The official results of the 9th Critical Assessment of Techniques for Protein Structure Prediction (CASP9) was disclosed on December 6, 2010. The JIANG_Assembly protein structure prediction server developed by a research group of Dr. JIANG Taijiao from the Institute of Biophysics, Chinese Academy of Sciences (IBP) was among the top 20, indicating that Chinese scientists have started to play a significant role in the field of protein structure modeling although in this and previous CASPs, most of the top groups were still from the US.

Protein structure prediction is one of the most challenging research directions with many prohibitive difficulties in computational biology. In order to obtain an in-depth and objective assessment of our current capabilities in the area of protein structure prediction, John Moult initialized a campaign for Critical Assessment of Techniques for Protein Structure Prediction, called CASP, which started in 1994 and organized every two years. CASP has attracted interests of many experts from biophysics, computer science, high energy physics, computational chemistry and computational mathematics. During the campaigns, participants will predict as much as possible about a set of soon to be known structures. These will be true predictions, not ‘post-dictions’ made on already known structures.

The CASP9 took place between early May and late July of 2010. About 129 proteins were used as prediction targets whose structures were determined by X-crystallography or NMR spectroscopy while remained unreleased during the campaign. There were 176 research groups and more than 80 protein structure prediction servers from all over the world participated in the CASP9. The protein structure prediction server JIANG_Assembly developed by Dr. JIANG’s group was ranked 19th.

Dr. JIANG returned to China in 2005 with the support of “Hundred Talents Program” of CAS after finishing his education in the US. Since then, his group had started to work on the area of protein structure modeling. His lab has developed effective scoring functions and new algorithms for modeling both protein backbone and side-chain conformations.