Shanxian Chemical
SUPPLEMENTS
Cysteine Hydrogen Bond
On the Wonder of Hydrogen Bonding of Cysteine
All things in the world, the mystery of biochemistry, often hidden in the micro. Cysteine is one of the amino acids, and its hydrogen bonding energy is really extraordinary.
Cysteine contains a sulfhydryl group, which is abnormally active. In the biochemical system, the hydrogen of the sulfhydryl group can form hydrogen bonds with the electronegative atoms of other substances, such as oxygen and nitrogen. This hydrogen bond is not a strong bond, but the force should not be underestimated.
Looking at the conformation of proteins, the hydrogen bond of cysteine is the most powerful. The folding and stability of proteins depend on this. When the polypeptide chain twists and turns, cysteine is in it, and hydrogen bonds are used to tie other segments, giving the protein a unique three-dimensional shape. In this way, a protein can perform its functions, catalyze biochemical reactions, or transport substances in and out of the cell, regardless of its shape.
And in the active center of the enzyme, the cysteine hydrogen bond is also the key. When the substrate approaches the enzyme, the force of the hydrogen bond can guide the substrate into place, just like the tenon and mortise fit, and it is accurate. In this way, the catalytic efficiency of the enzyme is greatly increased, and the biochemical reaction can be carried out efficiently and orderly.
Furthermore, in the way of cell signaling, cysteine hydrogen bonds are also useful. Information transmission between molecules often depends on the change of hydrogen bonds. Signaling molecules bind to receptors, and cysteine hydrogen bonds are either born or destroyed, and information is then transmitted, which regulates cell function.
Cysteine hydrogen bond, although tiny, is an indispensable element in the mystery of life. Exploring its mechanism and understanding its function is of far-reaching significance in the study of biochemistry and medicine.
All things in the world, the mystery of biochemistry, often hidden in the micro. Cysteine is one of the amino acids, and its hydrogen bonding energy is really extraordinary.
Cysteine contains a sulfhydryl group, which is abnormally active. In the biochemical system, the hydrogen of the sulfhydryl group can form hydrogen bonds with the electronegative atoms of other substances, such as oxygen and nitrogen. This hydrogen bond is not a strong bond, but the force should not be underestimated.
Looking at the conformation of proteins, the hydrogen bond of cysteine is the most powerful. The folding and stability of proteins depend on this. When the polypeptide chain twists and turns, cysteine is in it, and hydrogen bonds are used to tie other segments, giving the protein a unique three-dimensional shape. In this way, a protein can perform its functions, catalyze biochemical reactions, or transport substances in and out of the cell, regardless of its shape.
And in the active center of the enzyme, the cysteine hydrogen bond is also the key. When the substrate approaches the enzyme, the force of the hydrogen bond can guide the substrate into place, just like the tenon and mortise fit, and it is accurate. In this way, the catalytic efficiency of the enzyme is greatly increased, and the biochemical reaction can be carried out efficiently and orderly.
Furthermore, in the way of cell signaling, cysteine hydrogen bonds are also useful. Information transmission between molecules often depends on the change of hydrogen bonds. Signaling molecules bind to receptors, and cysteine hydrogen bonds are either born or destroyed, and information is then transmitted, which regulates cell function.
Cysteine hydrogen bond, although tiny, is an indispensable element in the mystery of life. Exploring its mechanism and understanding its function is of far-reaching significance in the study of biochemistry and medicine.
Scan to WhatsApp
