Oct. 9th, 2013 04:13 pm
tanarill: (Science!)
Today was shit. Mostly it was that I could not get to sleep last night, so I was running around on probably not more than six hours of sleep. I have learned that if I take the two sleeping pills as recommended, they will work as advertised. I was hesitant because I didn't want to be groggy in the morning, but I'm groggy anyway from not sleeping. In the future, I will RTFM.

Seminar: This is yesterday's seminar, from a German researcher named Otto. He works with a protein called "Mx," which is a protein that most lab mice don't have. The ones who do have it are much more immune to influenza, by which I mean when you deliberately inject the flu into mice, the ones without Mx die in a week and the ones with Mx just shrug it off.

Humans have two Mx-like proteins, called MxA and MxB. Otto works on MxA, and did a lot of experiments in petri dishes and the by making transgenic mice (mice which have human MxA instead of their normal Mx) and testing their immunities. What he has found is that MxA is really very active against viruses that attack other species. Or, in other words, only viruses that have evolved to be "invisible" to MxA can attack humans. He proved this by showing that both the 1918 pandemic strain of flu and the 2009 pandemic H1N1 strain of flu had the same mutations, those apparently being the mutations a flu virus has to make to become MxA-invisible. Then they were able to cross the species gap from pigs/birds to humans, and cause a pandemic.

This might seem like a failure, but actually it is very good. A virus generation is a few hours long. In the ninety-one years between 1918 and 2009, viruses had time for 265,720 generations, and they only successfully made the species jump . . . twice. So it seems that Mx, and proteins like it, form a very high barrier for viruses to become human-infectious. It protects us from getting sick constantly because of bets like cats and dogs and cockatrices. Once viruses are human-infectious, Mx is kind of useless.

Also, teaching friend Max to be learn chemistry. I learned this in my senior year of high school, during AP chem, so it has been six years. Still, I seem to have retained it fairly well. I've got him setting the problems up correctly, at least, so hopefully he'll be able to do it well on the test. It is good to be able to help.


Jul. 8th, 2013 08:16 pm
tanarill: (Science!)
So I successfully deplated the silver. I no longer have a mirrored Erlynmeyer flask, boo. Also, I discovered why we hate silver staining so much: not that it is not functionally better than the blue, but that cleaning up after it is a pain in the ass.

Now I am trying to see if my bacteria that grow after induction are doing so by mutating, and also if media makes a difference. So there is that.

An unrelated thing that happened that I didn't mention on this blog because I had fallen off the planet: there was an earthquake. This happened about a month ago, but the point was I had never been in an earthquake so it was a new and interesting experience. Also not scary. I mean, if it were more violent (it was only a 4.7) I can see how it would be, but I literally went, 'grumble stupid earthquake waking me up grumble' and turned over to sleep for another hour or so. I kind of liked it, actually. Score for geology! :D
tanarill: (Science!)
So, do you guys remember that one time I gold plated my magnetic stir bar? Today, I managed to duplicate the feat . . . in silver. So obviously the next thing to do is do it again in bronze, and then I can have a full set.

Actually, it wasn't just the stir-bar. Today I was doing silver staining, which is what you do when you have so little protein that the standard blue dye won't work. The thing is, at the end you have a solution full of silver and a slow-release reducing agent. This causes the silver to plate itself out on basically anything involved, and it will continue to do so for a couple of days. So in addition to a silver-plated magnetic stir-bar, I have a silver-plated glass stirring rod, a silver-plated protein staining bath, and a silver-plated erlynmeyer flask. The glass ones are particularly interesting, because glass + silver coating = mirror. I can see my reflection in them.

I will try deplating everything on Friday. It will involve strong acid. I can't do it now because strong acid + organic solvent (like is in the staining solution) = explosion. I have to wait until all the silver exits solution, pour off the solution, and then try with the strong acid. Wish me luck :D
tanarill: (Default)
After the Endeavour, it was time for Cleopatra, Queen of De Nile. Actually, aside from that thing where her religion said she was the mortal avatar of the goddess Isis, she seemed actually to have been pretty realistic in her views. She just took a big gamble in the whole war of succession following Caesar's death, and unfortunately she gambled on the wrong side.

History Lesson )
tanarill: (Science!)
This actually happened on the Friday after Thanksgiving, but I have been lazy and not posted about it. So now I am posting about it.

On that Friday, my family went in to LA, to go to the Science Center. It is interesting because it is a whole complex of museums, centered around a common, underground parking structure. We only visited the science museum, but it would take quite a lot of time to go through all of them. Perhaps I will go back and go to the cultural museum, which looked interesting, or the natural history museum, which I have no doubt takes advantage of LA's La Brea tar pits to get dead post-dinosaur pre-human things.

Anyway. We got tickets to two exhibits: the space shuttle Endeavour, and the Cleopatra exhibit. It was in that order, and if I had the day to do again I'd give myself more than an hour between the two, because the Endeavour definitely deserved more time.

Endeavour )

So that was the Endeavour. If you happen to be in this part of the world, or a different part of the world that also has a retired shuttle, I high recommend you go see it. It's worth it.

Just give yourself a whole lot longer than an hour.
tanarill: (Science!)
So this week I was debating going to seminar, because the email said it was about salmonella and metals and I am not terribly interested in infections bacteria-based disease. But then I went because I had to be on that side of campus anyway, and I am so glad I did.

Guts Under Here )
tanarill: (Science!)
These are actually quite common in molecular biology. They are used because often reactions don't produce a conveniently colored product, so they are not easily measurable. Thus, we add steps. Usually, we try to keep the number of steps down, though, because more complexity means more things that can go wrong.

Reaction I: A + B -> C + D, in the presence of enzyme 1
Reaction II: C + E -> F + G, in the presence of enzyme 2

A, B, C, D, E, F, enzyme 1, and enzyme 2 are all colorless. If you only had A, B, and 1, there would be no way to tell that a reaction is occurring. By adding E and enzyme 2 to your tube, you create a condition where enzyme 1 working allows enzyme 2 to work and make color. Since color cannot happen without the reaction I, you can now track it. This is a basic schema for a coupled reaction.

This is the current plan in my research as well. We have an A, B, C, D, E, G, 1, and 2 that are clear. Actually, so is F in the visible range. It is colorful in the UV range, which we poor humans can't see but our machine can, so as far as we are concerned, it is "colorful enough."

Next problem: We don't have any enzyme 2. We can't buy it because nobody makes it. We shall have to request some enzyme-2-making-cells from a lab that studies it, and extract the enzyme ourselves.

Let's do this thing!


May. 23rd, 2012 10:18 am
tanarill: (Science!)
Today is the forty-sixth day of the Omer, which is six weeks and four days into the Omer.

Operons )
tanarill: (Science!)
Today is the forty-fifth day of the Omer, which is six weeks and three days into the Omer. Cheesecake holiday begins Saturday night :D

A conversation I had.
Brett and I: [talking]
Me: [notices] Oh, my aglet is gone.
Brett: [ . . . ] Your what?
Me: The little plastic part at the end of shoelaces.
Brett: I only believe this is a word because it is you telling me.
Me: As it should be. [continued conversation as I begin digging through my backpack]
Brett: [disturbed] What are you looking for?
Me: Ah-hah! [hauls out a couple of shoelaces I'd put in one of the many, many backpack-pockets] I thought I had some shoelaces in here somewhere!
Brett: [ . . . ] Yes, along with your can opener.

I do, in fact, carry around a can opener. This has proven useful in the past.

A different ting was last week's Thursday Seminar, which was about a bacteria called Wolbachia (Wob). Wob is symbiotic with insects, but in a weird way: if a female has Wob symbionts, they will be in her eggs and her babies will also have Wob, but a male will not have Wob in his sperm. From the point of view of a Wob, it is a good thing to make sure your female hosts have wide, egg-bearing thoraxes, but your male hosts you don't care about. So Wob actively helps females, whereas in males it only doesn't hurt them.

Wob helps by killing any harmful bacteria living in the insect host, and also some viruses. (For reasons not discussed here, viruses that infect bacteria are Very Different from viruses that infect insects, and therefore the Wob are not in danger from the viruses they are killing.) What this means in practical terms is that if a mosquito that is carrying, say, dengue fever, becomes infected with Wob, it is no longer a carrier of dengue. This does not work for blood-born worms, like malaria, but there is a trial in Australia going with Wob mosquitoes and mosquitoes with a bacteria that is the surrogate "disease" and they are tracking the "disease" mosquito die-off.

So, in summary: more bacteria, fewer deadly disease. Weird how Science! works out, isn't it?


May. 14th, 2012 05:22 pm
tanarill: (Default)
Today is the thirty-seventh day of the Omer, which is five weeks and two days into the Omer.

My roommates are such enablers. To whit:

Me: And then I will use Lulu's toaster to toast the bread, and I will steal some butter, and I will have buttered toast.
Liz: Here's the butter! [passing it over]

Such. Enablers.

In other news, Science! is hard. This was the message at seminar last week; and although I had not thought about it before, it is very true. Evolution has made us into beings that can unconsciously observe, make incredibly fast decisions based on those observations, and most of the time, not get eaten by the tiger. Science requires that we wait until we have all the data to make decisions - which in turn, requires that we know what 'all the data' even means. Scientific thought is difficult, counter-intuitive, not easily within the realm of human understanding.

And so teachers do students who object to, say, Newton's First Law a huge disservice when they act like it ought to be easy. Anyone can see that if you throw a ball it falls down and then it stops; but the First says that in fact it ought to keep moving in the same direction and at the same speed - except that on earth we have things like gravity and friction to deal with. It took a genius (certifiable, but still a genius) to realize that the natural state is not lazy stillness, but inertia. Because Science! is hard.

The rest of the seminar was about how to teach children science! despite the fact that to our common-sense world, the idea of things like relativity and atoms and even germs are really, really weird. It was a good seminar.

tanarill: (Default)
Today is the twenty-seventh day of the Omer, which is two weeks and six days into the Omer.

1. Meat. Meaty meat meat. Which, as a unit of currency, the Hillel house Wins at.

You probably had to be there.

2. I had orange juice in the fridge. I did. And now I have . . . fizzy alcoholic orange juice in the fridge.

. . . so I can't grow bacteria I want, but I can get booze. Okay, this isn't so bad. XD

3. My professor spoke of his friends, Randolf and Ross. They were not only identical twins, but also personality twins. To the point that, at one point, he simply did not notice that Ross was not Randolf for some time. He called them "duplicate plates," because he is an awesome nerd.


Apr. 24th, 2012 11:03 am
tanarill: (Science!)
As you may or may not know, I spend my days in a lab, trying to make bacteria do things that they do not do naturally, like express GHB-dehydrogenase. (This is not entirely true. Bacteria make a protein that does the same thing, but we want to study the human version, so we have to get them to make said human version.) This is generally done in three steps:

1. Get the gene into the bacteria.
2. Grow the bacteria up, selecting for ones that have the gene we want.
3. Express the gene.

Step 1 involves a small ring of DNA, called a plasmid. These are natural, in that bacteria have plasmids, and when they do bacteria-sex it is usually plasmids that they pass around. Plasmids contain "accessory" genes - that is, genes that they might need right now but may not need later, and for this reason the plasmids are separate from the main genome, and can be tossed easily. The artificial plasmids that we make contain five things: the gene that codes the protein we want the baceria to make; an operon, which is like a DNA on/off swith so we can tell them when to make said protein; a promoter region; and origin-of-replication, so they can copy the plasmid each time they divide; and an antibiotic resistance gene. We do a thing that gets the plasmid into the bacteria, and we really have no idea how this works, but then the bacteria have plasmid.

Why, you might ask, is there an antibiotic resistance gene on the plasmid? For Step 2. See, when we but plasmid->bacteria, there is a lot less plasmid than there are cells, and so not every cell gets plasmid. We don't want to grow up cells without plasmid, so we grow the bacteria on a plate with the antibiotic inside. Only the ones that got the plasmid can live; all the other, useless cells die. This also promotes the cells to make plasmid; if there is no reason to keep it, they will just stop copying it. Surviving with an antibiotic is a good reason to keep the plasmid, and also the gene we want.

So I put plasmid->bacteria yesterday, and spread them out on plates with the ampicillin antibiotic. If my process did not work at all, I get no colonies; if it worked too well, or my sample is somehow contaminated, the whole plate is bacteria. If I did it right, I get a plate with single colonies dotted all over, and none of them are touching. This is what I got, so I am successful \o/

Today, I made liquid medium cultures. It is just like the stuff that I use for plates, only without the agar-agar so it does not gel up. I also added antibiotic so the bacteria keep the plasmid. For each culture, which is 5 mL in a test tube, I picked one colony. This is because each colony is from a single cell, and so if any colonies are the result of a bacteria figuring out antibiotic resistance on their own, only that colony will be affected. (This is also why we don't like colonies to touch.) These test tubes are growing in the 37C room. This step is mostly to grow lots of plasmid-bearing bacteria, which I will need for the next step.

Step 3 involves operons, which I will explain at a different time.

But, overall, this is good. In the past I have either gotten no colonies or too many. So I am very happy and excited that this time, I did it just right :D
tanarill: (Default)
Today is the twelfth day of the Omer, which is one week and five days into the Omer.

Hopeful Science Back Here )

New Term

Apr. 17th, 2012 10:56 pm
tanarill: (Default)
I have sadly neglected you, the people who follow my journal. This is bad, because wonderful Things have happened.

1. It is no longer That Holiday. It is, in fact, the eleventh day of the Omer, which is one week and four days into the Omer.

2. My schedule has worked out such that I get to go home on all the weekends. Last weekend, it was kind of drizzly Friday like we get only rarely in California, and then it cleared up a little, and I saw a rainbow. :D

3. Today, I was given a plant. The internets told me that the greenhouses (which apparently we have) were doing an open-house. So I went, and got a tour of their rare orchids, and on the way out they gave me a plant. I was going to refuse, being as I kill plants, but the options were cacti, which survive without water, and milkweed, which has weed in the name. I took the milkweed, because butterflies.

4. I went to a seminar. I shall not explain, save to say that it's a new approach to drug design. A wild and crazy wacko approach, but one which seems to get previously-impossible results. So there is that.

5. The one about the AIDS. I'll explain later.

6. Bees! On lupins!

. . . And many other interesting biogeek Things.


Another One

Apr. 4th, 2012 11:49 am
tanarill: (Science!)
All right, enough of That Holiday for a bit. Time for some Science! Or rather, another argument against intelligent design.

In most nerve cells, signals are transmitted as follows: The cell membrane has in it two proteins, the sodium ion pump (we will call this P) and the sodium ion channel (we will call this H). P use ATP to push Na+ out of the cell, and they work all the time. H open to let Na+ into the cell, but only when they receive a signal to do so. H can be signaled by a small molecule, like epinephrine or acetylcholine, or by other Na+ ions. So if the H at the synapse see some epinephrine, they open up, thus allowing Na+ in to the cell. The H a little further down see N+, and also open up, which trigger the H even further on. This is called the "depolarization wave," as it proceeds linearly down a nerve cell. Once the wave was passed, the P quickly pump all the Na+ out again to reset the system.

And it makes sense, right, that if the your hot-sensing nerve sees something hot, it sets off the depolarization wave, and sends a signal. This is how most senses work.

Except for vision. Instead, they have an arrangement of NOT signals, whereby there is a light-sensing cell, and immediately behind it, a cell that constantly tries to send signal. The light-sensing cell is always telling the one behind it to shut up, unless, of course, it sees light. Then the exact opposite of a typical signal happens: rather than opening H, they are closed, a signal is not sent to the next cell to be quiet, and the depolarization wave is started. Why? We have no idea!

It is (say it with me now) Yet Another Argument Against Intelligent Design.


Mar. 21st, 2012 08:51 pm
tanarill: (Default)
I fell off the intarwebz again.


1. I went home for the weekend, and the power went out. We had a wind storm, which presumably knocked down the power line. So instead of Oven Pizza Saturday, we had Sushi Saturday, followed by "sit in the dark and tell stories to each other by candlelight" night. It was not bad. Not something I would do for tremendous amounts of fun, but not too bad.

2. I have been to Science! seminars. Today the one was the one where they made every possible single point mutation it is possible to make in the gene for a protein called ubiquitin. (It is everywhere in every cell. The scientists at the time thought this made a good name.) Then they studied the fitness, by which we mean the ability of the organism to survive long enough to make more of itself. They used yeast, because twenty yeast generations takes about two days.

What they found was that out of the mutations that don't immediately kill the yeasts, there are some as good as not-mutated ubiquitin, but there are not any that are better. To which the obvious response is, duh. Do we think us scientists with out fancy-shmancy labs and our directed evolution can come up with anything better than Nature has in billions of years? It might not be an intelligent designer, but it has been tinkering for longer than our genus has existed. So the real conclusion that the lecturer made was that even the ones that, to us, look "as good" probably do have some not-as-helpful-as-the-not-mutated-kind effects, which only show up on timescales longer than two days.

3. I have been trying to make almost-but-not-quite dead cells, which are the kind which are too sick to notice when you add a few bits of DNA into them. These are E. coli cells, so it is kind of amusing that I am making the bugs sick. So far, it has not worked. Wah.

4. I got a rotation for next term! I will work on gamma-hyrdoxy-butyrate, possibly better known as the "date rape drug". For such a horrible drug, it turns out that very nearly no research has been done on how it affects our brains. It was only last year that a quick-test sensor (developed by my prof) was put into production. So now we can tell it's there, at least. Huzzah.

5. Passover in two weeks. I hate that [censored] holiday.

6. It is finals week. I am ded.

Now I go to fall off the internets again. Bye bye!
tanarill: (Science!)
Seminar yesterday was a researcher talking about his work on TRP channels (pronounced "trip"). These allow calcium (II) ions through membranes in response to certain signals. In neural cells, this sets of the depolarization wave that is how you think, so obviously is is very important.

The scientist was using fruit flies as a model, because messing with fruit fly genes is not ferociously unethical and gives a better idea of how these things work. They turn out to be involved in sensing, sending the signals to the brain that say, "there is green light" or "this thing is hot." It turns out that they are a two-part system. The first part responds to toxic things, tells the flies to avoid them, and does not ever change. The second part responds to non-toxic things, and can be changed. We think this is why poisonous things always taste bad but things like stinky cheese and natto can be delicacies.

The other thing is diseases that happen when TRP channels do not work. A lot of them are embryonic lethal - the animal dies very early in development. But some of them cause problems that Mom can take care of, so the baby is fine until they are born. This is the case with mucolipidosis type IV, a horrible disease which prevents lysosomes from working properly. They usually digest broken cell-bits, but when they cannot, the broken bits keep producing poison, eventually bursting the lysosome and killing the cell. Worse, the dead cell spreads the poison to all the cells next door, which also die and spread their poisons, and so on. So when people are born with this, their clock is ticking so quickly that they cannot even learn to speak, because they don't have enough of that type of brain cell left to learn when they get to that age.

So! As with many human proteins, there is a mouse analog which does the same thing and is related evolutionarily. We creepy sciency people found this analog and turned it off, thus successfully giving the mice mucolipidosis type IV. Then we began prodding at the mice to see what we can learn.

What we learned was thusly: you can only fully reverse the disease by turning the gene back on. But you can mostly reverse it by giving the mouse a few hundred phagocytes, which are cells that wander around looking for cells displaying "I am about to die!" signals and then eating them and degrading them. In the disease mice, of course, their phagocytes stop at the degrading them step like every other cell in their bodies, so it is no good using their cells. Phagocytes, though, are a type of white blood cell - meaning that giving the mice a simple white blood cell transfusion from a compatible mouse is able to significantly rescue them.

In people, this would be impractical, of course. The patient would need to have a constant supply of said cells, since mature white blood cells only live about nine hours. We have endless supplies of donor mice and we can quickly breed more, so it is not a problem for them; but finding a compatible human donor willing to be constantly having their blood sucked . . . However, you can give the sick mice a supply of donor bone marrow, which will produce enough healthy phagocytes to keep them healthy, at least for nine months. (After the nine months, the thing we did to kill all of the disease mouse's own bone marrow so it would accept the new marrow tends to kill the mice. Bummer.)

In humans, of course, the science of killing people's bone marrow and replacing it is well known and cures cancer. Now, apparently, it will also cure another deadly thing for which there is, otherwise, no effective cure.

tanarill: (Science!)
So, if you were designing an assembly line, you would logically make it so that process 1, which turns A->B, and process 2, which turns B->C, are fairly close together. If you are really good, B emerges from machine 1 right in the hopper for machine 2, like those cookie-making plants where the dough comes out of the mixer right into the cookie press. If you are the kind of person who is good at scheduling, you also make it so that all the things needed arrive where they're needed at about the same time, so instead of massive warehouses full of stuff waiting to go on the assembly line, you only need modest storage areas right at the unloading docks. In real life, there is a job, called "Industrial Designer," for the person who makes sure that plants and airports are built so everything can arrive right as it is needed, and nothing ever has to travel very far or wait very long*.

In many cells, this is sort of how it works. The DNA is transcribed into mRNA in the nucleus, and the ribosomes are waiting just outside to begin work. The endoplasmic reticulum is right there, actually physically connected to the nuclear envelope. Just outside that is the Golgi body, which does a lot of the post-translational modifications that are needed to make the protein work. All other things being equal, this is a very efficient protein-making assembly line.

Except. Neural cells can be as long as three feet (although they are long and skinny), and proteins that are needed way out at the tips are not needed near the center. So evolution designed a thing which waits until a ribosome is on an mRNA, then shouts "PAUSE!" and drags it out the edge. When that protein is needed, it can be made right there.

In theory.

In practice, the protein still needs post-translational modifications. Which means that the cell ships the mRNA-ribosome out to the ass-end of nowhere, makes a protein, ships the protein back to get modified, and then ships it out again to where it needs to be. How does this make sense? I don't know!

It is (say it with me now) Yet Another Argument Against Intelligent Design.

* Although airports tend to get clogged by bureaucracy, a good one can still have a plane off the ground every fourteen seconds during the busiest hours.
tanarill: (Science!)
Today, I began the third week-long shortcourse; this one is on translational machinery. And also, there was a quite fantastic thing to show how there is no intelligent creator.

The basis of the thing is in tRNAs. These shuttle amino acids along and allow the ribosomes to place a specific one into a growing protein. It recognizes which tRNA it needs using codon-anticodon complimentarity with the mRNA. So far, so simple.

But a three-base codon give sixty-four possible combinations. Even if you use use four of them to say STOP, that's still three times the number of needed codons. So some amino acids have more than one codon. This does not work out to three per amino acid, though; some have four and some have two. The reason is because it allows the third base pair to be "wobbly;" what is there does not matter quite as much as that it is always a purine (A or G) or a pyrimidine (U or C). This wobbly is good, since it means that if the ribosome makes a mistake matching the tRNA, it is less likely to affect the protein.

Then there is the strange case of Isoleucine and Methionine. Methionine is the amino acid that is always the one at the beginning of the protein - the Met codon is also the symbol for "begin!" It is AUG. AUX, where X is A, T, or C, means isoleucine instead. This means that the the ribosome absolutely cannot make a mistake in finding AUG versus AUX, or the protein doesn't start right.

Fortunately, there is the sugar inosine, which we show with I. I is a weird sugar, in that it can pair with A or T or U, but never G. It is made from A by a fairly simple reaction, and it is in fact how the body breaks down adenosine to become uric acid. So an intelligent designer would go, "Ah, the tRNA for isoleucine will have the anticodon TGI, and be able to pair with any AUX that is not AUG." And in fact when I was asked this in class today, this was my answer. It was a good answer, and my teacher went, "Huh. I like that." Is this how it actually works, though?

Of course not.

Instead, biology does the very strange thing of modifying the last base of the Met anticodon, so that instead of being TGC it becomes TG(k2)C. This somehow prevents the ribosome from ever putting the wrong tRNA in there, though mechanisms currently unknown. It is expensive, because instead of using a protein that already hangs around to digest A, there has to be another protein that does the C->(k2)C modification. It is inelegant. It reeks of a quick cludge to fix a problem after the fact.

It is, in short, another argument against intelligent design.


Feb. 17th, 2012 09:36 pm
tanarill: (Default)
More about tunicates in FNS today.

Apparently, if two botrylluses are living next to each other, and grow so that they touch each other, they can do one of two things. Either they will reject each other and continue to live next to each other as two organisms, or they can accept each other, thus fusing their tunics and sharing hearts, blood supplies, and genetic information. Like I said, these are weird.

The presenter today was talking about how this recognition occurs. In humans, we have a thing called a Major Immunohistocompatability Complex (MHC). There are lots of genes for these, and people who don't have two copies of the same gene are better at fighting off disease; this is one reason that inbreeding is bad. MHCs also help our immune system to tell if any given cell belongs to us, so they can attack foreign cells. Blood does not have these so much, but for organ transplants, matching MHCs are a big deal unless you want transplant rejection.

In botrylluses, they have things calle FuHC, which serves very much the same purpose. Apparently, if two touching botrylluses share one gene for a FuHC (they have two, just like us), they will fuse. Otherwise, they will reject. This process is mediated by proteins known as Fester and Uncle Fester, and he is trying to figure out how it works. It is not going well, mostly because they are not soluble proteins, which makes working with them very difficult indeed. So it was kind of a null bottom line, but interesting in background and the technical details of what they did.

Anyway, that was this week's interesting Seminar.