Intrinsically Disordered Proteins have Darwin in retreat.


Intrinsically disordered proteins (IDPs) are proteins that do not have a well-defined three-dimensional structure. They are thought to make up about 51% of all proteins in the human body. IDPs are often involved in a variety of cellular processes, including signaling, transcription, and translation. 

Neo-Darwinism is a modern synthesis of Darwinian evolution and Mendelian genetics. It is the prevailing theory of evolution in biology. Neo-Darwinism states that evolution occurs through natural selection, which is the differential survival and reproduction of individuals with favorable traits.

IDPs do not fit into the Neo-Darwinian paradigm. They do not have a well-defined structure, which makes it difficult to explain how they could be selected for. Additionally, IDPs are often involved in processes that are not directly related to fitness, such as signaling and transcription.

Here are some specific examples of how IDPs work outside of NeoDarwinism:

  • IDPs can act as molecular chaperones, which help to fold other proteins into their correct structures.

  • IDPs can act as signaling molecules, which transmit information between cells.

  • IDPs can act as transcription factors, which regulate the expression of genes.

  • IDPs can act as enzymes, which catalyze chemical reactions.

These are just a few examples of the many ways that IDPs can function without having a well-defined three-dimensional structure as required by NeoDarwinism.

Some IDPs are highly conserved over billions of years of evolution. For example, the HEAT repeat domain is an IDP that is found in proteins from bacteria to humans. The HEAT repeat domain is involved in a variety of cellular processes, including transcription, translation, and protein folding. No change in 1.5 billion years is clear evidence NeoDarwinism fails in this case.

Here are some of the possible reasons why IDPs are conserved over billions of years:

  • They may be essential for the function of certain proteins or cellular processes.

  • They may be able to adapt to changes in the environment more easily than globular proteins.

  • They may be able to interact with a wider range of other proteins than globular proteins.

Intrinsically disordered proteins (IDPs) can mutate and still function outside of NeoDarwinism. This is because IDPs do not have a fixed three-dimensional structure, and their role is not dependent on a specific conformation. NeoDarwinism was founded on fixed structure for function. Thereby a mutation could change this structure for natural selection to act on. No fixed structure, no NeoDarwinism. IDPs function through a variety of mechanisms, including:

  • Binding to other proteins or molecules

  • Catalyzing chemical reactions

  • Regulating gene expression

 However, in many cases, mutations in IDPs do not significantly impact their function. This is opposite from NeoDarwinism.  IDPs have a high degree of redundancy, meaning they can often compensate for mutations in one region by using other areas of the protein. Again if mutations have little effect this breaks the NeoDarwinian model.

Overall, IDPs are a diverse group of proteins that can mutate and still function. This is because their function is not dependent on a specific conformation, and they have a high degree of redundancy.

In summary IDPs can avoid change in function over a billion years. Their flexibility allows it to absorb mutations without change. One IDP can have many targets and effects invalidating the Darwinian "one gene- one protein- one function" model. Finally they are the majority of the proteins in humans.

NeoDarwinism is in full retreat.

Comments

  1. AnonymousSeptember 23, 2023 at 11:42 AM

    Darwinism does NOT require fixed structures, it only requires that something be USEFUL, defined as contributing to survival or reproduction. You very helpfully supplied a nice list of how flexible structures can do that. Thanks.

    ReplyDelete

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