"Protein intrinsic disorder and structure-function continuum" - Review




The concept of protein intrinsic disorder and structure-function continuum does not invoke NeoDarwinism. NeoDarwinism is a theory of evolution that states that evolution occurs through natural selection, which is the process by which organisms that are better adapted to their environment are more likely to survive and reproduce. Protein intrinsic disorder and structure-function continuum is a scientific theory that states that proteins can be disordered, or unstructured, and still function properly. This theory does not rely on the concept of natural selection, and therefore does not invoke NeoDarwinism.

The concept of protein intrinsic disorder and structure-function continuum is a relatively new one in the field of protein science. It challenges the traditional view of proteins as having a fixed, well-defined structure that is essential for their function. Instead, it proposes that proteins can exist in a range of different conformations, some of which are more disordered than others. These different conformations can have different functional properties, and the protein's ability to adopt different conformations can be important for its overall function.

There are a number of factors that can contribute to protein disorder. One is the presence of long stretches of amino acids that are non-polar and therefore do not interact well with each other. These stretches of amino acids can form disordered regions that are flexible and can adopt a variety of different conformations. Another factor that can contribute to protein disorder is the presence of post-translational modifications, such as phosphorylation or glycosylation. These modifications can alter the structure of the protein and make it more disordered.

The structure-function continuum concept suggests that the functional properties of a protein are not determined solely by its structure. Instead, they are also influenced by the protein's ability to adopt different conformations. This means that proteins can have a range of different functional properties, depending on their conformation. For example, a protein that is involved in binding to another protein may have a different conformation when it is bound to its partner protein than when it is unbound.

Here is a more detailed explanation of the two theories:

  • NeoDarwinism: NeoDarwinism is a theory of evolution that states that evolution occurs through natural selection, which is the process by which organisms that are better adapted to their environment are more likely to survive and reproduce. Natural selection can lead to changes in the genetic makeup of a population over time, which can lead to the evolution of new species.

  • Protein intrinsic disorder and structure-function continuum: Protein intrinsic disorder and structure-function continuum is a scientific theory that states that proteins can be disordered, or unstructured, and still function properly. This theory is based on the observation that many proteins do not have a well-defined structure, but are still able to perform their biological functions. The theory of protein intrinsic disorder and structure-function continuum suggests that the structure of a protein is not as important as its function, and that proteins can evolve to have new functions without changing their structure.

As you can see, the two theories are very different. NeoDarwinism is a theory of evolution that relies on the concept of natural selection, while protein intrinsic disorder and structure-function continuum is a scientific theory that does not rely on the concept of natural selection. Therefore, protein intrinsic disorder and structure-function continuum does not invoke NeoDarwinism.

Article snippets:

Protein intrinsic disorder and structure-function continuum

The functional proteome of a given organism noticeably exceeds its corresponding genome due to various events at the DNA (genetic variations), mRNA (alternative splicing, alternative promoter usage, alternative initiation of translation, and mRNA editing), and protein levels (post-translational modifications) that results in the appearance of various proteoforms; i.e., different molecular forms in which the protein product of a single gene can be found

In addition to these induced proteoforms, basic (or intrinsic, or conformational) proteoforms are generated due to the presence of intrinsically disordered or structurally flexible regions in a protein.

Furthermore, protein functionality can affect the structural ensemble of both conformational and induced proteoforms, and hence serves as a factor generating functioning proteoforms

Therefore, a single gene encodes for a wide array of different proteoforms, which represents the foundation for protein multifunctionality.

In other words, instead of the classical protein structure-function paradigm rooted in the “one-gene–one-protein–one-function” model, a correlation between between protein structure and function is described by a more general “protein structure-function continuum” model, where a given protein exists as a dynamic conformational ensemble containing multiple proteoforms (conformational/basic, inducible/modified, and functioning) characterized by a broad spectrum of structural features and possessing various functional potentials.

https://doi.org/10.1016/bs.pmbts.2019.05.003. 2019




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