Prof. Jordan Chill
CV
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 several 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.
Research
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.
Publications
Articles:
40. Qasim. A.; Sher, I.; Hirschhorn, O.; Shaked, H.; Qasim, Z.; Ruthstein, S.; Chill, J.H. A KcsA cytoplasmic pH-gate investigated in lipoprotein nanodiscs. ChemBioChem, 2019, doi: 10.1002/cbic.201800627
39. Baskin, M.; Zhu, H.; Qu, Z.-W.; Chill, J.H.; Grimme, S.; Maayan, G. Folding of unstructured peptoids and heterobimetallic peptoid complexes formation upon side chains-to-metal coordination. Chem. Sci. 2019, doi: 10.1039/c8sc03616k.
38. Halle-Bikovski, A.; Rozentur-Shkop, E.; Shaked, H.; Barda-Saad, M.† Chill, J.H.† From disordered polypeptide to functional regulator: a structural view of WASp-interacting protein and its complex with WASp in human T-cells. Biophysical J. 2018, 114(3), 26a.
37. Belostozky, A.; Richman, M.; Lisiansky, E.; Tovchygrechko, A.; Chill, J.H.; Rahimipour, S. Inhibition of tau-derived hexapeptide aggregation and toxicity by a self-assembled cyclic D,L-α-peptide conformational inhibitor. Chem Commun (Camb) 2018, 54(47), 5890-5893.
36. Halle-Bikovski, A.; Fried, S.; Biber, G.; Rozentur-Shkop, E.; Joseph, N.; Shaked, H.; Barda-Saad, M.† Chill, J.H.† New structural insights into formation of the key actin regulating WIP-WASp complex determined by NMR and molecular imaging. ACS Chem. Biol. 2018, 13(1), 100-109.
35. Levy, A.R.; Nissim, M.; Mendelman, N.; Chill, J.H.; Ruthstein, S. The Ctr1 intracellular loop is involved in the copper transfer mechanism to the Atox1 metallochaperone. J. Phys. Chem. B. 2016, 120(48), 12334-12345.
34. Rozentur-Shkop, E.; Goobes, G.; Chill, J.H. A J-modulated protonless NMR experiment characterizes the conformational ensemble of the intrinsically disordered protein WIP. J. Biomol NMR 2016, 66(4), 243-257s.
33. Barber-Zucker, S.; Uebe, R.; Davidov, G.; Navon, Y.; Sherf, D.; Chill, J.H.; Kass, I.; Bitton, R.; Schüler, D.; Zarivach R. Disease-homologous mutation in the cation diffusion facilitator protein MamM causes single-domain structural loss and signifies its importance. Sci. Rep. 2016, 6, 31933.
32. Chemerovski-Glikman, M.; Rozentur-Shkop, E.; Richman, M.; Grupi, A.; Getler, A.; Cohen, H.Y.; Shaked, H.; Wallin, C.; Wärmländer, S.K.; Haas, E.; Gräslund, A.; Chill, J.H.; Rahimipour, S. Self-assembled cyclic D,L-a-peptides as generic conformational inhibitors of a-synuclein aggregation and toxicity. Chemistry 2016, 22(40), 14236-14246.
31. Zhao, R.; Dai, H.; Mendelman, N.; Cuello, L.; Chill, J.H.; Goldstein, S. Designer and natural peptide toxin blockers of the KcsA potassium channel identified by phage-display. Proc. Natl. Acad. Sci. 2015, 112(50), E7013-7021.
30. Meirovitch, E.: Tchaicheeyan, O.; Sher, I.; Norton, R.S.; Chill, J.H. Structural dynamics of the potassium channel blocker ShK: SRLS analysis of 15N relaxation. J. Phys. Chem. B 2015, 119, 15130-15137.
29. Reytblat, I.; Keinan-Adamsky, K.; Chill, J.H.; Gottlieb, H.; Gedanken, A.; Goobes, G. NMR studies of DNA microcapsules prepared using sonochemical methods. Phys. Chem. Chem. Phys. 2015, 17(3), 2235-2240.
28. Chill, J.H.; NMR of proteins: Eavesdropping on molecular events. Isr. Chem. Eng. 2015, 1, 13-21
27. Elazari-Shalom, H.; Shaked, H.; Esteban-Martin, S.; Salvatella, X.; Barda-Saad, M.; Chill, J.H.* New insights into the role of the disordered WIP N-terminal domain revealed by NMR structural characterization. FEBS J., 2015, 282(4), 700-714.
26. Sher, I.; Chang, S.-C.; Li, Y.; Chhabra, S.; Palmer III, A.G.;.Norton, R.S. and Chill, J.H.* Conformational flexibility in the binding surface of the potassium channel blocker ShK. ChemBioChem, 2014, 15(16):2402-2410. Featured on cover. (*Corresponding author)
25. Elazari-Shalom, H.; Zazrin-Grynspan, H.; Shaked, H.; Chill, J.H.* An NMR study of the transmembrane domain of hepatitis C virus E2 glycoprotein. BBA Biomembranes, 2014, 1838(11):2919-2128. (*Corresponding author)
24. Kamnesky, G.; Hirschhorn, O.; Shaked, H.; Chen, J.; Yao, L.; Chill, J.H.* Molecular determinants of tetramerization in the KcsA cytoplasmic domain. Protein Science, 2014, 23(10):1403-1416. (*Corresponding author)
23. Fried, S.; Eliyaho, S.; Pauker, H.M.; Noy, E.; Reicher, B.; Chill, J.H. and Mira Barda-Saad. Triple color-FRET analysis reveals a dynamic conformational change within the actin regulating WIP:WASp complex. Science Signaling, 2014, 7(331):ra60. doi: 10.1126/scisignal.2005198.
22. Zazrin, H.; Shaked, H.; Chill, J.H.* Architecture of the hepatitis C virus E1 glycoprotein transmembrane domain studied by NMR. BBA-Biomembranes, BBA-Biomembranes, 2014, 1838, 784-792. (*Corresponding author)
21. Haba, N.Y.; Gross, R.; Novacek, J.; Shaked, H.; Zidek, L,; Barda-Saad, M.; Chill, J.H.* NMR determines transient structure and dynamics in the disordered C-terminal domain of WASp interacting protein. Biophyiscal J. 2013, 105(2), 481-493. (*Corresponding author)
20. Guttman, C.; Davidov, G.; Yahalom, A.; Shaked, H.; Kolusheva, S.; Bitton, R.; Chill, J.H.*; Zarivach, R.* BtcA, a class IA type III chaperone, interacts with the BteA N-terminal domain through a globular/non-globular mechanism. PLoS One, 2013, 8(12), e81557. (*Corresponding authors)
19. Shapira, R.; Rudnick, S.; Daniel, B.; Viskind, O.; Aisha, V.; Richman, M.; Ayasolla, K.R.; Perelman, A.; Chill, J.H.; Gruzman, A.; Rahimipour, S. Multifunctional cyclic D,L-α-peptide architectures stimulate non-insulin dependent glucose uptake in skeletal muscle cells and protect them against oxidative stress. J. Med. Chem. 2013, 56(17), 6709-6718.
18. Guttman, C.; Davidov, G.; Shaked, H.; Ganguly, A.; Miller, J.F.; Chill, J.H.*.; Zarivach, R.* Characterization of the N-terminal domain of BteA: a Bordatella Type III secreted cytotoxic effector. PLoS One, 2013, 8(1):e55650. (*Corresponding authors).
17. 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.
16. 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.
15. 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. (*Corresponding author)
14. 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. (*Corresponding author)
13. 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.
12. 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.
11. 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 α2 by cross saturation and an NMR-based model of the complex. Protein Sci., 2006, 15(11), 2656-2668.
10. 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.
9. 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.
8. Samson, A.O.; Chill, J.H.; Anglister J. 2D-measurement of proton T1ρ relaxation in unlabeled proteins: Mobility changes in α-bungarotoxin upon binding of an acetylcholine receptor peptide. Biochemistry, 2005, 44(32), 10926-10934.
7. 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.
6. 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).
5. 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.
4. Samson, A.O.; Scherf, T.; Eisenstein, M.; Chill, J.H.; Anglister J. The mechanism for acetylcholine receptor inhibition by α-neurotoxins and species-specific resistance to a-bungarotoxin revealed by NMR. Neuron, 2002, 35(2), 319-332.
3. 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.
2. 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.
1. Samson, A.O.; Chill, J.H.; Rodriguez, 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.
Courses
84-237 Spectroscopy and Structure Determination 1st year undergrad Thu 10-12
84-997 Magnetic Resonance Graduate Tue 12-14
84-887 Biomaterials and Biopolymers 3rd yr /Graduate Sun 08-10
84-107 Intro to Probability and Statistics 1st year undergrad Wed 14-16
Research Group
Group Members
Research Assistant
Dr. Hadassa Shaked
Post-doctoral fellow
Daniel Yeggoni
Inbal Sher
PhD candidates
Adi Yahalom
Chana Sokolik
Arwa Qasim
Nasrin Qasem
MSc candidates
Saja Baluom
Alumni
Hila Elazari-Shalom (PhD, 2007-2013)
Renana Shapira-Gross (PhD, 2009-2014) [High-school chemistry teacher]
Noam Haba (MSc, 2009-2011)
Guy Kamnesky (MSc/PhD, 2008-2014) [Brik laboratory, Technion, Haifa, Israel]
Orel Hirschhorn (MSc, 2012-2015)
Hadas Zazrin-Grynspon (MSc, PhD, 2009-2015) [Israel Police Forensics Unit]
Eva Rozentur-Shkop (PhD, 2012-2016)
Adi Halle-Bikovski (Msc, PhD, 2011-2017)
Matan Nissim (MSc, 2015-2017)
Netanel Mendelman (PhD, 2013-2018) [Post-doctoral fellow, Prof. Meirovich, BIU]
Veronica Lepushkin-Zilbermintz (MSc, 2016-2018) [PhD, Prof. Gruzman, BIU]
Last Updated Date : 06/03/2023
