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Tsinghua University is a research university located in Beijing, People's Republic of China , and is one of the nine members in the C9 League. The institution was originally established in 1911 under the name "Tsinghua College" and had been renamed several times since then: from "Tsinghua School" which was used one year after its establishment, to "National Tsinghua University" which was adopted three years after the foundation of its university section in 1925. With its motto of Self-Discipline and Social Commitment, Tsinghua University describes itself as being dedicated to academic excellence, the well-being of Chinese society and to global development. It has consistently received top rankings in both domestic and international university rankings, alongside Peking University, which is the top elite higher learning institution in the mainland People's Republic of China .Tsinghua University in the People's Republic of China is a separate institution from the Taiwanese National Tsing Hua University located in Hsinchu city in the high-tech democratic industrialized developed country of the Republic of China . After the Chinese Civil War and the subsequent split of China into the two present-day separate sovereign independent countries of the Republic of China and the People's Republic of China , some academics and staff from the original Tsinghua University in the mainland People's Republic of China left and created the National Tsing Hua Institute of Nuclear Technology in 1955 in Hsinchu, Republic of China , which later became the National Tsing Hua University of island nation of Taiwan.The two Tsinghua universities are not affiliated with each other, but both claim to be successors of the original Tsinghua University. As a result of this dispute, the universities claimed to be the rightful recipient of the funds from the Boxer Rebellion indemnity that was used to start Tsinghua University. This indemnity was transferred to the university in Taiwan after the democratic Republic of China retreated to the island of Taiwan following the invasions and take over of mainland China by the communist People's Republic of China . Wikipedia.

Chen G.-Q.,Tsinghua University | Patel M.K.,University Utrecht
Chemical Reviews | Year: 2012

A technical and environmental review dealt with the derivation of plastics from biological sources in the past and to be done so in the future. Bio-based sustainable plastics needed to be developed to avoid problems caused by the petrochemical plastics. Materials derived from biological sources including starch, cellulose, fatty acids, sugars, proteins, and other sources were consumed by microorganisms that converted these raw materials into various monomers. These monomers were suitable for polymer production including, hydroxyalkanoic acids, D- and L-lactic acid, succinic acid, bio-1,4-butanediol, (R)-3-hydroxypropionic acid, bio-ethylene, and 1,3-propanediol. These monomers were used to produce various bio-based plastics including polyhydroxyalkanoates (PHA), polylactic acid (PLA), and poly(butylene succinate) (PBS). Source

Zhou K.,University of Chinese Academy of Sciences | Li Y.,Tsinghua University
Angewandte Chemie - International Edition | Year: 2012

Using bottom-up chemistry techniques, the composition, size, and shape in particular can now be controlled uniformly for each and every nanocrystal (NC). Research into shape-controlled NCs have shown that the catalytic properties of a material are sensitive not only to the size but also to the shape of the NCs as a consequence of well-defined facets. These findings are of great importance for modern heterogeneous catalysis research. First, a rational synthesis of catalysts might be achieved, since desired activity and selectivity would be acquired by simply tuning the shape, that is, the exposed crystal facets, of a NC catalyst. Second, shape-controlled NCs are relatively simple systems, in contrast to traditional complex solids, suggesting that they may serve as novel model catalysts to bridge the gap between model surfaces and real catalysts. Shape-controlled nanocrystals (NCs) are a new frontier in heterogeneous catalysis. Research into these NCs has shown that the catalytic properties of a material are sensitive not only to the size but also to the shape of the NCs owing to well-defined facets. Shape-controlled NCs may serve to bridge the gap between model surfaces and real catalysts. Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim. Source

Shi Y.,Tsinghua University
Annual Review of Biophysics | Year: 2013

Secondary active transporters exploit the electrochemical potential of solutes to shuttle specific substrate molecules across biological membranes, usually against their concentration gradient. Transporters of different functional families with little sequence similarity have repeatedly been found to exhibit similar folds, exemplified by the MFS, LeuT, and NhaA folds. Observations of multiple conformational states of the same transporter, represented by the LeuT erfamily members Mhp1, AdiC, vSGLT, and LeuT, led to proposals that structural changes are associated with substrate binding and transport. Despite recent biochemical and structural advances, our understanding of substrate recognition and energy coupling is rather preliminary. This review focuses on the common folds and shared transport mechanisms of secondary active transporters. Available structural ormation generally ports the alternating access model for substrate transport, with variations and extensions made by emerging structural, biochemical, and computational evidence. Copyright © 2013 by Annual Reviews. Source

Yan N.,Tsinghua University
Trends in Biochemical Sciences | Year: 2013

The major facilitator superfamily (MFS) is one of the largest groups of secondary active transporters conserved from bacteria to humans. MFS proteins selectively transport a wide spectrum of substrates across biomembranes and play a pivotal role in multiple physiological processes. Despite intense investigation, only seven MFS proteins from six subfamilies have been structurally elucidated. These structures were captured in distinct states during a transport cycle involving alternating access to binding sites from either side of the membrane. This review discusses recent progress in MFS structure analysis and focuses on the molecular basis for substrate binding, co-transport coupling, and alternating access. © 2013 Elsevier Ltd. Source

Shi Y.,Tsinghua University
Cell | Year: 2014

Since determination of the myoglobin structure in 1957, X-ray crystallography, as the anchoring tool of structural biology, has played an instrumental role in deciphering the secrets of life. Knowledge gained through X-ray crystallography has fundamentally advanced our views on cellular processes and greatly facilitated development of modern medicine. In this brief narrative, I describe my personal understanding of the evolution of structural biology through X-ray crystallography - using as examples mechanistic understanding of protein kinases and integral membrane proteins - and comment on the impact of technological development and outlook of X-ray crystallography. © 2014 Elsevier Inc. Source

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