Two-Molecule Force Spectroscopy of Proteins

Hongbin Li

Department of Chemistry

University of British Columbia

Vancouver, BC V6T 1Z1, Canada

Abstract

Many elastomeric proteins, which play important roles in a wide range of biological processes, exist as parallel/antiparallelly arranged dimers or multimers to perform their mechanobiological functions. For example, in striated muscle sarcomeres, the giant muscle protein titin exists as hexameric bundles to mediate the passive elasticity of muscles. Recently we have developed atomic force microscopy (AFM)-based two-molecule force spectroscopy (TMFS) to directly probe the mechanical properties of two elastomeric proteins that are arranged in parallel. In this presentation, I will describe our recent progress in using TMFS to investigate the effect of oxidative stress on the folding/unfolding of titin Ig domains and myofibrils mechanics, as well as the scaling relationship of the unfolding force and the number of molecules in the parallel multimers.  

Short Bio

Dr. Hongbin Li is currently a Professor at the Department of Chemistry, the University of British Columbia, Canada, and Director of the NSERC CREATE Program on 3D Printing Technology and Materials (3DPTM). He held the position of Canada Research Chair in Molecular Nanoscience and Protein Engineering from 2004-2014. Prior to joining UBC, he worked as an Associate Research Scientist in Columbia University (2002-2004) and a postdoctoral research fellow in Mayo Medical Center (1999-2002). He obtained his Ph.D. in Jilin University in 1998 and B.S. at Tianjin University in 1993. His research interest is in the area of single molecule biophysics, single molecule force spectroscopy and protein-based biomaterials. He is an elected Fellow of American Associate for the Advancement of Science (AAAS Fellow). His contributions have been recognized by Charles McDowell Award in Research, NSERC Accelerator Award, Career Investigator Award from Michael Smith Foundation, JILA Distinguished Fellowship.