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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
email:
 

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

Anindita Dutta Award



Congratulations to Lidio Meireles, Ying Liu, and Lin Liu on their successful defenses!

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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

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