Progress in protein structure and function studies in China during 2010–2011

This is the authors' abstract. We don't add key points for this paper.

The last few years witnessed remarkable progress in the field of protein science research in China, as best illustrated by the increase in both the quality and quantity of publications by Chinese scientists in national and international journals. Here I would like to highlight some of the research and review papers published in China during the 20102011 period. 1 Computational and bioinformatics studies Yan et al. [1] studied the impact of different amino-acid networks (such as hydrophobic and hydrophilic networks) on the folding rate of proteins. The paper by Guo et al. [2] proposed an algorithm to predict protein folding rates based on primary amino acid sequences. The results showed that the folding rates could be predicted with relatively high accuracies. Zhang and Luo [3] revealed that protein folding is a quantum conformational transition and that the folding rate parameters can be quantitatively studied based on this observation. Chen et al. [4] demonstrated that with domain-domain interactions taken into consideration in studies examining protein-protein interactions, human protein interaction networks could provide more detailed information that was distinct from the networks based solely on protein-protein interaction datasets. Such results indicate that domain information should be used to provide additional information for understanding human protein interaction networks. Wei [5] constructed an interaction network for integrin-mediated cell adhesion proteins by data-mining. This study revealed a relatively small number of key motifs dominated by three-component complexes. The paper by Yan et al. [6] indicated that the composition of functional domains can be used to represent proteins in protein fold recognition. Cong et al. [7] performed extensive multi-conformational docking and molecular dynamics simulations on the possible binding mode of two inhibitors of N-substituted derivatives to the hydrophobic pocket of the HIV-1 envelope protein gp41. The results showed that binding is primarily driven by non-polar interactions. Nonetheless, polar interactions also play important roles in orienting the ligands in the pocket. Sun et al. [8] performed in silico studies on the he-magglutinin protein from the swine-origin influenza virus A, which caused a worldwide pandemic in 2009. Since hemag-glutinin is the most important protein for the molecular epidemiology and pathogenesis of the influenza virus, this study should shed new light on the determinants of the vir-ulence and pathogenicity of the virus. Li and coworkers [9] analyzed the rare codon and mRNA structure of Ustilago maydis CYP51 and performed docking of this protein with the fungicide Tebuconazole. The study …