Intrinsically disordered proteins (IDPs), which lack of a well-defined folded structure alone, play
important roles in a variety of intracellular activities. This is usually made possible via a disorder-to-order
transition when interacting with other biomolecules. However, there has been growing evidence towards the
indispensable roles of conformational flexibility and dynamics on regulating biological activities. Zheng's lab
focuses on investigating IDP interactions through developing multiscale computational modeling methods.
Dr. Zheng has a track record of developing all-atom, coarse-grained and polymer models for IDPs with
publications directly relevant to the research focuses. The lab has already contributed to modeling methods
for interpreting experimental data of IDPs through collaborating with multiple experimental groups. The
research program will be a good addition to the biophysics community within Arizona State University and
provide research opportunities to students on this timely topic. The long-term goal of the group is to gain a
comprehensive understanding of the driving force of disordered protein assemblies. Two interrelated
research topics are proposed including (1) deciphering the role of flexible regions when an IDP interacts with
its folded partner; and (2) investigating the mechanism of IDP-driven liquid-liquid phase separation (LLPS).
The project combines computational methods in multiple resolutions with a variety of experimental techniques
through three collaborations. Such unique combination of computational and experimental methods will
provide an unprecedented level of insights on the molecular mechanism of IDP interactions. The designing of
novel methodology framework for studying IDP assembly will benefit a broad range of audience interested in
IDP relevant biological process.