#chemistry major

[ifwebefriends]

Me reassuring myself: it’s okay Ford Pines probably also calculated a -513.0 M HEPES solution in biochem lab it’s okay

[mintysneezes]

Me after spending hours in the lab only to get a .05% yield

[consult-sherlockholmes]

Can you explain to me the chemistry behind the denaturation of enzymes and the process of allosteric and competitive inhibition?

First of all it's important to understand what an enzyme is. An enzyme is a protein, that catalyses reactions after binding to a substrate and then converts it or splits it. An enzyme has a very specific shape so it can bind to the substrate, it's like a key and a lock. The substrate binds to the binding site, and in the catalytic or active centre the reaction takes place.

This is important to understand denaturation: Proteins are made out of amino acids that are bound with peptide bonds. Proteins have several levels of structure: Their primary level is the sequence of amino acids, the secondary structures are folded structures due to interactions of the peptide backbones via hydrogen bonds, like alpha helices or beta sheets. The tertiary structure is folding of the peptides due to electrochemical interactions between different amino acids. Amino acids can have different charges due to their side chains, they can be positive, negative or neutral charged. So those charges will either attract or repel each other, putting the peptide chain in a certain three dimensional shape or conformation. In the quaternary structure several peptide chains come together to create a bigger functional unit (the enzyme) made out of subunits, they often also interact with ions (cofactors) as their catalytic centre where the catalysed reaction takes place. All those levels create the specific shape of the enzyme that is required to bind to their target substrate. So if those structures are changed in any way, it won't work anymore because it can't bind. Just reading it probably makes it difficult to understand, so here's a textbook graphic.

This shape can be changed by denaturation. A protein can be denaturated by heat, or changed pH or high salinity and other not optimal conditions. During those conditions like changed pH the interactions between the molecules and side chains do not work anymore because pH can change the charges of the sidechains, so secondary, tertiary and quarternary structures will be changed. When those structures are changed the binding site will change too and not resemble the lock anymore where the key substrate can bind, so now the enzyme is inactivated/inhibited.

Enzymes can also be inhibited (or activated) by regulatory molecules binding to the enzyme, inhibitors or activators. This can be a competitive inhibition, when the inhibitor binds at the same binding and active site and blocking it, making the actual substrate that should be processed unable to bind there. Like a lock that already has a key stuck in it, you can't put another key in there. Allosteric inhibition is when the inhibitor binds at another site, not directly at the active site where the substrate binds. But by binding to the allosteric site the conformation of the enzyme gets changed by chemical interactions, changing the binding site so the substrate doesn't get recognised anymore. A key can't be insterted into a lock that has been changed.

Inhibtion can be irreversible (making the enzyme dysfuntional for the rest of it's existence until it is degraded) or reversible.

[sleepy-gardevoir]

march 21, 2023 - tuesday week 3

tuesday is my busiest day because all of my classes and all of my extracurriculars meet, but i think i've got everything taken care of so i can go to sleep right when i get back to the room!

i did some annotations on the research paper that i'm summarizing for research rotation, and we had a lecture on how to properly do a research proposal. it sounded really daunting but i'm kind of excited to work more on what i think i want to do for the independent research section of the class!

i also transferred my anatomy notes. we finished our first section (basics of animal form and function) yesterday and started our animal nutrition unit! it's a really interesting class, and iirc we're actually starting with wet labs tomorrow!

song of the day: father by the front bottoms

[mikrhsnobara]

Scrolling through Pinterest and Tumblr to find inspiration to study and promptly not studying because inspiration (?)

[sunshinecomfybabe]

Every time one of my classmates calls me smart I feel like I'm gonna scream. I'm not allowed to complain because they brush it off and say I don't have to try too hard cuz I'm smart. I'm trying so hard that I have steam coming out of my ears!

[madam-quack]

Level 1: *forgets someone’s name and mentally sings alphabet to try to remember what letter it starts with*

Level 2: *forgets that a midwestern state exists, sings 50 states song to remember*

Level 100: *forgets element, sings periodic table to song while in the middle of a chemistry exam*

[chemstudent-sherlock]

The neuroscience lecture today was really fun. First about addiction, and then about depression. Discussing the neurochemical changes and how permanent they are. Changes in gene expression and nerve connections. Changes of brain anatomy. Not concerning at all.

....not that I have any of that. Anyway.

[absolute-travesty]

Bitches love me for my ACS style source citing

[walkingzero1]

Chem majors get all the respect from me because that's gotta be like layer 6.5 in the 7 layers of hell and they do that shit with joy and panache

[classickatze]

How I look pretending to pay attention in my chem lecture (I'm just going to watch a 10-minute YouTube video that explains the concept way better when I go back to my dorm)

[tea-from-apush]

"do you have to apply for the chemistry major or is it so unpopular they're like 'nah you're good'" - a classmate to our American history TA (a chemistry major)

[mintysneezes]

The life of a Chemistry major post breaking bad is constantly being asked if you know how to make meth

[consult-sherlockholmes]

Im majoring in chemistry, hopefully I can get a good paying job like data scientist or something alike

Chemistry? Well that sounds familiar, welcome to the chemists. Bachelor's or master's degree? Good luck then to achieve your dreams. But I think a data scientist also requires lots of bioinformatics and statistical knowledge, but that is included in most degrees nowadays anyway.

[sleepy-gardevoir]

december 6, 2023 - wednesday week 2

went on a grocery trip and proctored an exam for the pledges of my fraternity today! also got some stuff done for the pharmacology assignment due tomorrow, and finished a couple of physical chemistry assignments.

trying to take advantage of my free time to get back into reading - have been chugging through the audiobook of i'm glad my mom died by jennette mccurdy (which i highly recommend) and trying to finish up my read of the crow by alison croggon (which i started in august).

song of the day: dark green water - great grandpa

[mikrhsnobara]

Last year I had the highest grade in organic 1 by 0.1.

I like the teacher I like the lesson. I wanted to do good in organic 2 as well. I studied not as much as I could but a lot. I got 8,5. A girl got 10. I was so so sad and so disappointed in me. Like the girl she studied her ass off I know that. And I just couldn’t be happy for her. I was over reacting and I actually cried and I get so fucking dissapointed. I was so sad that I had dissapointed my teacher. She said she was expecting better. And all I could think about was you are not good enough you will never, you will just keep failing and you won’t make true any of your dreams.

But I did good. I did what I could at that moment and a test doesn’t define me. A grade doesn’t define me and just because I didn’t meet expectations doesn’t mean that my teacher hates me.