pH依赖蛋白质相互作用 z-bo 2020-10-28 347

　　The research team led by Feng Yinggang, a researcher in the Metabolism Research Group of Qingdao Institute of Bioenergy Processes, Chinese Academy of Sciences, is a pair of energy-microbe interaction protein modules with unique pH-dependent double binding sites. I found this switching phenomenon and clarified it. Its chemical and structural mechanism. Recently, relevant research results have been published in "Science Progress". This research reveals the complex and complex regulation mechanisms of biological systems and is used to develop pH-dependent protein equipment and biological materials. These proteins have important values in synthetic biology and biotechnology applications. We provide new materials.

　　PH is an important element in almost all chemical reactions that occur in aqueous solutions, and it plays an important role in the process of life. Biology has many pH-dependent protein function switches, which can regulate the physiological and biochemical processes of cells, and can be used as important detection equipment and function switches in the development of biotechnology. The currently known pH-dependent protein conformation changes are realized by sensing pH changes and realizing "on/off" switch control. The new pH-dependent protein interaction method has scientific application value. You can see there. The metabolomics research team is studying serum bodies, which are multi-enzyme complexes that can effectively degrade lignocellulose, and serum bodies of Clostridium acetobutylicum. , Found a new way to change the pH-dependent protein interaction. Using nuclear magnetic resonance technology, the researchers found that a pair of cell body assembly modules (adhesion module and docking module) in bacteria selectively bind to one site under low pH conditions and bind to one site under high pH conditions. We found that it is selectively bound to the site. Another website.

　　Therefore, it forms a transition between two interacting sites under different pH conditions (see figure). The researchers used a variety of biophysical techniques between these two protein modules (two of the docking modules), such as nuclear magnetic resonance, X-ray crystallography, trace calorie measurement, and molecular dynamics simulation. We will clarify the pH-dependent chemical and structural mechanisms of the interaction. The multiple pairs of asymmetric residues on the binding site are combined with the pKa drift of the negatively charged flexible region residue sequence on the adhesion module binding site, and bind to the pH-dependent site of the protein module interaction pair This will cause switching phenomena. Different from other known pH-dependent protein interaction methods, this pH-dependent protein interaction mode reveals the complex molecular mechanism of life, the development of biological materials, and the potential of protein sensing devices. The design and other biotechnology applications for designing and synthesizing biological components provide brand new materials and solutions.