Biomolecular NMR Group
Molecular insights into
protein structure and function
Welcome to our
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.
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
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.
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
Aims to complete the structure determination of the complex between the
Wiskott-Aldrich syndrome protein (WASp) N-terminal EVH1 domain and WASP-
Interacting protein (WIP).
Studies the effect of anti-
amyloidogenic peptides against amyloidosis.
Studied how the KcsA cytoplasmic C-terminal domain (CTD), a
homotetrameric 40-residue long helical bundle, modulates the opening of the
channel in response to pH changes.
Studies the intrinsically disordered
protein (IDP) WIP.
Studies the conformational ensemble study of the intrinsically disordered
WASp Interacting Protein by Nuclear Magnetic Resonance and