User:Shyarkin/sandbox/Isaiah Arkin

Isaiah (Shy) Arkin (born in 1965) is the Arthur Lejwa Professor of Biochemistry, Charmain of the Authority for research and development and vice president of the Hebrew University

Biography
Isaiah Arkin was born in Tel Aviv, a descendent of the Arkin family that were amongst the founders of Mazkeret Batya.

After military service, he started his academic studies at the faculty of agriculture of the Hebrew University where he studied animal life sciences for two years. The third year of his undergraduate program was completed in Tel Aviv University in biology. In 1989, he started his PhD studies at Yale University in the area of molecular biophysics under the supervision of professors Donald M Engelman and Steven O Smith. Subsequently he undertook post-doctoral training in the group of professor Axel t Brunger.

Arkin secured his fort academic position in 1997, where he joined the faculty of Cambridge University in the department of biochemistry. In 2000, he returned to Israel as an associate professor in the department of biological chemistry in the Silberman Life sciences institute of the Hebrew University. In 2005, after being promoted to full professor, he left for a two-year sabbatical in the D.E. Shaw Research group where he specialized in molecular dynamics simulations. In 2008, he was appointed as chairmen of the Silberman Life Sciences Institute, and in 2009 elected as vice president in charge of research and development of the Hebrew University. In his capacity as VP for R&D, he is the chairmen of the authority for research and development and a director of Yissum (the Hebrew University technology transfer company) and Integra holdings.

Scientific work
The scientific work of Isaiah Arkin revolves around understanding of structure function relationship in membrane proteins with an emphasis on methods development. Amongst his major contributions, one can list the development of isotopic labels for the use of infra-red spectroscopy and in particular the 13C=18O probe that is widely used in the community. Use of such labels enabled him and others, to develop tools that may be used to obtain structural model of transmembrane peptides in their native environment [1-2]. Similarly, isotopic labels have enabled him to obtain detail measurements of the strength of Hydrogen bonds in such systems [3-4]. Other discoveries include the elucidation of the mechanism of the sodium proton antiporter of bacteria based on molecular dynamics simulations [5] and establishing a method to model proteins based on silent amino acids mutagenesis [6].

Towards the end of the second decade of the 21st century, most of Arkin’s work concerns with understanding the mode of activity of antiviral drugs [7] and how viruses such as influenza and HIV develop resistance against them [8].

Reference

 * 1) ^ Arkin IT, Isotope-edited IR spectroscopy for the study of membrane proteins, Curr Opin Chem Biol, 10(5), עמ' 394-401, 2006
 * 2) ^ Manor J, Arbely E, Beerlink A, Akkawi M, Arkin IT, Use of Isotope-Edited FTIR to Derive a Backbone Structure of a Transmembrane Protein, J Phys Chem Lett, 5(15), page 2573-9, 2014
 * 3) ^ Arbely E, Arkin IT, Experimental measurement of the strength of a C alpha-H...O bond in a lipid bilayer, J Am Chem Soc, 126(17), page 5362-3, 2004
 * 4) ^ Feldblum ES, Arkin IT, Strength of a bifurcated H bond, Proc Natl Acad Sci U S, 111(11), page 4085-90, 2014
 * 5) ^ Arkin IT, Xu H, Jensen MØ, Arbely E, Bennett ER, Bowers KJ, Chow E, Dror RO, Eastwood MP, Flitman-Tene R, Gregersen BA, Klepeis JL, Kolossváry I, Shan Y, Shaw DE, Mechanism of Na+/H+ antiporting, Science, 317(5839), page 799-803, 2007
 * 6) ^ Briggs JA, Torres J, Arkin IT, A new method to model membrane protein structure based on silent amino acid substitutions, Proteins, 44(3), page 370-5, 2001
 * 7) ^ Leonov H, Astrahan P, Krugliak M, Arkin IT., How do aminoadamantanes block the influenza M2 channel, and how does resistance develop?, J Am Chem Soc, 133(25), page 9903-11, 2011
 * 8) ^ Assa D, Alhadeff R, Krugliak M, Arkin IT, Mapping the Resistance Potential of Influenza's H(+) Channel against an Antiviral Blocker, J Mol Biol, 428(20), page 4209-4217, 2016