Seminar:

Profile: Dr. Lin Li attended the Huazhong University of Science and Technology from 2005-2011 he received his Ph.D.  in Biophysics.  Dr. Li did his Post-Doctoral research in Biophysics at Clemson University, Clemson, SC from 2011 until 2013.  He was a Research Associate in Biophysics at Clemson University from 2013 until 2016.  In 2016, Dr. Li became a Research Assistant Professor until 2017.  Presently, Dr. Lin Li is an Assistant Professor in the Department of Physics at the University of Texas at El Paso, El Paso, TX.  Dr. Li’s research involves: DelPhi Development for Poisson Boltzmann Equation solutions, Membrane Potential (MEMPOT) tool is development and implementation into DelPhi programing, utilization of the docking algorithm (ASPDock) to calculate binding free energy of protein complexes, development of a Softly Restricting Method (SRM) which utilizes the unreliable binding site information to enhance success rate of docking, and ,using ASPDock and Softly Restricting Method, participation in two rounds of Critical Assessment of PRediction of Interactions (CAPRI) which yielded high-quality hits for T40 and T41 and LRMSD at 2.35 Å and 1.41 Å, respectively.  Dr. Li is the Principle Investigator for the Lin Li Lab. 

Abstract: Protein-protein interactions play crucial roles in many biology phenomena. Therefore, a lot of efforts have been made to model the protein-protein interactions in biological systems. However, it is extremely challenging to accurately calculate the electrostatic interactions in large biological systems such as dynein and viral capsid. Dynein, a molecular motor, is important for cargo transportation and force generation in cells. Dysfunction of dynein is associated with many diseases, such as ciliopathies, lissencephaly and other neurodegeneration disorders. I will introduce a novel multi-scale simulation approach which was used to study dynein’s motion along microtubules. The results demonstrate that the electrostatic interactions play significant roles in dynein’s motilities and functions along microtubule. Understanding the fundamental mechanisms in molecular motors sheds light on curing many molecular motor related diseases. Besides molecular motors, viral capsid assembly was also studied by this multi-scale approach. Assembled by capsomers periodically, the viral capsid holds, protects and ejects the genes of the virus. Paramecium bursaria Chlorella virus (PBCV) was studied to study the capsid assembly mechanisms. Three different capsomer-capsomer binding modes were found in PBCV viral capsid, which reveals interesting and fundamental mechanisms for viral capsids assembly.