Michal Sharon

Abstract

Angewandte ChemieVolume 133, Issue 36 p. 19673-19673 Introducing …Free Access Michal Sharon First published: 01 August 2021 https://doi.org/10.1002/ange.202108629AboutSectionsPDF ToolsRequest permissionAdd to favorites ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinked InRedditWechat Abstract “The biggest challenge facing scientists is navigating in the unknown … My favorite molecule is the proteasome complex …” Find out more about Michal Sharon in her Introducing … Profile. Michal Sharon The author presented on this page has published her first article as a submitting corresponding author in Angewandte Chemie: “Intracellular protein–drug interactions probed by direct mass spectrometry of cell lysates”: R. Rogawski, A. Rogel, I. Bloch, M. Gal, A. Horovitz, N. London, M. Sharon, Angew. Chem. Int. Ed. 2021, 60, doi.org/10.1002/anie.202104947; Angew. Chem. 2021, 133, doi.org/10.1002/ange.202104947. Position: Associate Professor, Department of Biomolecular Sciences, Weizmann Institute of Science Homepage: https://www.weizmann.ac.il/Biomolecular Sciences/MichalSharon/ ORCID: orcid.org/0000-0003-3933-0595 Education: 1996 B.Sc. in Chemistry, The Hebrew University, Jerusalem (Israel) 1996–2003 M.Sc./Ph.D. combined program (direct PhD) with Prof. Jacob Anglister, Department of Structural Biology, Weizmann Institute of Science, Rehovot (Israel) 2003–2006 Postdoc with Prof. Carol V. Robinson, Department of Chemistry, University of Cambridge, Cambridge (UK) Research: Structural mass spectrometry of proteins Hobbies: Hiking, reading, painting The biggest challenge facing scientists is navigating in the unknown. The most exciting thing about my research is that it never fails to surprise me going to unexpected directions. A turning point in my career was the decision to combine my chemical skills with biological questions. My long-term goal is continue and inspire young female scientists. I advise my students to believe in themselves. The most challenging part of my job is facing unfairness. I'm always in a good mood when I am inspired. To improve my work-life balance, I have wonderful friends. What I appreciate most about my friends is their endless support. The best advice I have ever been given is to be true to yourself. My biggest inspiration is my postdoc advisor Dame Professor Carol Robinson. The most important quality of a mentor is the ability to tailor support in a way that matches the student needs. My favorite thing about my lab group is that they are my second family. My favorite molecule is the proteasome complex. My favorite place on earth is the Israeli desert. Behind the Science References 1Recently, we developed a mass spectrometry (MS) methodology for in-depth, yet rapid, characterization of overproduced proteins without the need for protein purification. Although initially considered debatable, as prior purification of the protein complex of interest was considered a prerequisite for acquiring mass spectra. We have shown that it is possible to rely on the high expression levels of recombinant proteins and circumvented this tedious and laborious need. We wanted to adapt this direct-MS method to proteins generated intracellularly in human cells but this was extremely challenging. After multiple failures, we decided to adapt a system used during in-cell NMR studies, which turned out to solve the technical problems and pave the way for this study. Google Scholar Volume133, Issue36September 1, 2021Pages 19673-19673 This is the German version of Angewandte Chemie. Note for articles published since 1962: Do not cite this version alone. Take me to the International Edition version with citable page numbers, DOI, and citation export. We apologize for the inconvenience. ReferencesRelatedInformation