Intrinsically Disordered Proteins resist Darwin over billions of years


According to a 2017 study, about 51% of proteins in the human proteome are intrinsically disordered proteins (IDPs). IDPs are proteins that do not have a well-defined three-dimensional structure. Instead, they exist as a disordered coil of amino acids. IDPs can play a variety of roles in the cell, including signaling, transcription, and protein-protein interactions.

The study that found that 51% of proteins are IDPs was conducted by researchers at the University of California, San Diego. They used a method called "intrinsically disordered protein prediction" to identify IDPs in the human proteome. The study found that IDPs are more common in certain cellular compartments, such as the nucleus and the cytoplasm. They are also more common in proteins that are involved in signaling and transcription.

IDPs are a relatively new area of research, and scientists are still learning about their role in the cell. However, it is clear that IDPs play important roles in many cellular processes. As our understanding of IDPs grows, we will likely learn even more about their functions and how they contribute to human health.

Here are some additional resources that you may find helpful:

  • The Role of Intrinsically Disordered Proteins in Cell Signaling: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3137246/

  • Intrinsically Disordered Proteins: A New Frontier in Protein Science: https://www.nature.com/articles/nrc2119

Intrinsically disordered proteins (IDPs) have been conserved over billions of years because they are able to tolerate mutations in their disordered regions (IDRs). 

Billions of years with no evolution!!

This is because the disordered regions of IDPs are not as critical for their function as the structured regions. Mutations in the disordered regions can therefore be tolerated without significantly affecting the protein's overall function.


There are a few reasons why disordered regions are more tolerant of mutations than structured regions. First, disordered regions are often composed of amino acids that are relatively unstructured themselves. This means that mutations in these regions are less likely to disrupt the overall structure of the protein. Second, disordered regions are often flexible and can adopt a variety of different conformations. This means that even if a mutation does disrupt the structure of a disordered region, the protein may still be able to function properly by adopting a different conformation.

The ability of IDPs to tolerate mutations is one of the reasons why they are so abundant in nature. IDPs play a wide variety of roles in cells, including binding other proteins, interacting with nucleic acids, and serving as scaffold proteins. Their ability to tolerate mutations makes them well-suited for these roles, as they can adapt to changes in their environment without significantly affecting their function.

Here are some examples of IDPs that have been conserved over billions of years:

  • Tubulin, a protein that makes up microtubules, which are essential for cell division.

  • Histone H1, a protein that binds to DNA and helps to package it into chromosomes.

  • Lamin A/C, a protein that forms the nuclear lamina, which is a structural framework that supports the nucleus.

These are just a few examples of the many IDPs that have been conserved over billions of years. The ability of IDPs to tolerate mutations is one of the reasons why they are so important for life.

Neo-Darwinism counts on structured proteins for natural selection (Structured Sequence Hypothesis). Proteins are the building blocks of life, and they are responsible for carrying out many essential functions in cells. The structure of a protein is determined by its amino acid sequence, and this structure is critical for the protein's function.

Structured proteins provide a source of variation for natural selection because they can mutate, and these mutations can change the protein's structure and function.


In this way, structured proteins play a critical role in natural selection. They provide a source of variation for natural selection to act on, and they allow for the evolution of new and beneficial traits.

Neo-Darwinism is a theory of evolution that states that evolution occurs through the accumulation of mutations that confer a selective advantage. Mutations that disrupt the structure of a protein are often harmful, and they are therefore more likely to be eliminated by natural selection. However, IDPs are less susceptible to these mutations, because they do not rely on a specific three-dimensional structure for their function.

For example, a study published in the journal Nature in 2010 found that IDPs were more resistant to mutations that would normally disrupt their function. The study also found that IDPs were more likely to be found in species that are exposed to a lot of environmental change.

This suggests that IDPs may play an important role in the evolution of species, by helping them to adapt to new environments without NeoDarwinism.


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