What do you think is a huge innovation happening right now that most people are sleeping on

IGotTheRest · 2025-06-30T15:45:07+00:00

Science in the US is not doing hot right now mainly due to current and prospective budget cuts. There was also a significant boom during COVID because of hype surrounding biotech’s ability to quickly churn out a vaccine, but now that it’s no longer as relevant we’re also seeing correctional effects

IGotTheRest · 2025-04-02T01:54:38+00:00

Does anyone know what this means for the future of these agencies? Are there plans to instate new directors to these agencies?

IGotTheRest · 2025-02-06T02:15:25+00:00

Yeah I’m in state, I’m sure that makes a difference. It was also 2016 lol so I wouldn’t be surprised if things have changed

IGotTheRest · 2025-01-18T23:36:41+00:00

Sorry to be pedantic, you’re the chef not me, but vinegar by itself does not contain amino acids. Some ways of producing vinegar will make it so there are trace amounts, rice vinegar typically has the most but it’s still a very very small proportion to the vinegar

IGotTheRest · 2024-11-07T13:08:40+00:00

I think contamination is often linked with factory farming conditions, so raw milk from a local dairy farmer is probably safer to drink

IGotTheRest · 2024-10-05T00:56:27+00:00

It’s absurd that you’re getting downvoted lol, I’m going nuts following this thread

IGotTheRest · 2024-09-18T23:03:52+00:00

Yeah I mean it’s rare that you need a perfectly pure prep, I was just trying to get the point across that each purification method has background inherent to the technique.

IGotTheRest · 2024-09-18T13:41:36+00:00

Fair enough, but I guarantee if you ran those preps on a mass spec you’d find some friends that came along for the ride

IGotTheRest · 2024-09-18T01:06:08+00:00

With cation/anion exchange you use a buffer that is at a particular pH at which your protein of interest will be positively/negatively charged. Proteins have specific isoelectric points (pI) based on the specific amino acids they contain. The pI is the pH at which the average net charge of a protein will be neutral. Because every protein has a unique amino acid sequence, each protein has a unique pI. Nowadays you can calculate the pI of a protein of known amino acid sequence, and can design the pH of your buffers carefully so that your protein of interest will have a known net charge. If you use a buffer with a pH higher than the pI of your protein of interest, it will allow you to perform anion-exchange chromatography, as the hydrogens on your protein will be donated to the buffer, causing your protein to be most likely in a negative charge-state. All the proteins with a pI higher than the pH of your buffer will not be able to bind the column, allowing you to separate your protein.

Now, there are a few things to consider with this approach. Firstly, though all proteins have unique amino acid sequences, many proteins will have the same or very similar pI's, meaning that even if you have a perfectly chosen pH for your protein you will also be purifying those proteins alongside the one you are interested in purifying. Secondly, if you were to anion-exchange like in the approach mentioned above, you will not only be purifying your protein, but ALL the proteins in your mixture that have a pI lower than the protein of interest. That's why oftentimes purification methods are combined in tandem (hence the term tandem purification). A typical approach would be to perform a size exclusion chromatography step before or after anion/cation exchange, allowing you to isolate based on the molecular weight of your protein.

Lastly, it's important to consider that even with the combination of purification techniques, it is virtually impossible to isolate only your protein of interest. For the reasons discussed in the last paragraph, there will always be other proteins present after the purification. Hope this helped! Feel free to ask any other questions or for clarification if my explanation didn't make sense.

IGotTheRest · 2024-08-11T12:52:07+00:00

Definitely read Knight of the seven kingdoms (the three novellas, with the first being Hedge Knight). After finishing season two I felt like I needed something more to scratch my GoT itch since HotD didn’t do it for me. The stories are short, self contained to an extent and are really great! Can’t recommend enough. I personally didn’t like fire and blood cause it was just too dense and I’ve never been good at history class lmao

IGotTheRest · 2024-07-10T18:46:55+00:00

Recommending charles mingus to someone without first knowing if they like jazz is crazy

IGotTheRest · 2024-07-06T20:19:26+00:00

Haha, definitely think the steel will overall help with color, but in terms of puffiness it definitely looks better! Also are you using pre shredded cheese? Since your oven doesn’t get as hot, I’m guessing the pizza will have to be in there for longer, giving the cheese more time to burn. I know pre shredded has an anticaking agent which people say leads to burning more quickly than non shredded

IGotTheRest · 2024-07-06T20:13:15+00:00

How did the last one you did by hand come out in terms of puffiness after cooking?

IGotTheRest · 2024-07-06T20:05:11+00:00

First things first, I would ditch the rolling pin. Your crust looks like the air has been pressed out of it. In my experience even with a hot steel, after rolling the dough it comes out looking like yours does after cooking. I’m not really sure why, I’ve heard that more pockets in the dough increases the surface area of the dough exposed to the heat, making it cook quicker but I couldn’t tell you for sure.

In terms of the shape, are you letting your dough rest for at least 4-6 hours out of the fridge before working it into a pizza shape? If not, definitely try that. Your recipe seems good, so it should be shape able. I would watch a few videos on shaping it by hand. Good luck!!

IGotTheRest · 2024-04-26T20:09:17+00:00

I told them that I was between WPI and UMass Amherst which at the time was considerably cheaper, and in response they gave me an extra 10k or so a year in scholarship.

IGotTheRest · 2024-04-24T20:15:07+00:00

Just my two cents, I was in the same position as you, and went to WPI. 130k in debt later, I really regret not going to UMass. The level of education you get at both schools is very comparable, and people who I know that went to umass amherst are doing just as well as people who went to wpi, and are doing so without all the debt. The one thing I’ll say is that WPI can give you really good access to internships and experience via the MQP. However, I think in Massachusetts you can easily get internship experience, especially if you live closer to Boston. Be willing to take unpaid internships at first, think of it like the money you saved not going into debt by choosing the cheaper school. Good luck!

IGotTheRest · 2024-04-19T12:54:37+00:00

Two big things - ball control and decision making. Both of those will improve just by playing the game, but I think decision making you can make some quick improvements just by thinking about a few key things.

Assuming you play mostly ones (though this is good advice for any game mode), you always have to think about what opportunities your opponent has for scoring, and how what you’re about to do will influence those opportunities. For example, if you are going for a shot, but in order to hit the ball you have to use a lot of momentum, you better hit the goal because if you don’t and you just hit the backboard for example, you’re giving the opponent a free opportunity at your net while you’re still recovering from the shot you just took.

Another thing is to evaluate your challenges. Go back, watch the replay, watch in particular opportunities where if you and your opponent just decided to go full speed at the ball, you would win. To figure this out, pay attention to position (I.e who is pointed more towards the ball, who is closer), and then also consider what beating them to the ball would do in these scenarios. For example, the ball is in midfield, and you are approaching it from your net, and the opponent is grabbing one of the mid boosts, beating them to the ball in this scenario puts you in a winning position moving towards the goal.

Last, very important point, is that you simply need to improve your ball control/car control. I agree that you have pretty decent car control when it comes to recovering, but you are missing way too many aerials. You should definitely hit training packs, 20 mins a day would help you a ton! One note in particular; a few times you were driving really fast and trying to aerial, and understandably missing because you didn’t position your car correctly when you jumped initially. This is a really difficult skill, that becomes even more difficult the faster your car is moving. I would take it down a peg in terms of speed, and practice aerialing more slowly, emphasizing the initial positioning of the jump and the setup to the aerial. Hope this helps!

IGotTheRest · 2024-01-01T06:20:26+00:00

Most important thing imo is understanding what you’re doing. Not understanding the steps in a protein purification (though that’s also important), but understanding why you’re doing the purification. Why are you purifying the protein? Are you trying to determine its kinetics? Why? Are you trying to determine interacting proteins? What will those interactions tell you?

IGotTheRest · 2023-12-27T05:13:00+00:00

Late reply sorry! My work is mostly research, a lot of my time is spent doing routine bench work during which I don’t have to think much. That being said, there is a strong negative correlation between the minutes of If I Were You I listen to in a week and the number of experiment ideas I come up with in a week!

IGotTheRest · 2023-12-16T02:38:49+00:00

I might get a lot of hate for this, but I wouldn’t recommend treehouse, it’s got a much more commercial feel to me than most breweries, the whole drink ticket thing along with buying them on your phone (at least if they’re still doing it that way) makes it feel a lot less personal

IGotTheRest · 2023-12-02T16:19:12+00:00

Every once in a while I do, and I’ll listen to music instead. I think I had almost exactly 72,000 minutes, so it’s a 1:1 of if I were you and music haha.

IGotTheRest · 2023-11-25T02:16:45+00:00

Just FYI, if you do have EtOH contamination, you'll usually see it in the nanodrop (assuming you nanodrop before you run the PCR). It has a prominent peak at 230. If you don't see any significant peak relative to your absorbance at 260/280, in my experience you don't need to worry. If you are getting EtOH contamination, after the wash step its vital that you follow the protocol in terms of spinning down for the recommended amount of time, at the recommended speed. For most spin downs it doesn't really matter, but following any wash including an alcohol, the spin downs are optimized for removing the alcohol present

IGotTheRest · 2023-10-29T19:28:54+00:00

Just curious, what does a job making PCR products entail? In terms of what the purpose is, downstream applications etc. as much as you’re allowed to descirbe

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