Z. Nevin Gerek
Postdoctoral Research Associate
PhD, University of Akron, Chemical Engineering, 2006
Home Department Physics
ASU Affiliations Physics
Areas of Study Computational Biophysics; Chemical Process Engineering and Thermodynamics


Background Protein-protein interactions are key elements in building functional protein complexes. Among the many protein-protein interaction domains, PDZ domains (PDZs) are one of the most commonly found in organisms from bacteria to humans. PDZs distributed diversely in the genome play critical roles in: (i) targeting proteins to specific membrane compartments, (ii) assembling proteins into supramolecular complexes, and (iii) regulating the function of their ligands. This ties them directly to our most puzzling diseases such as Alzheimer’s, Parkinson’s, cancer and diabetics. They are approximately 90 residues long and were first identified as regions of sequence homology in diverse signaling proteins. The name PDZ is named after the combination of Post-synaptic density PSD-95, Discs large Dlg and Zona occludens-1 ZO-1. PDZs perform their job by binding the C-terminal peptide of specific protein partners. However, they are very promiscuous, binding to more than one protein, yet selective at the same time. Investigating the relationship between promiscuity, selectivity and allostery in PDZ domain binding interactions will help us to understand the central role of PDZ domain proteins in assembling and regulating protein networks. My current research is focused on understanding the principles of biomolecular interactions specifically domain binding interactions at different length scales using a broad range of methods, including elastic network models, molecular dynamics, and all-atom physics-based computer simulations.
Z. Nevin Gerek
Arizona State University
Department of Physics
PO Box 871504
Tempe, AZ 85287

phone: (480) 727-8897
email: Nevin.Gerek
@asu.edu
[Publication] Gerek ZN, Keskin O, Ozkan SB, "Identification of Specificity and Promiscuity of PDZ Domain Interactions through their Dynamic Behavior", Proteins (in press 2009)