Sushi (or Lack Thereof): Evolutionary Relationships through Muscle Protein Profiles

   The last few decades in science have centered on genomics, the study of genomes, especially the human genome. Though genomics is still an evolving field, proteomics, the study of the structures and functions of proteins, has emerged as one of the hottest fields in science. The genome, which consists of long stretches of non-coding regions, does not tell the entire story. Protein, the product of the coding sequences of DNA, can give a more straight-forward view. Proteins are also altered after translation from RNA, indicating that life cannot be entirely explained by simply referring to a sequence of DNA bases. Furthermore, it is possible that the non-coding regions of DNA have a role in protein regulation, but that cannot be determined without consulting the proteins themselves. Because of the importance of proteins in all molecular interactions, proteomics projects to be a ground-breaking science that could very well change our perception of life.
   Still, proteomics is an incredibly complex field because the proteome of an organism isn't constant. Every cell type utilizes different proteins to fulfill its duties, and these proteins vary as an individual grows and matures- and that is only within a single organism. Proteomics becomes vastly more complex when comparing species
   In the past, scientists had to examine anatomical features or track development and behavior to determine evolutionary relationships. Though the technique was often correct, it was extremely prone to error. Genomics and proteomics are much more accurate, as they illustrate relationships at the molecular level. The more similar the genomes or proteomes of two species, the more closely related they are (the more recently they diverged from a common ancestor).
   In this lab, we will attempt to infer evolutionary relationships by studying the muscle protein profiles of various sea creatures, isolated from sushi. First, we will add a buffer to begin the denaturation process of the muscle proteins. The buffer will also give the proteins a negative charge, so that they will run on the gel. We will then run our proteins on a gel, just as if they were DNA. The resulting gel will give us a general profile of the muscle proteins in each species, so we can create a cladogram.

Results:

Visible lanes from left to right: Kaleidoscope Marker, salmon, scallop, shrimp, actin/myosin marker