Junji Iwahara, PhD
Professor, Department of Biochemistry & Molecular Biology
Tel: (409) 747-1403
Fax: (409) 772-6334
E-mail: j.iwahara@utmb.edu
Campus Location: 5.104C Medical Research Bldg
Mail
Route: 0857
Pubmed Publications | Lab Webpage
Research
Biomolecular Electrostatics: In life, complex networks of molecular interactions involve electrostatic forces that influence structure and function of biological macromolecules. Electrostatics is important for our fundamental understanding of biomolecular functions as well as for drug development. Biomolecular electrostatics has been a subject of computational investigations based on 3D structures. Our nuclear magnetic resonance (NMR) methods are changing this situation. These solution NMR methods allow us to quantitatively investigate biomolecular electrostatics without any use of structure information. You can find more information about this research here.
Protein-DNA Dynamics: Protein-DNA interactions are dynamic. DNA-binding proteins dynamically and stochastically change locations on DNA to find their targets. At a sub-molecular level, considerable portions of DNA-binding proteins are intrinsically disordered regions (IDRs), which are flexible yet exert strong influence on the protein function. At an atomic level, when proteins bind to DNA, some counterions are released, which entropically contributes to the thermodynamics of DNA recognition by proteins. These dynamic processes are crucial for the functions of DNA-binding proteins. Using NMR spectroscopy and other biophysical methods, we investigate dynamic aspects of molecular processes whereby DNA-binding proteins scan DNA and recognize their targets. For more information, visit this webpage.
HMGB1 Biochemistry: HMGB1 is a very interesting DNA-binding protein that plays important roles in the cell nuclei and in extracellular space. Normally, HMGB1 exists in the cell nuclei and serves as a DNA chaperone and assists various other DNA-binding proteins. HMGB1 is released to extracellular space not only passively from dying cells, but also actively from platelets and some healthy cells. Extracellular HMGB1 serves as a danger signal that alarms nearby cells and activates an innate immune response. HMGB1 is involved in many inflammatory diseases and has been regarded as a potential therapeutic target. Using NMR spectroscopy and other techniques, we are characterizing HMGB1 and trying to find effective ways for HMGB1 inhibition. Visit this for more information.
