A joint research group of RIKEN, High-Brightness Photon Science Research Center, and Osaka University has succeeded in elucidating why the proteins produced by bacteria that live at temperatures above 100 ° C have high heat resistance.It is said that it will be possible to artificially design proteins with heat resistance, and it is expected that it will greatly contribute to the future utilization of functional molecules.
Protein is one of the main constituents of the body of living organisms and plays various roles necessary for survival.Protein exerts its function by connecting 20 kinds of amino acids like a chain and folding them precisely.When heat is applied to many proteins, the folded ones collapse and lose their functions.Stability is related to how strongly adjacent amino acids stick to each other when folded.However, various factors such as hydrophobicity (the property of repelling water) and static electricity are involved in a complicated manner, and it has not been known to what extent these factors affect them.
In 2006, the group discovered a protein that could maintain its function even at temperatures above 150 ° C.It has many parts where static electricity easily accumulates, and it was estimated that it is important for heat resistance.In this study, we compared this protein with normal protein and observed the change when heat was applied.As a result, it was clarified that in addition to the effect of static electricity, which was previously considered to be important, hydrophobicity also has a great effect.
This discovery is likely to force a significant shift in guidance in the design of protein-based materials.In order to confirm this discovery, it is necessary to repeat the demonstration experiment, but there is no doubt that a great clue was obtained.
Source:[Japan Agency for Medical Research and Development] Thermodynamically elucidate the mechanism of protein stabilization at temperatures above 100 ° C