Bahar Lab title bar Bahar Lab title bar

Dr. Ivet Bahar
Distinguished Professor & JK Vries Chair
Computational & Systems Biology Dept
School of Medicine, University of Pittsburgh
3064 Biomedical Science Tower 3
3501 Fifth Avenue, Pittsburgh, PA 15213

Voice: 412 648 3332
Fax: 412 648 3163

Pitt, CMU, PSC, and Salk Institute win grant for establishing a National Center, MMBioS,
for Multiscale Modeling of Biological Systems. December 3, 2012 Pittsburgh Post-Gazette.

See the Biophys Society 2014 video, and the International Innovation article.

Research Interests

Biomolecular systems dynamics at multiple scales; evolution of proteins' sequence, structure, dynamics and function; computer-aided drug discovery and polypharmacology; network models for protein-protein interactions, supramolecular machinery and allostery; modeling and simulations of membrane proteins dynamics and mechanisms of interactions.

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Two outstanding Tsinghua University Research Scholars, Feizhuo Kaitlyn Hu and Wenzhi Mao have returned to their home institutions after successfully completing extensive research, resulting in several publications in the Bahar Lab. We wish them continued success on their scientific journeys!

kaitlyn and mao

Anindita Dutta's recent award for the "Outstanding Student Researcher in the Department of Computational & Systems Biology of 2012".

Anindita Dutta Award


Publications 2014

Most recent study of Dr Gur (the Bahar lab) published in Biophys J is highlighted in Ricardo Baron's News & Notable, "Fast sampling of A-to-B Protein Global Conformational Transitions: From Galileo Galilei to Monte Carlo Anisotropic Network Modeling The new methodology, coMD, introduced by Gur et al is stated to "surely prompt new exciting routes to rapidly connect A to B, and vice versa."

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"Allosteric Transitions of Supramolecular Systems Explored by Network Models: Application to Chaperonin GroEL." Yang, Z., Majek, P., & Bahar, I. (2009). PLoS Comput Biol. 5: e100360. PMID: 19381265.

Comput Biol 5(4) cover


"Coupled Global and Local Changes Direct Substrate Translocation by Neurotransmitter-Sodium Symporter Ortholog LeuT" Cheng MH, Bahar IBiophys J. (2013). 105:630-639. PMID: 23931311

This is a first attempt to complete the molecular description of all steps involved in LeuT transport cycle. Notably, the secondary substrate-binding site S2, the functional relevance of which has been debated, appears to stably bind an alanine only when the transporter assumes an intermediate conformer close to inward-facing state.

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Coupling between the translocation of alanines bound to S1 and S2