Molecule companion and isomerase cooperation mechanism open

Molecule companion and isomerase cooperation mechanism open
It is reported the folding problem of protein is an outstanding great biological knowledge question of central rule of molecular biology. Recently, German scientist's experiment finds, companion's inferior base of molecule can strengthen the activity of isomerase in the folding course of protein, protein that has jointly produced the high efficiency of the two function folds auxiliary function. The relevant research results are published on " institute's publication of American national academy of sciences " of the near future.

Amino acid chain must be folded into particular space structure, protein has a biological function. When a kind of protein was not folded correctly, will cause a lot of kinds of diseases, such as sickle type cell anemia, mad cow disease and senile dementia,etc.. So, the folding question of protein is one of the front subjects of the domain of life sciences, closely related to human health.

The research in recent years shows, particular isomerase has function of promoting folding protein. Its in that the intersection of peptide and key to connect amino acid have until type and two kind different to construct the body against formula, allow to form slender peptide chain along type peptide key, cause the twisting together of peptide chain against type peptide key, particular isomerase can promote the above-mentioned suitable instead two kinds differently and construct the conversion between the body. If lack necessary isomerase, this course of conversion will be very slow. It is the molecule companion that another kind has the one that folded auxiliary function, it can discern the non- natural conformation of peptide chain and bind with it, prevent the mistake from being folded or the insoluble matter emerges, after finish the function and its separation, component not forming these proteins while carrying out the function. However, the mechanism in coordination with cooperation of the above-mentioned two kinds of auxiliary folding functions has not been clear all the time.

Germany visit the intersection of Roy and special university and Max - the intersection of Plonk and the intersection of protein and folding zymology study, stand the scientist's latest research indicate, at auxiliary folding the intersection of albumen and chain, have inferior help of base, companion of molecule, proline isomerase can blow get as good result to different amino acid. The scientist has described a kind of mechanism proved how these enzymes are inferior base which use them come as the best folding enzyme work. First of all, capture those yet folding peptide chains, then the inferior base of isomerase of giving them in inferior base of the molecule companion. This transmittance process finished soon has simplified the work of the inferior base of isomerase. The working speed of isomerase will probably depend on the transmission situations of these two function centres.

The above-mentioned conclusion is a scientist, through comparing two kinds of different enzymes are obtained, inferior base of isomerase of having proline alone of an enzyme, another kind has inferior base of companion molecule yet except catalyzing inferior bases. In a situation that not as companion's inferior base of molecule, short peptide that the isomerase activity highly depends on proline and corresponds to the array and treating the folding albumen chain. And there is existence of companion's inferior base of molecule, the activity of folding protein increases greatly, and the chemical property independent of amino acid. Unfolded albumen chain and good combination of the molecule companion can guarantee its very good folding, and can accelerate with folding enzyme independent of array. (Li Shan)

Molecule companion and isomerase cooperation mechanism open