Methylated Memory

Author: Sarah Kearns

Editors: Naiyiri Kaissarian, Patricia Garay, and Shweta Ramdas

If you saw a hippo on campus, you would remember it. But, would you expect that seeing such a pachyderm roaming on a university would alter the expression of your DNA? A recent study found that rats placed in an environment that tested their memory had alterations to their DNA, or epigenetic changes.

For a long while, we have generally known that neurons within the hippocampus of our brains are responsible for memory. The current model for memory storage is due to the plasticity of neuronal connections, but researchers have recently found that it also involves active changes at the genetic level. These changes come from external factors and are linked to retaining long-term memories, which has implications in stress-related learning and memory disorders.

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The After-Hours Life of a Protein

Author: Sarah Kearns

Editors: Zena Lapp, Jimmy Brancho, Noah Steinfeld

After you get home from work, perhaps after eating dinner, you may start working on other projects or hobbies. Humans aren’t the only ones that have a life after hours. Recently it’s been discovered that many proteins have roles in the cell outside of their main functions. This peculiar behavior led to the name ‘moonlighting,’ referencing individuals who have multiple jobs. A useful analogy might be a werewolf’s behavior under a full moon: being a person during the day, but a wolf at night.

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Analyzing without Lysing: Non-Damaging Techniques for Monitoring Cells

Author: Sarah Kearns

Editors: Whit Froehlich, Ada Hagan, and Irene Park

The interior of a cell is inherently complex with a myriad of processes going on all at once. Despite the clean images that are commonly shown in diagrams and textbooks, the parts inside are more of a whirlwind of structural components, proteins, and products (see Figure 1).

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Figure 1. Left is a cartoon image of a whole cell highlighting the different organelles (cellular compartments). Right is a computer simulation of the cytoplasm, the fluid between organelles. There are thousands of chemical processes going on within it.

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Computing Levinthal’s Paradox: Protein Folding, Part 2

Author: Sarah Kearns

Editors: David Mertz, Zuleirys Santana Rodriguez, and Scott Barolo

In a previous post, we discussed how proteins fold into unique shapes that allow them to perform their biological functions. Through many physical and chemical properties, like hydrogen bonding and hydrophobicity, proteins are able to fold correctly. However, proteins can fold improperly, and sometimes these malformed peptides aggregate, leading to diseases like Alzheimer’s.

How can we figure out when the folding process goes wrong? Can we use computers to figure out the folding/misfolding process and develop methods to prevent or undo the damage done by protein aggregates?

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How to Fold (and Misfold) a Protein (Part 1)

Author: Sarah Kearns

Editors: David Mertz, Zulierys Santana-Rodriguez, and Scott Barolo

Proteins do most of the work in your body: Depending on their shape, they can digest your food, fire your neurons, give color to your eyes and allow you to see colors. Proteins follow instructions encoded in your DNA to fold into their shape, but how do they “know” what shape to fold into to perform their biological functions? What happens when they fold incorrectly?

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