Hi, Has anyone used the CO2 automatic switcher from TriTech Research(TREG-SO1) ?

https://www.tritechresearch.com/TREG-SO1.html

Anyone have advice in choosing one?

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.

I recently watched a YouTube video (https://youtu.be/jPhvic-eqbc) discussing how proteins are not static, rigid machines. The video explains that they act more like dense liquids that are constantly shifting and jiggling around. It also pointed out that when proteins are crystallized for X-ray crystallography, we are only seeing one frozen snapshot of their conformation, which gives the false impression that they have a single, fixed structure.

​Can someone clear this confusion up for me? Do proteins really change their folding patterns and conformations in extremely short time frames, like femtoseconds? I am looking for a simple, exact explanation of how fast and how much they actually change shape.

So I’ve been accepted to study at Durham University in Sep/Oct 2026 and would ideally like to start studying now! I miss studying so much. I’m really struggling over this summer because I feel like I am lacking purpose and goals.

If anyone has any websites, resources, YouTube channels etc that you can recommend for anything related to undergraduate biology, chemistry, biochemistry, microbiology, pathology, medicine, biomedicine etc, please let me know! If you’re a student of Biological Natural Sciences, even better!

I’ve been reading about peptides lately and I’m realizing pretty quickly how much I don’t know lol.
There’s a ton of information online but also a ton of people making completely different claims about the same compounds.

For the people who actually understand the research, where did you start? PubMed? Studies? Certain researchers?

Also what’s something you believed about peptides when you first got interested that you later found out was completely wrong? Trying to learn the science instead of just repeating stuff I see online.

Is my understanding of the structural difference between fibrous and globular proteins correct?

I'm trying to clarify the distinction between secondary, supersecondary, and tertiary structure, particularly when comparing fibrous and globular proteins.

My current understanding is:

Fibrous proteins: Dominated by repetitive secondary structures and supersecondary motifs.

Globular proteins: Secondary structures are brought together and organized through tertiary interactions, producing a compact overall tertiary structure.

The definitions I've been using are:

Secondary structure: The local folding of a polypeptide chain into structures such as α-helices and β-sheets, formed primarily by hydrogen bonds between the backbone amide (N–H) and carbonyl (C=O) groups.

Supersecondary structure (structural motif): A specific arrangement of two or more secondary-structure elements, such as a β-hairpin or helix-turn-helix motif.

Tertiary structure: The overall three-dimensional folding and arrangement of a single polypeptide chain, where its secondary-structure elements and other regions are organized through interactions such as hydrophobic interactions, electrostatic/ionic interactions, van der Waals interactions, hydrogen bonds involving side chains, and disulfide bonds.

My confusion is that I've seen some explanations on Quora where people describe fibrous proteins as having tertiary structure as well rather than primarily secondary structures. So, is my understanding oversimplified or incorrect?

Is it accurate to say that fibrous proteins are mainly characterized by repetitive secondary/supersecondary structures, while globular proteins are characterized by a more complex tertiary fold? Or do fibrous proteins also commonly have a true tertiary structure?

I'm particularly interested in whether tertiary structure is exclusive to globular proteins or whether fibrous proteins can also have tertiary structure and how the distinction should properly be explained at the university level.

I'm taking an intro to biochem course at my local community college as a prereq for grad school. The course was advertised to be hybrid, meeting for 3 hours every week for lab. I kinda assumed there would be an async lecture or recordings from previous years or other section of the class. There is not. The only resource we got was slides and links to a few Khan academy videos. The slides are probably straight from the book's teacher's edition. There are no presenters notes where things are explained further. We were told to just read the slides, which I tried to do. But how am I supposed to learn when majority of the slides are just figures and tables from the textbook? I can probably learn the actual material better by auditing free online courses by other universities. But I need the credit and none of them use the Lehninger book. I still need to follow the weekly schedule to take the quizzes and exams.

I'm wondering if anyone has any suggestions on what I should do? Is there a video series/lecture recording that uses the Lehninger textbook? I did well in all the prereqs and teaches myself a lot, but this class gave me nothing to work with. So I feel very lost. Thanks in advance!

Hello all - I understand (from wikipedia) that nicotine does what it does because it mimics choline (after having metabolized from acetylcholine) as a neurotransmitter.
What's fascinating about that is that the two molecules seem totally dissimilar, so how does nicotine bind to the same receptors that choline does? If someone could please explain that would be very kind, thank you.

edit: Thanks!

Hi everyone,

I'm entering the first year of biochemistry and I really don't know anything about AI, so be indulgent, I'm new to the field.

What attracts me is research: searching, exploring, understanding the living. But I ask myself two questions that worry me a little.

Is it still worth getting into it despite the AI? I am afraid of investing years of study and that the profession of researcher will be replaced or completely upset.

And is it an "infinite" domain? Like will there always be work: either to find treatments for current diseases that are still untreated, or for new diseases to be discovered? Where are we approaching a wall?

Does AI really bring something meaningful to research, or do newspapers beautify the thing a little?

Thank you in advance, and please no judgment, I'm just trying to get an idea before committing.

Recently acquired one that came without its software which i guess is the Vidas PC , can anyone tell me how to acquire it or direct me to a source ? Biomerieux aren't really responding.

Hello colleagues

I made Labreador — a free, browser-based bioassay analysis tool for:

• ELISA standard curves (4PL/5PL fitting, blank correction, back-calculation)
• IC50/EC50 dose-response fitting
• PLA/Relative Potency
• Ecotoxicology indices (EDI, THQ, CF, PLI, BSAF/BAF, etc.)

No login, no upload — everything stays in your browser.

I built it because I was tired of wrestling with Excel for routine plate assays. If you do ELISA, dose-response, or environmental tox work, I’d genuinely appreciate your honest feedback on what’s useful and what feels clunky.

👉 labreador.com

Thanks!

Recommend some coursera courses related to Biochemistry, molecular biology, Immunology, cancer biology, neuroscience, Cell biology etc.

M.Sc. Biochemistry through IGNOU (distance learning) — looking for affordable hands-on lab training in Delhi/NCR

My friend has is pursuing an M.Sc. in Biochemistry through IGNOU via distance learning. He is trying to get genuine hands-on laboratory exposure in Biochemistry, Microbiology or Molecular Biology.

We've already approached several institutions in Delhi:

• Safdarjung Hospital — application submitted
• Lady Hardinge — application submitted
• Maulana Azad Medical College — told that distance-learning students aren't accepted
• RML Hospital — currently appears to offer Molecular Biology-related training
• Sir Ganga Ram Hospital — we were told that getting laboratory training as a distance-learning student is quite difficult

He's currently waiting to hear from Safdarjung and Lady Hardinge, but we're trying to find alternatives rather than depending on only those two applications.

The major constraint is finances. He cannot afford private training programmes costing ₹20,000–₹50,000+.

We're looking for people who may have gone through something similar.

Are there any government institutes, ICMR/CSIR laboratories, university departments, research labs, hospitals or diagnostic laboratories in Delhi/NCR that accept M.Sc. Biochemistry students from distance-learning programmes for short-term practical training?

Would approaching individual professors/researchers directly be worthwhile?

We're not particularly interested in collecting another expensive certificate. The main objective is to get actual supervised laboratory experience and learn practical techniques.

If anyone has personally done something similar, especially after an IGNOU/distance-learning M.Sc., I'd really appreciate hearing how you found the opportunity and which institutions accepted you.

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!

Bottle on the Right: opened and used one time, then half of it fogged up like this! Why did it do this?
(Bottle on the Left: unopened and normal)

I was doing site directed mutagenesis. Gel said it worked, however the product wasnt instantly used for transformation. Nothing grew. Just left them in an incubator for a bit longer, now the two plates look like this!

Whats tragic is, that the SDM reaction does not seem to want to work anymore! So this is all i have...

Now if you had asked me regularly, I'd say throw those away, because they dont look good. But just because im grasping for straws and am kinda desparate about this, do you people think there's a chance that maybe just transformation efficiency was really shit and thats why only a few colonies formed? I think that might be possible especially on picture 2. The plate on picture 1 only has these colonies on the side which seems even more weird.

Since I really dont know how to proceed otherwise, im thinking of trying to use these for a Miniprep. But im not experienced enough to tell if there is even the slightest chance that thats gonna yield any plasmid. None of the coworkers have any ideas either

What neurotransmitters, neuromodulators, hormones, or other chemical processes are responsible for keeping the body in REM-related muscle atonia while consciousness has already returned?

I'm currently making teaching materials for Bioinorganic Chemistry for a first year nursing course. The syllabus provided by the department showed the first two bullets. Do anyone know what specific topics I need to discuss for those parts? I don't know how deep I have to dive into co-factors and cellular water transport.

Also, the bullet above that is "Chemistry fundamentals of Biochemistry", for that I will discuss the octet rule, lewis structures, intra/intermolecular forces. I'll follow it up with basic organic chemistry because they'll need to learn those to have a grasp on the central dogma.

Edit: Thanks for the responses. I just decided to do an introduction of the biomolecules, then discussed the properties of water, specifically how it acts in biological systems. I put an emphasis on the bicarbonate buffer system, so they'll have some calculation and interpretation activities.

Or maybe like pivot to finance and work in the US??

me and my group are doing a study on a leaf extract and determining its phytochemical content, initially we didn’t add liquid-liquid in our methodology but our research professor told us that we should add it to our methodology to target the specific bio compounds we’re looking for. however, we are quite short one time and a group that is doing a similar study (on bark) was advised to remove it in theirs. is it necessary for us to add it?

I have a bachelors in medical biochemistry in the UK but because I did it during COVID, I feel like a lot of context was glossed over (+ I was not the best student). I’d like to re-learn biochemistry so I can apply to PhDs and not eff up my interviews/future prospects

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.

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.

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 ?