r/Biochemistry

I am a Biology student aiming for a career in biosynthesis of high-value products (not sure exactly which yet). To be competitive in applying for a relevant MRes, I need to 'catch up' with the most relevant skills that a Biochem BSc would have taught me. So, please could people who have recently completed a Biochem BSc let me know if you learnt how to:

1. prep samples for mass spec

2. choose the appropriate method of mass spec and machine configurations for your sample

3. interpret the mass spectrum

If you could also let me know whether you learnt to use spectrophotometry to characterise a molecule via its absorbance properties (using spectral data- peak shapes, wavelength Maxima, how abs changes with conc) that would be really helpful.

Thank you!!!

Hello! I'm a senior high school student from the Philippines helping fellow high school researchers who are currently developing their research projects.

We're looking to connect with professionals, graduate students, researchers, or faculty members who may be willing to answer occasional questions or provide guidance related to the following fields:

• Biochemistry
• Biotechnology
• Materials Science
• Nanochemistry / Nanomedicine / Nanotechnology
• Pharmacology
• Phytochemistry

We're also looking for individuals experienced in:

• Molecular Docking / In Silico Methods
• Diabetes Research

We're not asking for anyone to do the research—only hoping to build connections with people who might be willing to share their expertise or point students in the right direction when needed.

If you're interested or know someone who might be, I'd really appreciate it if you could leave a comment or send me a private message.

Thank you so much!

Tell me your crazy stories while you were studying biochemistry.

It can be either while you already graduated or still studying

His 1982 experiment single-handedly proved the function and universality of telomeres, along with predicting the existence of the enzyme. It was perhaps the decisive moment that catapulted the whole era of telomeres, anti aging therapy, and a new era of biology.

Third year biochem student here and man, some days I walk into lab and wonder how I even got this far. Like last Tuesday I spent 45 minutes trying to figure out why my gel wasn't running, only to realize I forgot to plug in the power supply. Meanwhile the sophomore next to me is casually explaining protein folding pathways like she's reading a grocery list.

I know the material when I'm studying alone. I can walk through metabolic pathways on my whiteboard at 2am no problem. But put me in a study group or have a professor ask me something on the spot and my brain just empties out. Then I stumble through some half answer while everyone nods along politely.

My advisor keeps telling me my grades are solid and I'm right where I should be, but I can't shake this feeling that I tricked everyone somehow. That any day now someone's gonna tap me on the shoulder and be like "hey so we reviewed your file and yeah, there's been a mistake."

The weird thing is I actually love this stuff. Give me a messy research paper and I'll happily spend my Saturday decoding it. I just feel like I'm playing catch-up while everyone else has some secret manual I never got.

Anyone else dealing with this? How do you get out of your own head when the doubt kicks in?

We have published a preprint titled “Evolutionary shifts in spike glycan-binding specificity suggest a possible association with host adaptation during SARS-CoV-2 Omicron evolution” .

does anyone have any recs on a good laptop that can preferably last me all 4 years? i am not getting a macbook thats for sure, but ive seen raves about windows and lenovo.

im mainly looking for performance/compatibility with software, durability, and long lasting battery life

please suggest me some, thanks :)

Science has a history of favoring specific groups of people. In 1977, Dr. Louise Chow's EM studies were instrumental in the discovery of RNA splicing. Yet in 1993, she was excluded from the Nobel Prize for the discovery. Despite this, she continued to change science. Her work with HPV unlocked mysterious of the cancer causing virus and helped influence vaccine and treatments.

While the Nobel committee may have overlooked her, the Titans of Virology and Vaccinology Podcast was lucky enough to get to hear her story. Like many great women in science, it is time for her moment.

I’m trying to understand how researchers actually track new papers in biochemistry and related fields. PubMed alerts, Google Scholar alerts, journal TOCs, Twitter/X, lab Slack, manual searches — I’m curious what people really use.

A few questions:

1. How do you currently find new papers worth reading?
2. What is the most annoying part of that workflow?
3. Would it help if a tool ranked new papers by relevance to your research topic and explained why each paper is included or excluded?
4. What would make such a tool genuinely useful rather than just another alert system?

I’m not trying to promote anything here — mainly doing user research for a literature-monitoring workflow. Would appreciate honest opinions, especially from grad students, postdocs, and researchers who regularly track papers.

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.

Been reading some papers lately about mirror life and getting bit confused. Scientists keep making these mirrored amino acids and proteins in lab, and every paper comes with warnings from big names in field saying we should stop. But they never explain properly what exactly could go wrong. I understand basic concept, mirrored bacteria might behave differently than normal ones, maybe become uncontrollable.

But I keep wondering couple things:

If we make mirror bacteria, can it even survive outside? Normal bacteria evolved to use specific substrates for metabolism, mirror version would need everything flipped too. Where would it find mirror nutrients in real world? Seems like it would just starve immediately.

And what about immune system? Adaptive immunity recognizes foreign patterns and destroys them through oxidative burst. Would mirror bacteria somehow bypass this? Maybe innate response is too slow to catch them initially?

I find this topic fascinating because there seems to be actual scientific value here, mirror proteins help with crystallography studies and other structural work. Question is where we draw the line. Anyone working in this area who can explain the real risks? Not just "it's dangerous" but actual mechanism of what could happen.

Hello, for some background I am an undergrad who had a single summer internship in a lab focusing mainly on protein purification, and was asked back for a hired summer position this year. My mentor is a post-doc who is slumped with work for a manuscript and I do almost all the manual work for purification. Generally I just follow protocol, but we started a new project with a new batch of proteases.

Currently, our lysing process is not working as it should be. We create our lysis buffer and then manual lyse via sonication, but the solution remains pretty opaque, and when clarifying the lysate, the pellet is much bigger than we want. Ni-NTA Chromatography and running a coomassie gel confirms most of the protein is stuck in the pellet. 

It’s possible that the protein is just insoluble or whatever else, but I’m really not sure. Our project is robust so my mentor is encouraging me just to move on and we’ll revisit, but it’s happened twice now and I’d like to help. Any ideas on how to optimize lysis would be helpful. 

For our current process: We are working with proteases and the current lysis buffer consists of 20mM Tris buffer, 100mM NaCl, 5% glycerol, 5mM BME. - We also induce secondary culture at 0.6-0.8OD with 1M IPTG and leave overnight at 18 degrees celsius. Idk if any of that helps. If more info is needed to help, please lmk!

Pthalocyanine was the first large organic molecule to incorporate the heavy atom method, which was the first true solution to the phase problem. This was later used to find the structure of penicillin. I’m interested to know how derivative of the method of finding the structure of penicillin was of the method of finding the structure of pthalocyanine, because I’m interested in seeing how the technique evolved, and also how much impact I should lay at the feet of this original 1935 experiment.

I take all of these substances on a semi-daily basis and I wanted to share my supplement intake.

Hope:

This one uses CAP-1/CapPER delivery system to inject nutrients into central biomass.

2 whole pan fried ghost peppers

1000mg fish oil delta

1 gram full protein like the chicken protein powder

80 MG amylase coq-6a

400 MG Coq-10

Green tea extract 1 gram

Coconut baby oil - 2 tablespoons

Algae extract 100 mg

Aloe Vera 10 ML

Black or earl Grey tea 1 emptied teabag

4 tablespoons fine grade coffee like Stumptown

Glucosamine Chondroitin 40 MG

Fizzle:

Bitter Orange Isopropylnorsynephrine 400 mcg

Moruga Scorpion Pepper Flakes - 1/4 Tsp

Black Pepper - 1 tsp

Royal honey - 1 tsp

Pomegranate juice 40 ml

Pureed Blueberry - handful

Pureed Strawberry - Handful

Orange Juice 40 ML

Bromelain - 100 MG

CBD Oil - 1 tsp

Magnesium 100 MG

MSG Sodium 40 MG

Wheatgrass pureed handful of stalks

Papaya - 1 fruit pureed

Starfruit - 2 fruit pureed

Banana - 1 pureed

Wolverine:

Calcium Citrate - 400 MG

Aloe Vera mixed with zinc 100 MG

Fish Oil 1000 mg

Blue Agave syrup - 2 tablespoons

Iron supplement - 1 dose

All Vitamin supplement

Collagen Type I II & III - Full dose

Beef Bone Broth - 1 serving

Pork Rind - 3 Tablespoons

Turmeric -1 tsp

Yew Root Extract - half teaspoon

Paprika - 3 teaspoons

Ghee - 1 teaspoon

Owl :

100 mcg ghost pepper Capsacin

1 tea spoon ground cacao nib

10 MG Zinc

100 MG Green Tea Extract

Banana Pear and Peach extract 1 gram

Riboflavin 400 MG

60 MG Magnesium

Mountain Laurel Flower petal extract 4 MG

Kava Root 100 mcg

Morning Glory petal extract - thimble full

Coconut oil 1 tablespoon

Animal Pak whole complex

Average multivitamin like Centrum

L-Tryptophan 1 gram

L-Valine 1 gram

5-HTP 1 dose

CBD Oil 1 teaspoon

Pink Brain:

500MG 5-HTP crushed and ground

400MG Sodium Chloride

40MG Oxaloacetate

10MG Folic Acid

1 Tablespoon MCT Oil C-8 only

4 Melted Haribo Gummy Bears or equivalent pure glucose syrup

2 tablespoons gelatin

Type I II & III animal or vegetable collagen

Sunflower Extract - 100 MG

Dandelion Extract - 100 MG

Beta Carotene 100 MG plus 4 teaspoons Carrot Juice

Ostarine - Soak Whole lemons in isopropyl alcohol, wait for extraction, then torch alcohol and burn off. Crystallize with Sodium Chloride, Potassium Sorbate, Magnesium Citrate and BhB Salts 100 mg

Cardarine. Same process as lemons, same salts.

Ligandrol - Simmered Duck and Goose Fat mixed with plum, pear, peach, apricot, Acai, Zinc, brazil nuts and pecans. Strain through cheese cloth and re-low flame simmer the extract, then consume.

Bind all three Ostarine Cardarine and Ligandrol with 40 MG zinc sodium solution and that's called Cat.

Meater - enhances meat consumption, allows for easier digestion, and promotes lifespan and satiety

3 tablespoons crushed pork rinds

1 tablespoon powdered bone broth

1 tablespoon Ghee

1 scoop of type I II & III Collagen

Fish Oil taken at same time

Kava root 100 MG

Shitake Mushroom ground up - 1 tablespoon

Magnanese - 40 MG

Pureed sticky rice - 2 tablespoons

1 gram pureed fresh edible Algae

1 gram chicken meat protein powder

Rosentide -

1 Gram ground ostrich egg shell

1 gram algae chlorophyll extract

How do I say, basically some amount of Soylent protein. Half the bottle

10 grams chicken protein powder

1 gram chicken egg shells

1 egg scrambled

2 eggs egg whites

Sodium potassium magnesium

BCAA 10 gram

Zinc Antioxidant Pomegranate Acai Blueberry Complex

10 MG Raspberry Ketones

Exogenous Ketone powder 1 tablespoon

Tawny Moon is

10 MG Beta-Alanine

35 MG Citrulline Malate

5 Grams Creatine

40 MG Taurine

100 MG Carnitine

BCAA Isoleucine Lysine Leucine 10 Grams

Histidione

Magnesium

Aloe Vera

Cocoa Powder

Molecular docking is typically performed between a ligand and a protein. Is it possible to perform molecular docking between two ligands instead?

Background first so you know where this is coming from, I'm not in the field at all, I just read a lot and got stuck on something I can't find addressed anywhere. Happy to be told it's already solved.

The proteins that won't classify cleanly no matter how much data you throw at them, the intrinsically disordered ones. The ones that just won't settle.

My question is whether we're looking at the final shape or the path that got it there.

Because if two proteins end up at roughly the same final structure but got there through different folding sequences, the internal contact points would be different. Parts of the chain that are far apart in sequence but end up sitting next to each other in the finished fold, those bridges only exist because of the specific path it took. Different path, different bridges, even if the outside looks similar.

So my question is basically: are those hidden contact points being tracked and compared between the disordered cases and the ones that resolve cleanly? Because if the disordered ones are arriving at their weird ambiguous state via a different pathway, maybe the bridge pattern is the variable nobody's looking at yet.

Probably already accounted for somewhere and I just haven't found it. What am I missing?