AP Biology class blog for discussing current research in Biology

Tag: #proteinstructure

SARS-CoV-2 Is Making My Heart Ache??

New research from the University of Maryland School of Medicine’s (UMSOM) Center for Precision Disease Modeling identifies the specific protein in SARS-CoV-2, the virus responsible for COVID-19, that causes damage to heart tissue.

Protein Structure Gif

Some experiments they did were performed on fruit fly hearts. When Nsp6 is present in a fruit fly heart, the heart shows structural defects compared to a normal heart without the viral protein. However, when fruit fly hearts with the viral Nsp6 protein are treated with the drug 2DG, the hearts begin to resemble normal hearts more closely.

In their latest study, researchers found that the Nsp6 protein is the most toxic SARS-CoV-2 protein in the fruit fly heart. They also discovered that the Nsp6 protein hijacks the fruit fly’s heart cells, activating the glycolysis process and disrupting the mitochondria, which produce energy from sugar metabolism. When they blocked sugar metabolism in fruit fly and mouse heart cells using the drug 2DG, they found that it reduced the heart and mitochondria damage caused by the Nsp6 viral protein.

Dr. Han, the lead researcher, says this about the protein : “We know that some viruses hijack the infected animal’s cell machinery to change its metabolism to steal the cell’s energy source, so we suspect SARS-CoV-2 does something similar. The viruses can also use the byproducts of sugar metabolism as building blocks to make more viruses,”


Drosophila melanogaster under microscope

Thus, the University of Maryland School of Medicine’s research identified the specific protein in SARS-CoV-2 that causes damage to heart tissue and has found a potential treatment for it. The protein, called Nsp6, activates the glycolysis process in heart cells and disrupts the mitochondria, which are responsible for producing energy through glycolysis and oxidative phosphorylation. By blocking the processes  with the drug 2DG, the researchers were able to reduce the heart and mitochondria damage caused by Nsp6. This discovery aligns with the topic of glycolysis and ATP generation in AP Biology as it highlights the importance of proper metabolism in the functioning of cells and the potential consequences of disruptions to this process.


Advancements in Molecular Imaging May Further Human Knowledge

As we’ve learned throughout unit one, protein shape and structure are pivotal for deciding the protein’s function inside of the cell. Some proteins serve as enzymes to speed up chemical processes, while others serve as antibodies to protect against infectious diseases. Some are hormones, others provide structural support. What all of these proteins have in common is their amine group and carboxyl group which are both bonded to the central carbon, or alpha carbon; consisting of hydrogen, carbon, nitrogen, and oxygen, all proteins seemingly possess the same traits. But not all proteins are the same, in fact, there are twenty different amino acids which all pay tribute to the variable R group. Yet proteins are far more complex than just their variable R group. Proteins are able to reshape and undergo complex transformations that drastically alter their function inside the cell. These complexities, along with outdated technology, have created a substantial lapse of knowledge in this field, and scientists are in dire of a better understanding of the intricacies of protein structure.

Amino Acid Structure

Taking on the challenge of creating cutting-edge technology, a group of scientists stationed at the University of North Carolina Medical School discovered a new methodology to capture live-time imagery of unique protein shape and structure. This technologically advanced technique is being coined the ‘Binder Tag,’ which, “allows researchers to pinpoint and track proteins that are in the desired shape or “conformation,” and to do so in real-time inside living cells” (UNC Health Care).

The group of scientists, led by Ph.D. Klaus Hahn and Ph.D. Timothy Elston understood that they would be attacking a “fundamental challenge” of molecular imagery; this being that working molecules inside of cells are unable to be photographed because light from standard microscopes bends irregularly around particles inside the cell, creating a nearly impossible image to render. The ‘Binder Tag’ method avoids these limitations by inserting a molecule that has received a ‘tag’ into a protein, and then a separate molecule binds to the tag once the protein undergoes some type of formation alteration. Assuming the process is done correctly, researches are able to effectively image the precise location of tagged molecules over time, documenting real-time changes in the protein shapes.

Main protein structure levels en Furthermore, “a technique called FRET (Förster resonant energy transfer), which relies upon exotic quantum effects, embeds pairs of such beacons in target proteins in such a way that their light changes as the protein’s conformation changes” (UNC Health Care). However, FRET has its own limitations, such as the fluorescent beacon may be too weak to track live protein dynamics.

Hopefully, this method can be further experimented within the scientific community so we are able to better understand the complex, dynamic world of protein structure.




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