Speaker : Prof. Turkan Haliloglu
Affiliation : Polymer Research Center & Chemical Engineering Department, Bogazici University, Turkey.

Date: SEPTEMBER 21, 2016

Location : Science building 604

Time: 5 pm

abstract  :

Biomolecules are complex molecular machines that visit many conformational and dynamic states to perform their functions. As much as the stable conformational states, the transition pathways in between are of interest to comprehend the molecular functional mechanism. Intrinsic dynamic modes driven Langevin Dynamics simulations are able to disclose plausible conformational pathways between two given states and underlying dynamical network of mechanistically key sites from globular to nonglobular proteins. As exemplary cases, conformational transitions of adenylate kinase, a membrane protein vitamin B12 transporter BtuCD, and pore forming bacterial protein cytolysis A (ClyA) are presented to show how intrinsic dynamics modulate the conformational transition and alternative pathways may appear with the hindrance of some specific modes of motion with the change in the transition cooperativity and allosteric interactions between functional sites. Understanding the transition process and the conformational control may contribute to the design of new strategies for protein design and engineering.