Advances in the study of the structure and function of calcium-tuning proteins.

Recently, Li From the Wuhan Institute of Physics and Mathematics of the Chinese Academy of Sciences made new progress in the study of protein structure and function under restricted conditions.
magnetic resonance spectrum is the most powerful means to obtain the high-resolution structure and function of proteins in complex environments.
used MRI to study the structure and function of the important signal transducting protein, the calcitonin- protein, in an anti-adhesive beam that simulates a limited-domain environment.
limiting environment is common in cells, such as molecular machines such as molecular companion protein GroEL, peptide chain channels of the nuclear glycogen, and membrane gaps in a variety of cellular devices.
studies have shown that the limit environment has an effect on protein folding, stability, etc., but little is known about the influence of limit domain on the structure and function of multistruct domain protein.
This study found that: 1) the structure of calcium-tuning protein is significantly different from that of thin solution, in which calcium-tuning protein mainly exists in a stretched structure, while a compact spherical structure is formed in the limited-area environment; 2) Calcium-tuning proteins can interact with MLCK peptides, AcN19 peptides, and somatostatin peptides in the solution, while in the limited-domain environment, calcium-tuning proteins can bind to MLCK and AcN19 peptides, and somatostatin peptides can hardly be combined.
further study found that the difference in function between the two environments was due to spatial volume effects rather than affinity differences.
the study analyzes the high-resolution structure of dual-domain proteins in the first limited-domain environment, and provides a structural basis for understanding the environmental effects of protein function.
, the study suggests that cells may be able to regulate the function of some bio-macrons using a limited environment.
Guohua, an assistant researcher at the University of China, and Dr. Jian Kai are co-authors of the paper, and researcher Li Zhigang is a communications contact.
the study was supported by the Ministry of Science and Technology of China, the Youth 10,000 Program, the National Natural Science Foundation of China and Wang Guangcheng's First Talent Program.
study was published in the German journal Angew.Chem.Int.Ed.
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