Darwinian natural selection theory on evolution is a compelling asset for science, both in nature and in lab experiments. An enzyme, for example, can trigger multiple mutations and functional selection in itself so that it can boost its function by over 1000 times. We can witness this type of evolution in virtually anything including synthesized medications and tumor-targeting antibody therapies. However, what’s that spark that created life, that produced something from nothing? Now, the scientists think they discovered that missing element.
Scientists from the Monash Biomedicine Discovery Institute (BDI) discovered what they’ve called Structural Capacitance Elements in genetically mutated proteins linked to various human diseases, including cancers.
Structural Capacitance Elements reside inside the regions of disorder of the proteins where the possibility of fusion into micro-structures after a mutation occurs is present. They have the role of a “feedstock” for evolution to continue, showing the fundamentals of Darwinian evolution by natural selection.
The spark that created life, the Structural Capacitance Elements, found by scientists within proteins
“Up until now, the prevailing belief amongst structural biologists has been that mutations that are implicated in disease act by disrupting protein structures, typically referred to as the ‘loss-of-structure-function’ paradigm. However it has recently been uncovered that more than 40 percent of proteins have no well-defined structure at all,” explained the Associate Professor Ashley Buckle, the study’s leading author.
The team continued to analyze these mutation associated with diseases and uncovered that the Structural Capacitance Elements permits variations to promote a “gain-to-function” feature building new structures where none existed before.
“We realized that our work might have several implications. Not only does it shed light on the evolution of protein structures, but it may also provide insights into the engineering of highly evolvable proteins, and the identification and selective targeting of human disease epitopes,” Ashley Buckle said. “Understanding if and how a mutation may change the protein shape will be pivotal in targeting that protein for use in therapeutics that recognize the mutated region,” the researcher concluded.