New research helps to solve the mystery of protein folding

Du Qishi, a researcher at the Guangxi Academy of Sciences, found that a poorly understood force, the polar hydrogen-p bond, plays an important role in the irregular loop structure of proteins The results were published in the Journal of biomolecular structure and dynamics According to reports, in the three-dimensional structure of protein, the In 1951, according to the concept of hydrogen bond, American chemist Pauling predicted theoretically the existence of a-helix and b-fold, which were confirmed by X-ray diffraction experiment six years later However, what forces support the various loop structures? This problem has not been explained theoretically Duqishi found that the polar hydrogen-p bond in the loop structure may be the supporting force of the loop structure In protein peptide chain skeleton, when the P-plane of two peptide bond units is in the same plane, hydrogen bond can be formed; while when the P-plane of two peptide bond units is perpendicular to each other, polar hydrogen-p bond may be formed Four basic loop configurations and four polar hydrogen-p bond types of dipeptides have been found by advanced quantum mechanical scanning From this point of view, it is possible to derive a more complex loop structure The biological functions of various living bodies in nature are performed by proteins The primary structure of a protein is a peptide chain composed of dozens to hundreds of amino acids Peptide chains are cleverly folded to form a unique three-dimensional structure of various proteins, which perform a variety of biological functions The folding of peptide chain is complex but regular What forces guide peptide folding? This problem is called "the mystery of protein folding" The latest research can help to solve the mystery of protein folding and play a role in protein engineering, enzyme molecular rational transformation and other fields of life science.