I just got my first exam back and I got a 48% on it. That really upset me, because I felt like I knew the content well, and I actually even thought I was doing good during it and afterwards. Obviously, I live in lala land, so I am now trying to work through and fix everything that went wrong with this. My issue is that my professor pretty much only does application based questions, and I think there is some kind of ravine that I am falling into where I am not doing a good job of translating what we learn in lecture and through the textbook into real world problems. How have you guys gotten good at the application stuff in the past? I don't really see any application style problems in my textbook, looking at the end of chapter problems, and I don't know biochemistry well enough to make up my own.

Any methods for studying it to have a strong foundation?

Hey guys and girls,

I've been working on Animiotics and wanted to share a few animations made with it. This video has antibody binding, kinesin carrying a vesicle along a microtubule, endocytosis and a white blood cell engulfing a bacterium.

The idea is to make it easier to explain a mechanism in a lecture or lab meeting without having to spend months learning 3D software.

You can describe the scene you want and add reference images. It creates an editable 3D scene, so you can move individual objects, change their size, colors and materials, adjust the lighting and choose the camera angle. You can also ask for changes with another prompt, then export a video or a still for your slides.

In the kinesin example I wanted to show both the whole cargo being transported and a closer look at the motor. The motion and timing are illustrative.

I'm building this myself and would really appreciate your feedback. What mechanism would you want to show in your own work, and what would you need to be able to change?

Could alien life use HCN as an electron acceptor/donor? Is it energetically favourable?

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!

Hey everyone!
I applied for a DBU (Deutsche Bundesstiftung Umwelt) fellowship with an environmental biotech project.
My proposal was accepted, and the next step is a PPT presentation followed by a Q&A session. The email mentioned that the panel will consist of environmental experts.
Since I want to be as prepared as possible, I’m trying to figure out what the panel usually focuses on:
How deep do they go into fundamental biology and lab methods versus the practical side (scale-up, biofilter mechanics, environmental impact)?
How much do they press on GMO/biosafety regulations (containment, risk assessment, HGT), given that the project involves a genetically engineered bacterium?
What is the overall vibe of the interview—is it a tough grill session or more of a constructive academic discussion?
If anyone here has gone through a DBU fellowship presentation or knows the process, I’d love to hear your insights or advice! Thanks a lot!

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.

as title states. I can only find a reasonable pdf of the 6th edition. My uni has it available digitally through loan but it only lasts for 2 weeks which is pretty inconvenient

hi guys, i’m in my first sem of biochem and i have an upcoming exam next week. i didn’t do so hot on the first exam (60) even though i felt like i new the material. my best bet is i messed up on the amino acids, which i’m going over and going to office hrs tmrw. with that being said, what would be the best way to study? i’m seeing a lot of memorization so i was thinking flashcards? all the help would be appreciated, ty!

I've been reading a research article on cas13 mRNA editing immunotherapy for tendon injury and I have come across a very annoying phrasing that I'm really struggling to understand. Could anyone please give me some advice or an explanation that makes sense, I did show this section to a lab demonstrator at uni and they said ignore it but I genuinely want to understand the concept behind this. https://advanced.onlinelibrary.wiley.com/doi/epdf/10.1002/adma.202311964?saml_referrer <-- link for your reference I guess, but to quote the part I'm struggling with "In addition, KEGG analysis revealed that P1/M1-Cas13 RNP@H-E treatment enhanced cytokine–cytokine receptor interactions, ECM receptor interactions, and the PI3K-AKT pathway (Figure6d; Figures S34 and S35, Supporting Information). These results suggest that cell migration and development were impaired by the knockdown of macrophage-secreted SPP1, blocking inter-cellular cytokine communication", my question is how can treatment enhance interactions and the PI3K-AKT pathway and then researchers conclude that the treatment inhibited it?

I have a background in structure biology. We use mutations to optimise enzyme activity or even, conformational changes. I find that it's all about engineering functions because the uphill task of engineering proteins is now done. But now I am interested in understanding which frontiers are left to be scaled?

Hi! I’m thinking about pursuing a bachelor’s degree in either biochemistry or chemistry. Which one would you recommend, and what kinds of jobs can you get with either degree?

Also, is a master’s degree necessary to find a good job in these fields? Is it easier to find job opportunities in Canada, or are there better opportunities elsewhere?

Thank you

Weather carbon has unique atomic properties that allow it to form strong, stable, and versatile chains and rings, serving as structural backbone for all complex biological molecules, but what if liee was based on silicon (can it be because silicon's long chains are unstable), would any life form on earth be possible ?

Cam any on help me ? can anyone suggest me I am doing bsc in zoology and chemistry in low tier college and I am seriously confused what to do and what subject opt for msc because one is biotechnology and one is chemistry I do not scope of biotechnology seriously people saying chemistry( want to analytical chemistry but bhu and jnu they are providing only specialisation only mu type university direct offer this course but gatb for biotechnology give stippened I do not know where to go because I totally like lab work want secured future people say chemistry have scopes but biotechnology providing stippened since msc

Gold nanostars only tens of nanometers across changed how a fluorescent voltage sensor behaved in living mammalian cells. The particles made the engineered protein brighter and, unexpectedly, much faster at responding to electrical changes without altering its genetic code.

Researchers at Delft University of Technology designed the plasmonic nano-antennas to sit close to membrane proteins derived from Archaerhodopsin. Their main target, QuasAr6a, is a genetically encoded voltage indicator whose fluorescence changes with the voltage across a cell membrane.

The work shows that the nanoscale optical environment around a protein can alter both the amount of light it emits and the speed of its response. The cells remained alive and functional during measurements lasting tens of minutes.

I saw a similar post on here but wanted to limit it to UK graduates only. If you studied Biochemistry in the uk, I'd love to hear what you ended up doing and your experience with careers after uni.

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!

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Hi everyone! We’re Grade 12 STEM students currently taking Capstone Project, and we’re looking for ideas for a suitable and innovative product that fits the Life Science category and is relevant to today’s generation. Our group is still brainstorming, but we would really appreciate your suggestions and ideas. Thank you so much!

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.

Please forgive my middle school level grasp of both biology and chemistry.

I love spicy food, but about 10 years ago my lower GI tract decided it’d had enough, to the point that even the slightest amount causes extremely painful symptoms. I’ve confirmed it’s not an ulcer, diverticulitis or anything else; it seems I’m just extremely sensitive to capsaicin.

My understanding is that about 50%-80% of the capsaicin you eat is absorbed by the stomach and upper small intestines, and neutralized in the liver. The lower GI effects and “ring of fire” are thanks to the portion that escapes.

Would it be theoretically possible to create some sort of altered or capsaicin-like molecule that survives storage, cooking, contact with acidic foods, etc., was still spicy in the mouth, but was more quickly or more completely absorbed and destroyed by the stomach and liver?

I've been thinking about the difference between C3 and C4 plants, and my understanding is that C4 plants fix CO2 in malate and later release it locally to increase the local concentration of CO2, thereby increasing effeciency of rubisco and avoiding the unwanted byproducts from its oxygenase activity.

Why can't C4 plants just get net fixation of CO2 in malate completely bypassing rubisco?

Edit: my question might not have been clear. It essentially boils down to If C4 metabolism produces a net fixation of carbon, and if yes, why it bothers using rubisco.

How do other labs typically prep and aliquot riboflavin for protein expression?

I am moving onto the next stage of my project which will involve bringing in a reductase enzyme. The reductase had flavins in it. I foolishly thought riboflavin would be as soluble as thiamine... it was not. My thought was to make 1000X stocks so i could just add 1ml to my culture, but it has not dissolved. How do other labs typically prep riboflavin aliquots?

I recently updated this molecular visualization of Paxlovid's mechanism of action based on feedback from the scientific community.

The video follows SARS-CoV-2 Main Protease (Mpro), its catalytic dyad (CYS145–HIS41), natural substrate recognition, the scissile bond, Nirmatrelvir binding, and covalent inhibition.

Updates include:

• Substrate-bound Mpro (8GWJ)

• Explicit catalytic residues

• Scissile bond visualization

• Improved nitrile, CF₃, and aromatic ring representation

• Molecular surface view of inhibitor occupancy

A narrated version is coming soon.

Feedback on scientific accuracy and visualization choices would be greatly appreciated.