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Protein NMR Research laboratory

Nuclear Magnetic Resonance (NMR) spectroscopy; proteins structure and function; Intrinsically Unfolded Proteins (IUPs); drug discovery; Biophysics

Dr. Maayan Gal

972-4-7700514
Contact Dr. Maayan Gal

Today it is known that the genome of different organism does not reflect its complexity. It is the protein-protein interactions (PPIs) network which determines its complexity and responsible for all cell processes. As part of all signal transduction proteins interact with one another and with other biomolecules in the cell. In our lab we study the molecular-level mechanistic basis of these interactions focusing on the structure-function relation and unstructured proteins. In addition, we use the structural data to develop new PPIs inhibitors as the basis for potential drugs.
Our research is multidisciplinary by nature dealing with molecular biology, bio-chemistry and the use of state-of-the-art physical tools to answer these interesting questions. In addition, we are collaborating with the group of Itai Bloch which is dealing with computational chemistry and modeling to shed light on these matters.
One of our research tools in Nuclear Magnetic Resonance (NMR) spectroscopy. NMR is a spectroscopic tool which enables the elucidation of atomic-resolution data on the target molecule (small molecules, proteins, DNA etc').


 

CV

Education
Ph.D., 2009, Direct track, Dept. of Chemical Physics, Weizmann Institute of Science, Rehovot,
Israel.

Academic and research experience
2012 Principal Investigator, Migal research center, Kyriat Shmona, Israel.
2009-2012 Human Frontiers fellow, Post-doctoral studies, Dept. of Biological Chemistry and
Molecular Pharmacology, Harvard Medical School, Boston, MA, USA.

Honors and awards
2009 Human Frontiers Science Program – Long-term fellowship
2007 Magnetic Resonance in Chemistry Award for young Scientist.
2002 Student excellence award – Physics department, Bar Ilan University.

Selected Publications

Speeding up direct 15N detection: HCaN 2D NMR experiment

Journal of Biomolecular NMR 2011 Volume 51 Issue 4 Pages 497-504 M. Gal; K. A. Edmonds; A. G. Milbradt; K. Takeuchi; G. Wagner Read online

Single-scan 2D NMR correlations by multiple coherence transfers

Journal of Magnetic Resonance 2010 Volume 203 Issue 2 Pages 311-315 M. Gal; L. Frydman Read online

Native-unlike long-lived intermediates along the folding pathway of the amyloidogenic protein β2-microglobulin revealed by real-time two-dimensional NMR

Journal of Biological Chemistry 2010 Volume 285 Issue 8 Pages 5827-5835 A. Corazza; E. Rennella; P. Schanda; M. C. Mimmi; T. Cutuil; S. Raimondi; S. Giorgetti; F. Fogolari; P. Viglino; L. Frydman; M. Gal; V. Bellotti; B. Brutscher; G. Esposito Read online

Real-time multidimensional NMR follows RNA folding with second resolution

Proceedings of the National Academy of Sciences of the United States of America 2010 Volume 107 Issue 20 Pages 9192-9197 M. K. Lee; M. Gal; L. Frydman; G. Varani Read online

Solid-state single-scan 2D NMR under magic-angle-spinning

Chemical Physics Letters 2008 Volume 459 Issue 05-ינו Pages 188-193 M. Gal; C. Melian; D. E. Demco; B. Blümich; L. Frydman Read online

Real-time monitoring of chemical transformations by ultrafast 2D NMR spectroscopy

Journal of the American Chemical Society 2006 Volume 128 Issue 3 Pages 951-956 M. Gal; M. Mishkovsky; L. Frydman Read online

Students

Post-graduate and post-doctoral research training

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Laboratories and research projects

Business

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