Editors: Andrew McAllister, Molly Kozminsky, and Whit Froehlich
If you’re a millennial who thinks dating in the age of Tinder is difficult, you may find parallels between your dating life and the complexities of reproduction. The process of a sperm meeting an egg to create a cell that successfully implants in the uterine wall and subsequently creates a human is incredibly intricate. Similar to the world of dating, two have to meet, decide they like each other, and then invest time and energy to grow together as a couple. From finding a mate to the biological processes behind pregnancy, reproduction may seem downright impossible. Luckily mother nature has devised sneaky and fascinating ways to improve the chances of a successful pregnancy. Evolution favors those who pass their DNA on to as many offspring as possible, and natural selection has worked for years to optimize reproduction. If only Tinder were that good at getting you a date!
Editors; Noah Steinfeld, Tricia Garay, and Scott Barolo
A glance into any organic chemistry or biochemistry textbook reveals a dizzying variety of chemical compounds, reactions and mechanisms. It is not at all obvious why one particular class of reaction, the attachment and detachment of a phosphate group (PO43-) to molecules like nucleotides and proteins, is central to making the chemistry of life “go.”
So where do we find phosphorylation in biochemistry? The answer is: pretty much everywhere! I will discuss two key examples. Firstly, phosphorylation is important in “cell signaling,” the sensing of messages from outside a cell and their incorporation into cellular decision-making. It’s worth observing that there isn’t anything we’d recognize as a brain in cells – decision-making is an emergent property of the integration of these signals, not the doing of a microscopic cellular homunculus pulling levers or “thinking.”
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).
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?
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?