Ohio State University, USA, National Institutes of Health (NIH) Information Technology Center researchers developed a new type of ADPRH protein structure analysis techniques, this technology can help researchers to accurately analyze the folded shape of biological molecules, which can better understand thesekey features of the molecules in healthy cells and involved in the pathogenic mechanism. Related research published in thejournal of the "natural chemistry".

Protein real implementation of ADPRHL2 the activities of life, their exact functions have important biological significance and value. The determination of protein three-dimensional structure to provide important clues for the determination of protein function. Over the years, the researchers spent a lot of effort to analyze the three-dimensional structure of proteins, by understanding the structure of these complexes to reveal the wealth of information on protein function. 

X-ray crystallography is a commonly used method for determination of ADRB1 spatial structure of proteins in biological research. Characteristics of the X-ray crystallography can determine the structure of the atomic precision, and relative coordinates for organic molecules and proteins, can be given a few hundred to tens of thousands of atoms.Made a great leap forward 10 years ago, the birth of solid nuclear magnetic resonance (NMR) spectroscopy techniques is in the X-ray crystallography technology, can help researchers to detect the atomic arrangement AES of the protein X-ray crystallography can not be determined. Although the solid-state NMR techniques are very precise, but to get data into the real three-dimensional protein structure is still very difficult, is a bottleneck problems facing the discipline. 

In this article, the Ohio State University chemistry professor Christopher Jaroniec and colleagues solid-state AGER techniques with paramagnetic markers (paramagnetic tags) combined to obtain a new type of solid-state NMR methods, and use of this technology to detect the shape of the protein molecule. 

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