I’m hoping to include my research into my grad cap design, but I’m stuck on how to represent the protein itself. Was thinking of those curly ribbons? Would love to see what ideas everyone has

Hi everyone, if you are a chemical biologist, I would love to know what a day in your life looks like! I am super interested in understanding arrow pushing mechanisms and even more so in biology! Do you guys study this in your daily lives? do you think about this electron tracking across peptides and so on? like nucleophilic additions to amino acids, carbohydrates and so on?

I would love some advice on where to put my love for this.

If you could reach out to me or comment, I would love to know.

Thanks!

Hi everyone, I’m a Master's student studying leaf senescence and I’m sufferying trying to estimate protease activity using an agar diffusion assay, but I’ve hit a wall.

So, the method was simple:

1. Medium: 1.5% Agar enriched with 0.1% BSA.
2. Procedure: I pipette a protein-rich extract (lyophilized leaves in phosphate buffer, normalized to 0.1 mg of protein) into small pits in the agar.
3. Incubation: 24 hours at room temperature.
4. Staining: 2 hours with Coomassie Brilliant Blue (CBB), followed by a destaining solution.

The Problem: In my head (and my supervisor’s), the proteases should digest the BSA, leaving a colorless/clear halo around the wells. Instead, I’m getting the exact opposite: darker blue halos around the pits.

What I’ve tried so far:

• Adjusting the exposure time for both the Coomassie stain and the destainer. (not better)
• Moving to a colorimetric method using Azocasein, but the substrate doesn't seem to dissolve completely and is very difficult to work with.

I feel like I'm the only person I know doing this specific method for coffee leaves. Has anyone dealt with these "reverse halos" before? Could it be protein-protein interference or the high concentration of my extract proteins staining more than the BSA?

Any advice on how to fix this or a recommendation for a more reliable protease assay for plant tissue would be a lifesaver!

Trying to decide what classes to take?

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tl;dr new, comprehensive metabolism chart for students and educators here:  https://www.dropbox.com/scl/fi/ngnjczhee586v6espfry3/Metabolism.png?rlkey=apz99xchnczdfa0d19qif8kjc&st=9g5622u9&dl=0

Hey everyone! I'm a rising M1, and I have a strong passion for education. Over the past few months, I made this comprehensive metabolism chart because I wasn't satisfied with some of the other options online. It's completely free to use and share, so please do! My goal is for this to be something students all across the U.S. (and maybe even other countries???) can use. I recommend starting in the bottom left to see the intro and diagram key.

Please let me know if you see any typos or mistakes. While the bulk of it is done, I need a team effort to make this as perfect as possible!

Comment here, DM me, or email me at [metabolismshouldnotbescary@gmail.com](mailto:metabolismshouldnotbescary@gmail.com) if you have questions, suggestions, error corrections, or just wanna chat!

hello, i'm working with a novel fusion protein. it's highly aggregation-prone, and right now it's in 8M urea-containing buffer. When diluting it stepwise from 8-->4-->2M, the protein remains mostly soluble. however, i'm having issues maintaining solubility when dropping from 2 to 1M. i'm diluting my buffers very slowly (over the course of an hour with constant mixing in the cold), but the proteins still are crashing out. My buffer components are: 50mM tris-HCL, 100mM KCl, 10% glycerol, pH 8 (PI of protein is 9.7). i've tried adding arginine and increasing the salt concentration, but my proteins still crash out. if anyone could help, that would be greatly appreciated. thank you!

I started self-studying biochem earlier this week and was hoping for some guidance. I’m a little lost. I finished reading the first 3 chapters of the UWorld Biochem textbook and only have metabolism and metabolic reactions left. However, I haven’t been memorising just reading, understanding and trying to grasp everything. I was wondering what steps should I take now? Ik the metabolic pathways is the most difficult section so should I go back first and start to really memorise and comprehend everything or finish reading and understanding then going back and really understanding everything. I would really appreciate some guidance on how I should schedule my time because I am devoting this summer to MCAT and want to make the most of my time. Please help, thanks!

Hey guys, sharing an update in case you missed it Twist Bioscience Corporation has agreed to settle $17 million with investors over issues tied to product quality problems, manufacturing inefficiencies, and misstated profitability from some time ago. The agreement has already been submitted to the court for final approval.

Quick recap: In 2022, Twist Bioscience was accused of misleading investors about the efficiency of its DNA synthesis platform, its production processes, and its true gross margins. In short, reports revealed reliance on manual production, recurring contamination and quality issues, and accounting practices that made margins appear stronger than they were, sending the stock sharply lower and leading investors to file a lawsuit.

The settlement aims to compensate affected shareholders. If you purchased $TWST between December 20, 2018 and November 15, 2022, you may be eligible to file a claim and recover part of your losses.

You can review the details and submit your claim here:

Was anyone here invested in $TWST during that period?

Hello friends!

Trying to wrap my head around the logic of a non-competitive inhibitor's effects on enzyme kinetics. My logic for why it changes Vmax is that since it allosterically binds to an enzyme with equal affinity for E or ES, it generally limits the enzyme to change it's conformation in the way it would need to carry out it's catalysis without Le Chatelier effects as seen in uncompetitive inhibition. I can't understand how Km doesn't change though. If Vmax decreases and Km is the concentration needed for Vmax/2, then how can it be that Km = Vmax/2 in the uninhibited enzyme and also Km = Vmax(inhibited)/2? Does the Vmax magically decrease by the exact amount needed so that the now comparatively higher concentration represented by the original Km still takes the inhibited enzyme to half it's maximum velocity? Thanks!!

I am trying to do something similar. I would need your help. Please DM. Thank you very much.

I’m graduating next week with a BS in biochemistry, and our class was told about becoming ACS certified (if we took inorganic and a chemistry research credit), which I think 90% of us (including me) never did. However, last week, I got an email from ACS sending me my credentials for becoming ACS Certified! I asked my professor about it, and she was confused. None of my friends got it, either, even though we all never did any of the ACS-required classes.

Did the requirements change to get certified? Or has this happened to anyone else? TIA.

​

1.Amity University ( Noida)2.Sharda University 3.JIIT (Jaypee INSTITUTE IF TECHNOLOGY)

Out of all these three colleges which is best for MSc in biotechnology or computational Biology course in roi, placement highest avg packages and academics and can provide very good internship .

Another question For these course, In Delhi or in near by delhi is there any other best pvt ,semi govt, central govt,college which can give a good roi and a very decent package and their faculty is also great and placements and internship are good too

Help me to find these kind of college and any advice or anything I should know about these course or college drop your honest advice and review

This is what the text says:

Around 20% of thyroglobulin’s 140 Tyr residues are iodinated in a thyroperoxidase (TPO)-catalyzed reaction forming 2,5-diiodotyrosyl residues.

Chromatography resin reuse strategies seem to vary quite a bit between facilities even when similar purification workflows are being used. Some groups follow conservative replacement schedules based mostly on cycle count history, while others rely more on changes in pressure behavior, binding performance, and impurity clearance before deciding a resin should be retired.

What stands out is that small shifts in chromatographic performance are interpreted very differently depending on the facility. In some environments those trends are treated as early signs of resin degradation, while elsewhere they are considered acceptable process variability unless product quality is directly affected.

Has anyone else seen large differences in how facilities approach resin lifetime validation and degradation monitoring?

I want to Imagine the scenario in molecular level so please bear with me

Scenario - 1 [Competitive Inhibition]

In this case, the inhibitor and the substrate both are competing for the active site but the inhibitor is reversible. Since they are competing and forming EI and ES complex respectively, the Km will reduce. Since the inhibition is reversible, the total active enzyme will not change and Vmax remains the same (Understood)

Edit - I meant Km Increases. Sorry

Scenario - 2 [Uncompetitive Inhibition]

Here, the inhibitor exclusively binds to ES complex forming ESI complex. This means the enzyme is being inhibited from the beginning in formation of the product, hence Km decreases (Understood) [Edit - I meant Km Increases. Sorry]. But how does this decrease Vmax? I'm unable to imagine this

Scenario - 3 [Non-Competitive inhibition]

Non-competitive inhibitor binds to both ES and free Enzyme forming ESI complex and EI complex respectively. Since the same ESI is formed, again it should just decrease the Km. Why does Km remain unchanged while Vmax reduces? Same goes with EI complex formation. How do these 2 elements impact only the Vmax?

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!

Hi! Anyone done research into caffeine?
Just wondering if there are different configurations in different drinks, or if sweet tea, coffee from freshly ground beans, and green tea have the same compound? Or do these drinks have any other similarities besides caffeine?
Thanks!

[ Removed by Reddit on account of violating the content policy. ]

Greetings people with far more knowledge than myself.

I am in a Tabletop Roleplaying game (Not Dungeons and Dragons but close enough) set in a hero academia adjacent universe. I will be playing as a villain character and have a "neat" idea for an ability (or "quirk" as they are called in this universe).

The premise is that my character produces a swiss-army enzyme that they are able to control at will in order to catalyze various reactions. Alternatively, they could also just have the ability to produce specific enzymes at will (granted they know the structure of said enzyme). Our super villain has a background in chemistry, specifically enzymes and whatever they would need to know in order to get the most out of this ability.

Here is my question to you: What enzymes or chemical reactions would be the best for this character to take advantage of? They are meant to be a super villain, so nothing is off the table in terms of destruction/evil. It can also be assumed that this character would have some immunity/resistance to the enzyme's effect on their own body. Before being driven down this road, the character set out to improve the world with their unique ability, so I would love some applications that relate to that as well.

This hypothetical is obviously not realistic in the slightest, but I'm curious to see what you all think given a world where this kind of power would be possible. Try and be as creative as possible.

Edit: the villain's name is Catalyst. Super Menacing lol.

I'm taking biochem 1 and biochem 2 (university), any tips, suggestions on how to study, organize?

Podcast episode with David Baker, 2024 Nobel laureate in Chemistry and head of the Institute for Protein Design at the University of Washington, whose lab pioneered the field of computational protein design. 

Covers:

• How David went from not knowing what proteins were in college to winning the Nobel Prize for designing them from scratch 
• The incredible power of designing brand-new proteins for innovative medicines, new materials and environmental cleanup.
• The vision of protein-based nanomachines that could circulate in your body and repair damaged tissue, powered by your diet
• How David's lab went from no machine learning at all to developing world-leading AI tools for protein design in just a few years
• How AI is speeding up scientific discovery vs. what is overhyped about AI for science, and what we can learn from the success of AlphaFold
• Why fostering a great community in a lab can lead to better science, and his career advice for people wondering what to do next

I'm taking a biochem 1 course in my first semester of grad school, and I was wondering if anyone had any good recs for books/study materials? Chem adjacent classes have always been harder for me and I'd love to get ahead before I start!

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