Research in the Chill group is dedicated to unraveling the secrets of structure, dynamics and function of proteins, including their interactions with ligands and other proteins, in health and disease. Motivation for structural bioNMR studies of proteins and their interactions is convincing: all biological processes are based upon cellular events of protein-protein encounters, and a structural view of these is vital for achieving a deeper understanding of and developing approaches for controlling them. The main tool employed is high-resolution biomolecular nuclear magnetic resonance (bioNMR), a powerful approach distinguishing itself from other biophysical methods by offering an exquisitely molecular-level view of protein behavior.

Prof. Chill completed his PhD studies under the supervision of Prof. Jacob Anglister (Weizmann Institute of Science, Israel), determining the structure of the human interferon receptor, followed by a post-doctoral fellowship with Dr. Adriaan Bax (NIH, USA), applying bioNMR to characterization of a membrane-embedded K+-channel.

As an independent investigator at Bar Ilan University (since 2007) Prof. Chill pursues bioNMR studies of proteins and combines them with biophysical and computational methods in a wide range of projects. Four main efforts are:

1) The interactions between K+-channels and their inhibiting toxins,

2) Intrinsically disordered proteins (IDPs) and their folding upon encountering binding partners, 3) The structural biology of Wiskott-Alrdrich syndrome, specifically the mechanism of interaction between WASp and WIP, and

4) Amyloid-related aggregation and pathologies.


These represent experimentally challenging aims at the forefront of structural biology today and impact the fields of protein-protein interactions and drug design. The group also collaborates with biologists and chemists in academia and industry, resulting in significant contributions of structural evidence for biological studies and drug-design projects. Overall these efforts have led to ~55 publications and patents (>1200 citations, h-index 19).

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