Biography

lee-jinwoo

CONTACT INFORMATION

 Office Phone: 301-405-5091
 Office Address: 2111 Biomolecular Sciences Bldg.
 Email: jinwoo@umd.edu
 URL: Group Website

Assistant Professor

Education

B.S., Chemistry, 2006, Hanyang University, Seoul, Korea
M.S., Chemistry, 2008, Lehigh University, Bethlehem, PA
Ph.D., Chemistry, 2013, Lehigh University, Bethlehem, PA
Postdoctoral Research Associate, 2013-2018, University of Virginia, Charlottesville, VA

Professional Experience

Assistant Professor, Department of Chemistry and Biochemistry, University of Maryland, College Park, 2018-present

Research Interests

Biochemistry and Biophysics of Membrane Proteins, Membrane Protein NMR, Protein-Protein Interaction, Protein-Lipid Interaction, Viral Membrane Fusion, Magnetic Particle, Kidney Disease.

Professional Societies

American Chemical Society; Sigma Xi; Biophysical Society

Major Recognitions and Honors

Student Chemistry Foundation Fellowship, Lehigh University, 2011

Research

Overview

My research interests are how the structure of membrane proteins contributes to disease pathogenesis and how structural information can give mechanistic insights into disease progression and intervention. Biochemical/biophysical analysis of membrane proteins will contribute to the identification of structure-to-function relationships of disease-related membrane proteins.

Lassa Virus Membrane Fusion:

In recent years, the numbers of threatening epidemics caused by emerging viruses like MERS, Ebola and Avian Influenza are rapidly increasing. Lassa virus (LASV) shares similar symptoms (hemorrhagic fever) and features (both are single-stranded RNA viruses) with Ebola virus (EBOV) although they belong to two separate virus families. As a result, both viruses are recognized to pose a serious threat to public health and biodefense. Therefore, new interventions for the prevention and treatment of infectious diseases like EBOV and LASV are urgently needed. Investigating the structure and function of LASV GPC will not only further our understanding of the LASV membrane fusion mechanism, but will also illuminate a new target for drug design by determining if there is an interface, which could be disrupted before association with the target membrane bilayer.

Unusual Hairpin Structure of Podocin’s Intramembrane Domain:

The major function of the kidney is filtering blood to remove waste in our body while retaining useful macromolecules. This filtration occurs in the Bowman capsule of the glomerulus where extensions of podocytes called foot processes, cover the capillaries of the glomerulus. The spaces between the podocyte foot processes comprise slit diaphragms (SD) that form the matrix for filtration. The SD is composed of the nephrin/podocin/CD2AP protein complex and podocin is a crucial member of this complex. However, it is not clear how the unusual hairpin domain of podocin contributes to its critical functions. To elucidate the detailed functions of the unusual hairpin intramembrane domain of podocin, biochemical/biophysical and structural studies of podocin in the lipid bilayer will be investigated.

Magnetosome Associated Membrane Protein:

Magnetotactic bacteria are Gram-negative bacteria with the ability to use geomagnetic fields for navigating. This ability is governed by magnetosomes, which are magnetite (Fe3O4)-containing vesicles. To understand the biomineralization mechanism, I will examine the structure and function of proteins that control the size and shape of magnetic particles in presence of a lipid bilayer. Many magnetic particle applications are possible; processes such as catalysis, magnetic storage, targeted drug delivery, cancer therapy, and magnetic resonance imaging (MRI) can benefit tremendously from more precisely controlled magnetic particle.

 

 

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