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The magic of hydrogen bonds: How do β-sheets connect the fate of proteins?
β-sheet is a common structural feature in protein secondary structure, consisting of a structure containing multiple β-strands that are connected to each other by hydrogen bonds. These folded shapes resemble ripples of cloth, with twists and wrinkles, and play important roles in many natural biological processes, particularly in the stability and function of proteins.
Basic structure and formation of β-folding
β-sheets are composed of multiple β-strands, which are connected by hydrogen bonds. In the β-chain, hydrogen bonds mainly occur between the nitrogen and oxygen atoms of the amino acid backbone. The stability of this structure makes β-folding widespread during evolution.
The "folded" appearance of the β-sheet arises from the effects of tetrahedral chemical bonding, which results in a distance of about 6 Å between adjacent Cα atoms instead of 7.6 Å.
History and Development
The discovery of β-folding can be traced back to the 1930s, when scientist William Astbury first proposed the principle of β-strands interacting through hydrogen bonds. However, the model at the time was incomplete due to the lack of necessary amino acid bond geometry data. Later, in 1951, Linus Pauling and Robert Corey modified this model, establishing the planarity of the peptide bond and adding accuracy to the β-sheet structure.
Importance of Hydrogen BondingThe stability of β-folding lies in the formation of its hydrogen bond network, which not only provides structural support but also affects the function and interaction of proteins. β-folds can be divided into two forms: parallel and antiparallel. The antiparallel form is more stable because this arrangement can form planar connections between hydrogen bonds.
In the antiparallel arrangement, the orientation of the β-strands alternates so that hydrogen bonds can form in an ideal plane for maximum stability.
Biological significance
β-folds are not only present in functional proteins, but are also associated with a variety of diseases, including Alzheimer's disease and other protein aggregation diseases (proteinopathies). The development of these diseases is often due to the degradation of hydrogen bonds and abnormal protein folding, leading to the formation of aggregates and cellular toxicity.
Structural types and common structural modules
Common structural modules of β-folding include β-hairpin, Greek key and β-α-β structures. These structures are not only widely present in proteins, but also play a vital role in structural stability and cell signal transduction processes.
The β-hairpin structure is composed of two antiparallel β-strands connected by a short loop in between, and is commonly found in the structures of many enzymes.
Future Research Directions
With the advancement of biotechnology and computational biology, scientists have gained a deeper understanding of β-folding. By studying the role of β-folding in various biological processes, new treatment pathways may be opened up in the future to address a variety of diseases caused by abnormal hydrogen bonds.
The structure of β-folds and their functions in biology are so important. Have you ever thought about the secrets and detailed mechanisms behind these structures?
