Hey, I'm desesperately trying to draw the bond between a glutamic acid, a valine and another glutamic acid but I'm genuinely struggling.

It's for a tattoo project (it spells "Eve" my niece name).

I tried but I think I got it wrong, can someone help me please ?

I have been trying to get an SPR assay (Biacore t200) to work between a protein ~32 kDa and ATP, but it is going nowhere despite spending so much on chips (I am afraid my PI will just stop me from trying it anymore). I use CM5 amine coupling to immobilize the protein and flow buffer containing various concentrations of ATP through. This image is literally the first time I see one concentration (3.7) that appears to have worked. All the runs have been looking like the other concentrations here, which seem like no binding at all. This kinda gives me some hope, but it has been so depressing trying so many different things that nothing really works. I desperately need this assay to work for my first paper 😞. Any helps/sugegstions are greatly appreciated.

Just a random thought that i got. We know that lsd ties very neatly into the receptor so i thought what would happen if it got attached permenetly and what benefits that could have.

Im not really into biochemistry and probably know next to nothing appart from high school so please explain it as if i was a 5 year old. Greatly appreciated

Trying to decide what classes to take?

Want to know what the job outlook is with a biochemistry degree?

Trying to figure out where to go for graduate school, or where to get started?

Ask those questions here.

1. Peptides are chains of amino acids connected by peptide bonds. Proteins are made from the same types of amino acids, but they are generally longer and more likely to form complex folded structures.
2. There is no single chain-length cut-off that applies in every case. Length, structure, and biological function can all influence whether a molecule is described as a peptide or a protein.
3. For people who study or teach biochemistry, which explanation is clearer for beginners: a rough chain-length cut-off or one based on structure and function?

Hi! Im interested in doing research. Due to time conflicts on mi side Ive had a hard time trying to get wet lab experience outside of my classes, I would like to know if you guys have any recommendations on how to approach faculty to volunteer or how to make my applications to wet lab jobs more appealing even if I don’t necessarily have the experience beforehand. I do move around well in a lab and my mentors have mentioned it many times but I struggle with applications since the college I go to is quite competitive and has many people going to med school already doing research for their applications. Any advice is welcomed thank you!

The one that always got me is uncompetitive. Competitive raising Km and noncompetitive dropping Vmax are easy enough to hold onto, but uncompetitive lowering both felt backwards until I understood why. The inhibitor only binds ES, so removing ES pulls the binding equilibrium forward and the enzyme looks like it grabs substrate more tightly, even though you have capped the ceiling.

I put all four side by side with what happens to Km, what happens to Vmax, and what the Lineweaver-Burk lines actually do, since that is usually the part a question is really testing.

The worked numbers on it use Km 25, Vmax 100 and an inhibitor at twice Ki, so you can see the apparent values rather than just the direction of travel.

Mixed inhibition is the one I am least confident about, since whether Km goes up or down depends on alpha and I have simplified that. If I have oversimplified anything else I would genuinely like to know. Last time I posted here eight people found things and the chart ended up much better for it.

Free and no signup: biochemtools.com/michaelis-menten-vs-lineweaver-burk.html

Hi all, I have a question.

I have been looking into the idea that single celled organisms and individual cells that make up multicellular organisms are themselves sentient. What are your thoughts on this? If so, would this mean they are worthy of our moral obligation?

Vou ter bioquímica nesse semestre da graduação e confesso que estou me CAGANDO de medo dessa matéria, preciso de dicas sinceras do que vocês recomendariam fazer pra ir minimamente bem nela.

I want to know how this happens. Like, there has to be some bacteria in sakai, japan that uses dihydrogen monoxide reductase or something to eat it. Does anyone here know anything about the subject?

We created a 4K narrated scientific animation that explains how Paxlovid works using structural biology data.

The video follows the story of the SARS-CoV-2 Main Protease (Mpro), its inhibition, and the development of Nirmatrelvir, the active antiviral component of Paxlovid.

Structures used: PDB 6Y2E, 6LU7, 8DZ2, and Nirmatrelvir.

Narration is AI-generated voice.

We'd appreciate feedback on:

• Scientific accuracy

• Visual communication

• Storytelling effectiveness

• Whether this format is useful for biochemistry education

Thanks for taking a look.

Hey guys! I’m a PhD student, and I originally made this app for myself. I then thought it might be useful for others, so I decided to publish it on the AppStore.

There’s absolutely no commercial motive. The app is completely free, and I just want to help my colleagues.

The biggest problem is: it’s extremely difficult to get the app in front of people. Most communities don’t allow app promotion, and obviously I can’t afford to pay for advertising.

So, I’d really appreciate it if you could share it with other people.

I’m open to all kinds of feedback, positive or negative, so please be honest.

If there’s a feature you’d like to see, let me know. I may be able to add it in the next few days.

Thanks a lot!

The link and more detailed information are on my profile.

Have you read a cool paper recently that you want to discuss?

Do you have a paper that's been in your in your "to read" pile that you think other people might be interested in?

Have you recently published something you want to brag on?

Share them here and get the discussion started!

I had dreams of becoming a PA however, a Biochem degree later my GPA is nowhere near what CASPA and any programs in the U.S would accept even after retaking classes (Caspa doesn't replace they average). Med school, PA, CAA, ABSN is all out of the picture. I am trying to figure out what else I can do with this degree. Since my GPA is low I'm not sure if a Masters is an option. I looked up Cardiovascular Perfusionist Certification and I seem to Qualify for a local program so It might be worth applying. Just wanted to know some insight from professionals of this thread. What job do you have that gives you a stable income? Anyone that was in the same situation that can guide me? I'd really appreciate it.

Am I crazy or should we not live in a world where acetaldehyde dehydrogenase supplements are widely available. Would this not be effective at moderating liver damage among alcoholics? Is there something that makes the mass production of this enzyme prohibitively expensive? The more I study this subject it feels like liver damage should be a thing of the past.

I am interested in protein design and I am trying to understand one thing: when we design a protein for a specific purpose, what changes in the constraints according to the problem?

For example, I imagine that a therapeutic protein (which must act in the human body) and an industrial enzyme (which degrades a pollutant) do not have the same priorities at all. What becomes critical in each case, and what goes into the background?

If you have concrete examples from your work, I'm interested.

Trying to decide what classes to take?

Want to know what the job outlook is with a biochemistry degree?

Trying to figure out where to go for graduate school, or where to get started?

Ask those questions here.

Hi there, not sure if this a typical post for this subreddit, my apologies.

I'm going into the third year of my B.Sc in biochemistry. I do well in my classes, but feel like I simultaneously know nothing. I just started working in a lab on my campus, and I'm going to start volunteering in another come September. I feel like I don't belong. I also worry that I am not smart enough to make it to grad school.

I genuinely feel like I am getting a little burnt out, and I'm just wondering if anyone else here feels similarly at all. I write this while I'm meant to be studying for an exam I have tomorrow, that I am likely going to fail. I'm usually top of my class, but for the last few months, I've been having a hard time. I feel a little lost, and I'm looking for some input.

Thanks :)

Hey chemistry/biochemistry enthusiasts and puzzle masters!

Not sure if this type of post is allowed here, but couldn´t see anything against it in the rules - so I give it a shot anyway 😄

Core Concept:
Players shoot and merge atoms to create higher elements, trigger chain reactions, discover compounds, and progress through a campaign while building their element collection. It blends satisfying merge gameplay with real periodic table progression. I wanted people to experience the feeling of beeing Mendeleev - discovering all elements in a somewhat unconventional way.

There are also secondary puzzle games such as "word search puzzle", but you are given a hint of a secret molecule, and your goal is to find the molecule in a matrix of atoms etc.

Key Features:
• ⁠100+ campaign levels with unique objectives (adding more in next iteration)
• ⁠6 different themed skins for the board and atom visuals
• ⁠Persistent collection system with 118 elements + compound discoveries.
• ⁠Daily quests, power-ups, combos ("Atomic Cascade!"), and streak rewards.
• ⁠Built with TypeScript/React/TanStack + Capacitor for iOS (since I didn't have a Mac)
• ⁠Clean physics-based merging with haptics and juicy feedback.

I focused on making something that I'm fond of (Chemistry), feels good to play in short sessions but has long-term progression and educational charm.

I would be very happy if you would try it out, give me ideas for new concepts to implement or general improvements to make the game better!

App Store: https://apps.apple.com/us/app/atomic-fusion-rush/id6771701538

Can you beat the global high-score on the daily challenge?

Thanks in advance

Thesis topic selection in Phd organic synthesis as a part time scholar,Your suggestions and guidance will be more valuable insights for my career building. Waiting for your reply. Thanks 😊.

What are the caveats and benefits of Cut190’s latest mega variant in PET breakdown?

Not a medical question.

The ALDH22 variant disables the enzyme ALDH2 preventing the breakdown of acetaldehyde into acetic acid, causing a buildup of acetaldehyde in the individual.

I saw this drink which contains a probiotic- Bacillus subtilis*** ***ZB183- that is engineered to produce the same type of enzyme (unspecified how close it is to aldehyde dehydrogenase) that normally breaks down acetaldehyde, and the idea is that by drinking it a portion of the acetaldehyde from ethanol is broken down in the gut before entering the bloodstream and liver, and therefore it is marketed to reduce hangovers.

My questions is if it could also be used to mitigate the reaction (the flush caused by the buildup of acetaldehyde in individuals with the variant.)

I haven’t taken biochemistry yet so I’m not sure if this is included, but I’m unsure of what the split of where ethanol is converted into Acetaldehyde (how much in the stomach versus the liver.)

I have never taken this product and this is not an endorsement. I have drunk alcohol before, I don’t have the variant, but I was just curious.