Ivet Bahar, PhD

Distinguished Professor & JK Vries Chair Computational & Systems Biology Dept School of Medicine, University of Pittsburgh

Ivet Bahar, PhD

bahar@pitt.edu

Office: BST3 3064
Phone: 412 648 3332
Fax: 412 648 3163

Computational & Systems Biology

Biosketch

Bogazici University, Istanbul BS 6/1980
Chemical Engineering Bogazici University, Istanbul MS 6/1983
Chemical Engineering Istanbul Technical University, Istanbul PhD 2/1986 Chemistry

As the Founding Chair of the Department of Computational and Systems Biology at the University of Pittsburgh, School of Medicine, and an Associate Director of the University of Pittsburgh Drug Discovery Institute, I am dedicated to initiating and establishing collaborative and interdisciplinary research and training activities in the areas of computational and systems biology. Our lab is currently developing models and methods for exploring the structure and dynamics of complex biological systems at multiple scales, from full atomic interactions to supramolecular machinery. We have made online accessible to the biomedical community a large number of broadly used software, servers, and databases. Our overarching goal is to bridge between molecular structure and biological function, and to fill the gap between current molecular simulations and systems-level mathematical models. To this aim, we have introduced coarse-grained models and methods with structural and/or spatiotemporal details at various levels of resolution which can efficiently and accurately explore mesoscopic scales.

  1. Yang LW, Eyal E. Global dynamics of proteins: bridging between structure and function. Annu Rev Biophys. 2010;39:23-42. PubMed PMID: 20192781; PubMed Central PMCID: PMC2938190.
  2. Bakan A, Bahar I. The intrinsic dynamics of enzymes plays a dominant role in determining the structural changes induced upon inhibitor binding. Proc Natl Acad Sci U S A. 2009 Aug 25;106(34):14349-54. PubMed PMID: 19706521; PubMed Central PMCID: PMC2728110.
  3. Tobi D, Bahar I. Structural changes involved in protein binding correlate with intrinsic motions of proteins in the unbound state. Proc Natl Acad Sci U S A. 2005 Dec 27;102(52):18908-13. PubMed PMID: 16354836; PubMed Central PMCID: PMC1323175.
  4. Yang LW, Bahar I. Coupling between catalytic site and collective dynamics: a requirement for mechanochemical activity of enzymes. Structure. 2005 Jun;13(6):893-904. PubMed PMID: 15939021; PubMed Central PMCID: PMC1489920.
  5. Haliloglu T, Bahar I. Adaptability of protein structures to enable functional interactions and evolutionary implications. Curr Opin Struct Biol. 2015 Dec;35:17-23. PubMed PMID: 26254902; PubMed Central PMCID: PMC4688206.