top of page
Screenshot 2021-07-29 174920.jpg

Biomolecular NMR Group

Molecular insights into
protein structure and function
using NMR

Welcome to our


BIU Solution
BioNMR group

In our group we investigate the structure and dynamics of proteins, and how these impact their function in the biological environment.

Our primary tool is solution nuclear magnetic resonance (NMR), a powerful method for understanding the behavior of proteins in close-to-native conditions.

Molecular biology, biochemistry, and various biophysical and computational methods are all part of our arsenal aimed at achieving these goals.

Visit us to see what we are up to.

Screenshot 2021-07-29 174920.jpg
Screenshot 2021-07-29 174920.jpg

Hadad, E.; Rudnick-Glick, S.; Grinberg, I.; Kolitz-Domb, M.; Chill, J.H.; Margel, S. Synthesis and characterization of poly-(RGD) proteinoid polymers and NIR fluorescent nanoparticles of optimal d,l-configuration for drug-delivery applications - in vitro study. ACS Omega 2020, 5(37), 23568-23577.

Sokolik, C.G.; Qassem, N.; Chill, J.H. The disordered cellular multi-tasker WIP and its protein-protein interactions: a structural view. Biomolecules 2020, 10(7), 1084-1093.

Zhao, R.; Dai, H.; Mendelman, N.; Chill, J.H.†; Goldstein, S.A.N†. Tethered peptide neurotoxins display two blocking mechanisms in the K+ channel pore as do their untethered analogues. Sci. Adv. 2020, 6(10), eaaz3439. (†Co-corresponding author)

Chill, J.H.*; Qasim, A.; Sher, I.; Gross, R. NMR perspectives of the KcsA potassium channel in the membrane environment. Isr J. Chem., 2019, 59(11-12), 1001-1013. (*Corresponding author)

Prof. Jordan Chill

Chana Sokolik



Structure-function studies of potassium channels and toxin inhibitors

Potassium channels (K+-channels) are homotetrameric membrane-embedded assemblies that control the influx/efflux of K+ ions in cells and play critical roles in all biological systems. While much is known about the structural basis for ion selection and gating in such channels, their interaction with various inhibiting toxins is rather enigmatic because of the lack of toxin-channel complex structures. In our lab we aim to unravel the secrets of how toxins bind to the channel opre in a specific manner and block ion conduction.

Screenshot 2021-07-29 174920.jpg

The Team

Our vibrant team of post-docs, PhD and MSc students all team up to gain insight into the molecular basis of protein structure and function. For more details on individual projects.


Prof. Jordan Chill

Group Head

 Associate Professor


Dr. Hadassa Shaked

Lab Manager and Research Assistant

bottom of page