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1. Research activities

By using magnetic tweezers, atomic force microscope and mass spectrometry, we studied the effects of pH on oxaliplatin-induced DNA condensation, the DNA persistence length, the amounts of micro-loops and of oxaliplatin bound to DNA.

We observed and quantitatively analyzed the formation of micro-rod structures of DNA induced by cisplatin.
Heptaplatin is a third-generation platinum antitumor drug. It has a chiral isomer. We studied the interactions between the two isomers and DNA by using magnetic tweezers and atomic force microscopy.

Under the torsion constraint condition, the interactions between DNA and oxaliplatin were investigated. It is found that torsion constraint in DNA enhances the ability of oxaliplatin for shortening DNA. The transplatin helps oxaliplatin combine to DNA and increase the rate of DNA condensation.

We studied theoretically the kinetics of mRNA translocation in the wild-type Escherichia coli ribosome.

We introduced a novel method to map rapidly the diffusion distribution in single cells based on single-particle tracking of quantum dots (QDs). The diffusion map reveals the heterogeneous intracellular environment and, more importantly, an unreported compartmentalization of QD diffusions in cytoplasm. Simultaneous observations of QD motion and GFP-tagged endoplasmic reticulum (ER) dynamics provide direct evidence that the compartmentalized diffusion is defined by ER.

DNA twist is the key to understanding the topological kinetics of DNA condensation. We traced both the DNA twist and DNA length by the freely orbiting magnetic tweezers and the tilted magnetic tweezers, providing a more complete description of multivalent cation-dependent DNA condensation.

Three stages of DNA cisplatin interaction is revealed by a solid-state nanopore.

Based on our observations and previous studies, we propose a dynamic model of how chromosomal DNA in E. coli is organized during a cell division cycle.

We studied the dynamic features of the polypeptide linkers of DNA polymerase I, T7 primase and DNA polymerase IV. We find that for any enzyme whose two domains are connected by an unstructured flexible linker, the stretched length of the linker in the finally active mode and the optimal number of the residues in the linker satisfy a common relation.

We studied the unwinding activity and structure of the BsPif1 helicase and find that a major movement of the 2BSH3 domain is required for DNA unwinding.

We employed magnetic tweezers to investigate the influence of cisplatin on the folding kinetics of single human telomeric G-quadruplex. It was revealed that cisplatin and G-quadruplex interact in two different and competitive ways that depend on cisplatin concentration.

In eukaryotes, the packaging of genomic DNA into chromatin plays a critical role in gene regulation. With single-molecule method, we studied the assembling and disassembling dynamics of the chromatin fiber. We find that the histone chaperone FACT (Facilitates Chromatin Transcription) and the linker histone H1 play important roles in the stability of the tetranucleosomal unit of the chromatin.

2. Group Publications

Number of SCI papers published over the past three years: 37 (Including one in JACS [impact factor 13.038], three in Nucleic Acids Research [impact factor 9.202] and one in Molecular Cell [impact factor 13.958].

3. Funds, staff and students

Our group is supported by the Chinese Academy of Sciences, the National Natural Science Foundation of China, the 973 Program and the National Key Research and Development Program of China. In the research group, we have four senior and three young research fellows (five members having Ph.D. in physics, two members having Ph.D. in biology). All group members have a good division of research and collaboration, forming a strong team.
Currently there are 12 graduate students working for their Ph.D. theses in the group. We have outstanding graduate student enrollment sources such as Peking University, Tsinghua University, Fudan University, Beijing Normal University, Shandong University, Wuhan University, Xi'an Jiaotong University, Sichuan University, Nankai University, etc.

The Institute of Physics, Chinese Academy of Sciences P.O.Box 603,Beijing 100190,China
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