.; Quadt, S.R.; Levy, R.; Schreiber, G.; Anglister J. The human type I interferon receptor: NMR structure reveals the molecular basis of ligand binding.  Structure (Camb.), 2003, 11(7), 791-802.
  14. Samson, A.O.; Scherf, T.; Eisenstein, M.; Chill, J.H.; Anglister J. The mechanism for acetylcholine receptor inhibition by a-neurotoxins and species-specific resistance to a-bungarotoxin revealed by NMR. Neuron, 2002, 35(2), 319-332.  
  15. Yao, Y.; Wang, J.; Viroonchatapan, N.; Samson, A.O.; Chill, J.H.; Rothe, E.; Anglister, J.; Wang, Z.Z. The human interferon receptor: Yeast expression and NMR analysis of the extracellular domain of muscle nicotinic acetylcholine receptor alpha subunit. J. Biol. Chem. 2002, 277(15), 12613-12621.
  16. Chill, J.H.; Nivasch, R.; Levy, R.; Albeck, S.; Schreiber, G.; Anglister, J. The human interferon receptor: NMR-based modeling, mapping of the IFN-α2 binding site, and observed ligand-induced tightening. Biochemistry. 2002, 41(11), 3575-3585
  17. Samson, A.O.; Chill, J.H.; Rodrigeuz, E.; Scherf, T.; Anglister, J. NMR mapping and secondary structure determination of the major acetylcholine receptor alpha-subunit determinant interacting with alpha-bungarotoxin. Biochemistry 2001, 40(18), 5464-5473.



84-102          Inorganic Chemistry       1st year undergrad          Sun 14-16, Mon 12-14


84-997          Magnetic resonance        Graduate                        Tue 12-14


84-887          Biomaterials and              undergrad/graduate       Sun 16-18



1. The KcsA potassium channel - structural basis for channel inhibition by toxins

2. Intrinsically disordered proteins, methods for their study by NMR

3. Protein-protein interactions affecting the cytoskeleton and actin polymerization

4. Membrane spanning peptides – how viral invasion of the membrane occurs.

Research Group

Group Members


Research Assistant

Dr. Hadassa Shaked


PhD candidates

Renana Gross

Guy Kamnesky                            

Hadas Zazrin

Eva Skop

Inbal Sher                           

Adi Halle-Bikovski

Nati Mendelman                           


MSc candidates

Adi Shane

Orel Hirschhorn