After years of collaboration with a research team at Academia Sinica, Prof. Rong-Long Pan and Prof. Yuh-Ju Sun have successfully outlined the molecular structure of the membrane protein H⁺-pyrophosphatase that acts as a hydrogen ion channel of plant vacuoles. This breakthrough in membrane protein research attracted the attention of international researchers, and was published in Nature on May 29, 2012.

President Lih J. Chen expressed, during the press conference held at National Science Council on April 9^th that all excellent researchers have two things in common: one is its significance, while the other is its uniqueness. The result of the research done by Professors Pan and Sun is undeniably important and unique. The reviewers of their article commented that "the science community has been waiting for this for about thirty years!"

Prof. Pan indicated that the research of genetic cloning and purification of H⁺-pyrophosphatase were already done and published by foreign research teams twenty five years ago. However, his research team decided to utilize the strength of NTHU's College of Life Science in structural biology to continue their study in this field, and it took only 5 years to surpass all other research groups in the world. President Chen praised the NTHU's team for doing the research that other labs thought impossible and is currently the first research team in Taiwan to successfully resolve the structure of multiple trans-membrane membrane proteins./p>

Prof. Yuh-Ju Sun pointed out that 30% of cell protein is in the form of membrane proteins. Currently, only one percent of all types of membrane proteins' structures are resolved and analyzed. The reason being, it is difficult to extract membrane proteins from cell membranes, and it is equally challenging to crystallize membrane proteins to build high resolution molecular structure for analysis. Prof. Sun's research team, however, used X-ray crystal diffraction method and successfully built the 3-dimensional molecular structure in high resolution of H⁺-pyrophosphate, and thus unveiled the mystery of this proton channel.

Furthermore, H⁺-pyrophosphatase is composed of two similar protein molecules, with each protein molecule penetrating the cell membrane 16 times. Its structure is extremely complex and can also transform the chemical energy of metabolic byproduct pyrophosphate into energy that other enzymes can utilize. Prof. Sun stated that H⁺-pyrophosphatase in plants can influence the growth rate and capacity for salt, cold and drought, thus, H⁺-pyrophosphatase is a key enzyme in the development and improvement of commercial crops. In addition, pathogenic bacteria such as Tetanus, Periodontal and Pylori also have similar protein as H⁺-pyrophosphatase on their cell surface, this means that the H⁺-pyrophosphatase can also be used to develop drug that targets protein structures on the pathogenic bacteria.

Lastly, the research done by Professors Pan and Sun built the foundation for H⁺-pyrophosphatase's use in the improvement of commercial crops, drug engineering, and biomass energy supply, moreover, it wins Taiwan an international recognition and establishes a milestone in the field of membrane protein study. "It is expected that their work will have great potential in the research on environment, green energy, agricultural and medical field, and I am proud that they are members of National Tsing Hua University," said President Chen.