Shanxian Chemical
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Alpha Helix Beta Sheet Hydrogen Bonds
On the Wonder of Hydrogen Bonds in the Structure of Peptides
The structure of polypeptides is related to the mystery of biological functions. Among them, the Alpha helix and the Beta fold, and the shape of the hydrogen bond between the two are different, but they are very useful for maintaining structural stability.
Alpha helix, the peptide chain is coiled in a regular shape, similar to a spiral. The hydrogen bond extends from the carbonyl oxygen of the peptide bond to the amino hydrogen separated from the three residues, just like a ring interlocking, making the helix stable. Each circle contains about 3.6 residues, which gives the polypeptide a specific stiffness and flexibility, and affects its fit with other molecules.
Beta folding, the peptide chain extends in layers. The hydrogen bonds exist between different peptide chains, or at the reentry part of the same peptide chain. The hydrogen bonds between the chains are arranged in an orderly manner, like the interweaving of warp and weft of the fabric, forming a planar structure. The direction of the peptide chain is divided into parallel and anti-parallel, and the hydrogen bonds of the anti-flat are more regular and the structure is more stable.
Although the hydrogen bonds of the two are different, they are both important for the shape retention of peptides. Without this hydrogen bond, the conformation of the polypeptide may change, and the biological activity will also be damaged. Therefore, the study of the hydrogen bond between the Alpha helix and the Beta fold is of great significance in understanding the mystery of biomolecules and the mechanism of life, and opens up a new way for the fields of medicine and biochemistry.
The structure of polypeptides is related to the mystery of biological functions. Among them, the Alpha helix and the Beta fold, and the shape of the hydrogen bond between the two are different, but they are very useful for maintaining structural stability.
Alpha helix, the peptide chain is coiled in a regular shape, similar to a spiral. The hydrogen bond extends from the carbonyl oxygen of the peptide bond to the amino hydrogen separated from the three residues, just like a ring interlocking, making the helix stable. Each circle contains about 3.6 residues, which gives the polypeptide a specific stiffness and flexibility, and affects its fit with other molecules.
Beta folding, the peptide chain extends in layers. The hydrogen bonds exist between different peptide chains, or at the reentry part of the same peptide chain. The hydrogen bonds between the chains are arranged in an orderly manner, like the interweaving of warp and weft of the fabric, forming a planar structure. The direction of the peptide chain is divided into parallel and anti-parallel, and the hydrogen bonds of the anti-flat are more regular and the structure is more stable.
Although the hydrogen bonds of the two are different, they are both important for the shape retention of peptides. Without this hydrogen bond, the conformation of the polypeptide may change, and the biological activity will also be damaged. Therefore, the study of the hydrogen bond between the Alpha helix and the Beta fold is of great significance in understanding the mystery of biomolecules and the mechanism of life, and opens up a new way for the fields of medicine and biochemistry.
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