Capture and Release of Genomic DNA Using Functional Magnetic Nanoparticles
Water actively participates in the protein-protein interaction through hydrogen bond, contributing to the structure stability, molecule recognition and interface complementarity. Thus, it should be seen as part of protein structure, and be taken into account in the study of protein-protein interaction. Considering that water which may contribute to protein interaction must bind fast with protein, here we solvated the complex on the concept of ‘the first hydration shell, which is often used in the molecule dynamics study. Then we identified all the interfacial residues, and analyzed characters of residues mediated by water. This method was applied to 12 CAPRI targets. Results show that water mediated interaction and direct hydration bonds are not only the same abundant, but they also interlace to form network, the way in which they contribute to the stabilization of complex. The analysis of water is supposed to provide helpful information for recognizing binding interface and further improving the accuracy of protein structure prediction.
water mediated residues protein-protein interaction
Song Li Hongna Liu Zhifei Wang Yafei Guo Lan Tian Lin Lin Nongyue He
Key Laboratory of Green Packaging and Application of Biological Nanotechnology of Hunan Province, Hu State Key Laboratory of Bioelectronics, Department of Biological Science and Medical Engineering.Sou
国际会议
The 5th International Forum on Post-genome Technologies(5IFPT)(第五届国际后基因组生命科学技术学术论坛)
苏州
英文
2007-09-10（万方平台首次上网日期，不代表论文的发表时间）