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An ancient scientific controversy: How did Pauling and Crick uncover the secret of the conjugated helix?
In the 1950s, there were many studies on protein structure in the scientific community. Conjugated helices, or cohelices, have become an important subject of research, and this structural feature occurs in many proteins. At the heart of this fascinating story is the heated debate between the famous scientists Linus Pauling and Francis Crick. Did the two scientists actually steal design ideas from each other in their independent research?
Discovery of cohelix
The existence of cohelical structures sparked controversy when it was first proposed. Pauling and Crick concluded almost simultaneously that this structure was possible. In the summer of 1952, Pauling traveled to England to visit Crick's laboratory, and the two discussed various topics. Crick even asked Pauling if he had considered the concept of co-spirals, and Pauling replied that he had. Paulin has since continued research on the topic and submitted a full-length paper to the journal Nature in October.
"How blurred is the line between innovation and plagiarism in the process of scientific research?"
Crick was dissatisfied with Paulin's report shortly after. He believed that Paulin had stolen his idea, and he submitted a shorter article a few days after Paulin's manuscript was submitted. After some debate, Crick's team concluded that both parties had independently discovered the concept and that no knowledge theft had occurred. Crick's short paper proposed a structural model of the cohelix and introduced repulsion and computational methods to determine its structure.
Molecular structure of cohelix
The structure of a cohelix consists of a repeating pattern of hydrophobic and charged amino acid residues called heptapeptide repeats. Specifically, this repeating pattern is
"The stability of this structure comes from the burial of hydrophobic surfaces."
Role in biology
Co-helical structure is a very important stabilizing element in a variety of proteins, which can promote interactions between proteins and maintain various cellular functions. Its main functions include: membrane fusion, molecular spacing, oligomerization labeling, vesicle movement, and cell structure. For example, HIV infection relies on the membrane fusion properties of co-helices to enter host cells. After the glycoprotein gp120 binds to the host cell receptor, the membrane fusion peptide sequence of gp41 enables the virus to fuse with the cell membrane and ultimately achieve entry.
Design and biomedical applications
With the deepening of knowledge about co-helices, scientists have begun to explore its application potential in the biomedical field. Because cohelices are simple to design and versatile, scientists hope to exploit their properties to develop new drug delivery systems. Co-helical structures can be used to achieve precise targeting of specific cells or molecules, which is critical to improving the effectiveness of drug treatments.
"New nanostructures and protein building blocks can be created through the combination of co-helices."
Additionally, the use of cohelices as the basic building blocks of proteins is changing the way three-dimensional cell culture is performed. These methods not only help scientists study tissue engineering, but also provide new ways to improve treatments and academic research. As science advances, how influential will these small structures be in the promising future?
