Ching-Hwa Kiang Assistant Professor of Physics & Astronomy Department of Physics & Astronomy 6100 Main Street - MS 61 Rice University Houston, TX 77005-1892 Office: Herzstein Room 107 (713) 348-4130 (713) 348-4150 chkiang@rice.edu group webpage: www.chkiang.rice.edu

Education
B.S., National Taiwan University
Ph.D., California Institute of Technology
Postdoctoral Associate, Massachusetts Institute of Technology

Awards and Honors
The Best of Small Tech Researcher of the Year award (2007) (Link to press release) (Link to Small Times Magazine)
Cram Teacher-Scholar, University of California, Los Angeles (1996-1999)
Student Thesis Fellowship, IBM Corporation (1992-1995)

Press Releases
(APS March 2007 newsletter Mapping Protein Folding)
(Science News Pulling Strings: Stretching proteins can reveal how they fold)
(Rice News & Media Relations press release Protein pulling: Learning how proteins fold by pulling them apart)
(PhysicsWorld Microscope unravels the intricacies of protein folding)
The Best of Small Tech Researcher of the Year award (2007 Best of Small Tech Award Researcher of the Year)
Rice News & Media Relations press release (Kiang named 'Researcher of the Year' by Small Times: Physicist recognized for new method of mapping protein folding

Publications
Recent Invited Talks
Recent Presentations
Book Chapters
Patents
Interview on "Molecular Nanotechnology" for BBC Radio 4 (London) program "News: Leading Edge."
CV

Single-Molecule Manipulation Experiments

Research Interests

Our research focuses on understanding the interactions of biological molecules and complexes. We use atomic force microscopy to study the forces between and within single biological molecules. The development of single-molecule techniques to studying molecular properties at the molecular level has expanded our understanding on the details of how biology and medicine function at the microscopic level. We are studying protein-nucleic interactions, virus assemblies, and protein-cell interactions. as well as developing new nanomanipulation techniques to study the properties of single-molecules.

Projects

Virus Packaging Influenza A virus consists of four general structures - an integral glycoprotein on the surface that guarantees entry into the host cell, a RNA-dependent RNA polymerase that later transcribes and replicates the RNA in the nucleus, eight segments of negative-sense viral RNA, and a complementary number of nucleoproteins (NP), also known as single-stranded RNA (ssRNA) binding proteins. Out of all of the components of influenza A, the nucleoproteins (NP) are a prominent factor in the life cycle of the virus. NP organizes a variety of functions that assist in the effectiveness of influenza A and is pivotal in its interactions with neighboring macromolecules from the virus and host cell. We are studying the interactions of RNP assemblies to understand the RNA transcription, replication, and packaging. The difference in free energies between ssRNA, NP, and RNP will allow use to understand the binding interactions between NP and RNA.

Protein Mechanical Activation Von Willebrand factor (VWF) is a large glycoprotein that is responsible for blood clotting and thrombosis. To maintain hemostasis, VWF mediates platelet adhesion to the subendothelial connective tissue that lines the interior of all blood vessels and binds to the clotting factor VIII. As a glycoprotein, it can reach up to 100 micrometers in length and can exhibit tremendous flexibility in its structure. VWF function is activated by an allosteric mechanism or by high-shear induced force. Beyond the allosteric model, VWF are generally regulated by hydrodynamic forces within the blood vessels. In blood vessels, the shear rate of fluid is at its maximum near the subendothelial wall. Shear-induced adhesion enables VWF to bind to the endothelial under pathophysiological conditions and to initiate the blood clotting process at the site of vessel damage. We are studying VWF and ultra-large VWF resistance to mechanical forces and the effect of shear induced property changes. We will also study the VWF properties in the presence of ADAMTS-13 to test its reductase activity.

DNA Melting and Phase Transition The DNA-gold nanoparticle system is a model for phase transitions. Melting of short, free DNA is not a phase transition. However, when short DNA are bound to gold particles, the system undergoes a phase transition because the DNA-gold particles form networks of micrometer size, which is approaching a bulk phase. Thus, the binding transition in the network is much sharper than that of free DNA in solution, due to the cooperative melting process. Many fundamental aspects of phase transitions may be investigated with this biomolecular system.

Graduate research assistantship positions available