Why You Gotta Be a Fool? Don't You Know I'm Human Too

Wow, a lot has happened this week. Although I got rejected from my "reach" schools, I still have quite a few options for colleges. I'm having a tough time deciding what to do. I wish I could see into the future, but I suppose life is more fun when it's surprising.

Anyways, it's amazing how much can change in a few weeks - and how much stays the same. I'm glad to be back in the lab, actually doing something. (As an added bonus, it keeps my mind from over-stressing about college decisions.) But, early Monday morning, still groggy from getting up at 4am, I walked into the lab hallway to be greeted with a sign. You know it's a Monday when you see this:

How, exactly, you can close a hallway, I'll never know.

I didn't want to walk through that hallway, anyways. Thanks for asking.

I tried to make more liposomes on Monday, but in hindsight, I should've just waited. I spent at least an hour preparing my lipids and M2 proteins, and everything was going fine. I was even told that we got more internal buffer (it was running out before I left. I actually thought we weren't going to have any when I returned). Unfortunately, somebody didn't put the red tape back onto the internal buffer.

So I may or may not have put 1M NaOH into my lipids instead of internal buffer. Whoops. (I'm sorry, liposomes. I failed you.) How can such a small change of tape color make such a difference.... (I know, I know, I should've read the label on the bottle, but I wasn't expecting it to change.) At least this mistake shows that I am, indeed, human.

I was also told that we had three working pH meters now. Sadly, I ended up doing my tests - or at least trying to do them - on April Fool's day. I feel like the world wanted to prank me, so, naturally, all three pH meters weren't working. I mean, I know computers don't like me, but can't pH meters at least tolerate me? (Is that too much to ask for?) So Wednesday was spent trying to make them less noisy and less drifty, with moderate success.

On the bright side, some of the pranks I saw were highly amusing. Especially this one.

Notice how there are posters and even a lamp.

What are the handrails doing in an office, you might ask. This "office" is actually an elevator, and the teacher spent his day greeting unsuspecting students as if they had all come to his office hours. (I suppose that's one way to get a higher turn-up for office hours....)

On Thursday, only one pH meter was working (I really shouldn't be surprised), which meant it was a long day. One of the pH meters had almost no noise, and I was excited to use it. It wasn't meant to be, however. I discovered that if I leaned on the table, the two new pH meters would exhibit "artifacts," basically spikes in the pH readings that are not from pH changes in the solution. I thought I was onto something important, until my uncle informed me that this effect was common in pH meters.

Basically, my body was acting as magnetic field, which interfered with the voltage readings from the pH meters. To solve this, we have to ground ourselves, or the pH meters. (One solution involved me wearing a metal bracelet, which was strapped to some kind of "ground." I felt like I was chained to my experiment....) I don't think we've found a permanent solution yet, but I hope that we're on our way. It's odd that only the new pH meters are affected by my proximity. (Such is new technology, I suppose.)

Speaking of new technology, when I was gone, my lab decided to update the Windows 2000 computer, which is the computer that records all the pH changes. This lab must be allergic to new technology or something, because apparently the new program crashed, and brought down the program I used with it. Thankfully, we had another similar - and older - program that I now use.

Don't worry, though - this means that the Computer Says game just became more interesting! Only now, the correct information isn't even displayed on the computer; I had it written in my lab notebook somewhere.... The computer beeps one sometimes, usually before it thinks I'm supposed to do something, then kindly beeps three times ten seconds later. I think I'm becoming more adept at ignoring the beeps. (And this is coming from someone who rushes to get everything out of the fridge before the fridge beeps as a reminder that it's been left open.)

In other news, my results from testing AK40 again were inconclusive. Sometimes, it seemed like I had drug, and sometimes the drug was suspiciously absent. I suppose I should've seen this one coming; the drug was hard to get into solution. My mentor thinks that there was a very small amount of drug precipitate that wasn't in solution. So, only one thing to do from here: make more liposomes.

On the bright side, at least my graph from AK11 (the first drug I tested) still looks nice.

Until next time!
- Lauren

All The (Incredibly) Small Things

Last week felt oddly empty. Maybe it was because I wasn't in the lab, or that I wasn't constantly thinking of (hopefully) funny things to put into my blog. (Or maybe, I actually missed blogging in general. What a weird concept to think about.) Either way, my break was relaxing. Mentally, at least. It was pretty physically challenging with soccer games, so I suppose these balance each other out.

On a separate - but not any less important - topic, the decisions are coming, the decisions are coming! I'd like to thank all the "reach" schools I applied to for waiting until the last moment to release their decisions (some will be released as late as March 31st in the evening). I guess this is all a lesson in patience. 

Since not much new has happened, I've decided to go back to the basics for this blog post and describe how the influenza virus works. I don't claim to be an expert in this subject, so bear with me.

Sadly, I didn't draw this. (Surprising, right?)
 Credit to: http://www.nature.com/nbt/journal/v28/n3/fig_tab/nbt0310-239_F1.html

In replication, the virus first binds to a sialic acid-contating receptor on the host cell, which triggers the endocytosis of the virus. On a side note, do you recall that the types of the flu are labeled as HXNY, where X and Y are numbers? (If you didn't, now you do.) The "H" part of this - the hemagglutinin (HA) part - is responsible for the binding of the virus onto the host cell. There are around 18 known variations of the HA, although only a few, such as H 1, 2, and 3, are common in humans.

Once the virus is engulfed, it's inside an endosome that has a pH of about 5 or 6. Because of this low pH, the M2 channels in the virus allow protons to enter the virus, which then changes the virus's conformation, essentially activating it. This is the step that my lab is trying to prevent. Block the M2 channels, block the proton uptake - and therefore block viral replication. (In theory, anyways.)

The pH also allows the virus to release its eight single-stranded "negative-sense" RNA into the cytoplasm and, eventually, nucleus. In this stage, new HAs can be formed when two different strands of the influenza virus, such as a human and avian strand, infect the same host. The RNAs are mixed, and the viruses that are produced contain RNA from both sources. The "negative-sense" means that the RNA cannot be directly made into proteins; first, it must be translated into "positive-sense" RNA. (At least this naming makes sense.)

The host cell makes more "negative-sense" viral RNA. The virus even prevents the host cell from making its regular mRNA, so the host cell is basically converted into a virus-producing factory for the rest of its short lifespan. After enough viruses are produced, the cell breaks down. Poor cell.

Viruses are produced when they "bud" off of the host cell. In doing so, the RNA is enclosed in the host cell's membrane, along with the HAs and neuraminidases (NAs) - the "N" part of HXNY - that the host cell also produced. (You totally remembered these too, right?) After the "budding," the virus is still attached to the cell through the sialic acid. The NA cleaves the sialic acid, releasing the virus, which can then go on to infect more cells. (More viruses. Yay.)

And that's the process. Simple enough, right? If not, I'm always open for questions. In the meantime, good luck to anyone who's waiting for more college decisions!

Until next time!

- Lauren

Shake It Out

These last few weeks have been filled with learning experiences. I think one of the biggest lessons I've learned is that the bus waits for no one. Although this lesson was a hard pill to swallow, I've (mostly) accepted my fate of missing the bus. Fortunately for me, the bus comes every 15 minutes. This, however, doesn't make me feel any better when I'm about one minute from the bus stop and the bus suddenly pulls into the bus stop, waits ten seconds (if I'm lucky), then continues on its path.

Also, I've taken the lack of comments from my blog group on my last post to mean that they don't mind if my blog posts get to be a bit longer, or if I decide to start posting more often. Thanks, guys!

As for new experiences this week (since missing the bus isn't exactly new):

My cousin and I in bubble balls.

Enough said on that topic.

Earlier, I was able to watch tests on oocytes (frog eggs). Since I'm not a student at BYU, I can't really work with living cells, but I'm still able to observe (and, of course, ask questions). My trainer, Kelly, injected oocytes with the full length M2 protein, then waited a few days for the cells to express the channels. His results will be a bit more accepted than mine, mostly because oocyte tests are common, while make-your-own-liposome tests are few and far in between. Anyways, moving on. When he was ready to test his oocytes, I followed him into the lab next door and saw this.

How come their death ray machine is better than our death ray machine? We have to step up our game.

I'm glad that I was able to see this experiment, though. Apparently Kelly has been working on this setup for months, and he's only started getting decent results recently. (And, as a side note, I think that we're eventually getting one of these in our lab. Yay for two death ray machines.)

After much more discussion, we've decided to change the M2 protein and lipid concentrations - again. I hope this is the last time, but I wouldn't be surprised if it was changed again while I'm gone for two weeks. (I'm going back to Arizona for some prior commitments, but I'll come back to the lab. And yes, in case you were actually worried, I will still be making blog posts) Naturally, we didn't decide on this until after I made my liposomes, so I'll make liposomes with the correct concentrations when I return.

Everything mostly ran smoothly this week, so I can't really complain. I learned, however, that chemicals and equipment tend to run out rather quickly, especially when you're not in the lab. So I spent some time on Thursday making new CCCP and valinomycin solutions, and I'm willing to bet that those will be gone upon my return. Such is life in the lab. I also learned that some substances just don't like to be dissolved. It turns out that most of the drugs I'm testing have hydrophobic groups.

This week, I think I've almost perfect my vial drying method. Since any water droplet in a test tube or vial could dilute our solutions, we have to shake them out and let them air dry until all visible water droplets are gone. The shaking includes vigorous amounts of arm shaking, along with a bit of wrist flicking. And the best part is, I haven't accidentally let go of the vial while drying it. (Yet.) (It's amazing how much our technology our methods use. It's almost as if I'm back at school.)

Because seven out of my eight minutes of actually testing liposomes is filled by me staring at the clock, waiting for the right time, I've come up with multiple ways to keep myself entertained. Sometimes, I'll try to clean up as much as I possibly can (or add pipette tips to the box) before my minute is up and I have to add something to the liposomes. Other times, it's as if I'm playing Simon Says, except it's Computer Says. I have to make sure I follow what's on the computer screen. To make things more difficult, the computer beeps at different intervals (it was used for similar testing, but the process has changed, and no one bothered to make the beeps on time). I think I'm winning this game of Computer Says so far.

Four out of six of my liposome samples this week were great. As for the other two.... The results from the S31N without drug and S31N with drug look exceedingly similar. Which isn't really that good. The drug is either horrible at blocking this mutant M2 channel, or there's something about the higher concentration of M2 proteins and lipids that's not ideal. Either way, I'm sure I'm going to be testing this same drug when I get back, just to see what the problem is.

I'm sure I'll have plenty of time to explain what "good" and "bad" results are later, but for now, I'll explain about pH meter "noise" (I'm sure I could explain both, but this post is getting to be longer than expected. Hopefully no one minds).

With "noise."

Without "noise."

Pictures, I think, speak louder than words. And maybe you can now appreciate the small scale that we're working on. Also, the numbers on the left are not the actual pH; they're a voltage of some sorts. The pH is somewhere in the 6 to 7 range, but the change in the voltage and the change in the pH are the same.

And happy early pi day! I wish I had been born tomorrow at 9:26 am.

Until next time!
- Lauren

P. S. I think I'm going to claim next week as my "spring break" since I'll be playing soccer all of next weekend, so if I don't post, that's why (I know, I know, I can sense your disappointment).

It's a Tall World After All

I learned earlier this week that my brother, sister, and mom are getting their motorcycle licenses. I leave for three weeks, and this is what happens.... I hope this means I'll get the car though. I could live with that.

On another note, it actually snowed this week. I can't even remember the last time I woke up and the ground was white. I never thought I'd say this, but I'm glad that it's back in the 40s again. Who knew that I could actually enjoy weather below 80 degrees (what is this blasphemy?).

As for new experiences, this weekend will be interesting. I can't remember the last time I had to change my clocks for daylight savings. What kind of nonsense is this? It just seems so inconvenient to change the time and lose an hour of sleep. It's not like the sun is staying in the sky for an extra hour or anything. I'm glad Arizona doesn't follow daylight savings - but then again, we get enough sun as it is. Why would we inconvenience ourselves for "more"? (Okay, maybe I'm a bit mad that I'm losing an hour of my day.)

I think my body has an internalized alarm clock, but I'm not sure yet. I'm not used to getting up by myself in the mornings since my mom usually wakes me up. (I know, I'm 18 years old, and my mom woke me up for school. And while I'm at it, I'll say that my dad still made my lunch. Sue me.). Whenever I set my alarm, I think I subconsciously get anxious that I'll miss the alarm, so I wake up around 30 minutes before it actually goes off. Does this happen to anyone else?

If there's one lesson I learned this week, though, it's that labs are not meant for short and/or small people (even if they're meant for working with small measurements). I mean, the pipettes can measure under 5 μL of fluid. I've never seen beakers so tiny either.

Aren't they so cute? Shh, don't tell Kelly (the person training me) that I said that. He thinks it's weird that people call beakers cute.

There are even smaller flasks than that. The two pieces on the left measure 25 mL. I couldn't find any dirty 10 mL ones to borrow for a picture. At least the lab has extra small gloves (but those are still too big. There's no winning. Sigh.). You would think that with all of these small things, that maybe there's be an extra small lab coat. But I guess that's too much to ask for. Don't worry, though; they still give some consideration to short people.

See? I get my own stool. It was just kind of  lonely so I claimed it.

Okay, I think I'm done with my (not so) passive aggressive ranting. Maybe. But I have good news! All my liposomes were good this week, and I had to make six vials instead of four. I'm two for two so far. I wasn't so sure about my S31N liposomes (which have mutated M2 channels that prevent amantadine from binding) because I left the dried lipids out for a few hours. I wasn't expecting to do that, but when I couldn't find any S31N protein, I had to ask for more. Which led to the S31N samples being put into the photospectrometer. Then I had to learn how to convert the absorbance into an actual concentration. I suppose I wouldn't learn as much if everything was easy.

On this note, I have more good news (surprising, right?): we received new pH meters on Wednesday.

This is where I test the liposomes. The computer is good for something, it turns out. It tells me when to add chemicals, and then beeps at the wrong time intervals. As long as I just look at the information and ignore the beeping, I'm fine.

However, I learned that new does not necessarily mean improved. One of the pH meters was too "noisy," meaning that there was too much fluctuation in its readings. And the other meter just didn't work. So I only had one pH meter to use. To test six different vials. Twice each. And the tests last about 10 minutes every time. Yay. When I think about it, the situation is kind of funny. We get new technology, and it doesn't work, but the older technology works just fine. Oh, the irony. (Maybe I should use floppy disks and Windows 2000 more often.)

Overall, I think this week was filled with too much waiting. I had to wait for the concentrations of the M2 proteins before I could resuspend my lipids in solution. I had to wait to see which concentrations of the lipids and proteins that I should use. I had to wait for the filter supports to arrive (which they did on Wednesday). (Insert more discussions on lipid and protein concentrations here. I think we're back to using what I originally had in my last post. That's what I used anyways.) I had to wait for more CCCP because I ran out in the middle of my experiments. Thankfully, we found some in the freezer. (Not before I put everything away, though.) But, since my liposomes ended up okay, I don't think I can complain much. I just hope that I can test a drug that'll be a decent block against the mutated viral proteins.

I always feel like I have so much to say (well, to write). Maybe I should start posting twice a week.... I'm not sure my blog group would be too happy with that. Oh, well.

Until next time!
- Lauren

P.S. Success! I still managed to finish this on Friday, even if it is late. I hope I can keep my goal to post on Fridays to be somewhat consistent.

Just a Small Town Girl, Living in a Snowy World

This week, I saw snow. I know snow isn't exactly uncommon (especially on the East Coast right now), but where I live, even rain is a Facebook event. And snow? That'll blow up your feeds for the entire day. I admired the snow for a few minutes, but the novelty wore off as soon as I went outside. Snow is cold; I am not. Unfortunately for me, I had to walk in this weather from the bus stop to the house. I'm not looking forward to doing this again next week. Fortunately, I had a nice warm coat so I didn't get too cold (except for my nose). I'd like to thank the parental units (again) for getting me said coat.

Weather aside, I'd like to think that this week went pretty well (in the lab, at least), although I was a bit dubious in the beginning. I'll use this post to explain more in detail what I'm doing, so bear with me (or skip until the end if you really want. I won't know the difference).

First, I got four small vials and had to clean them. To this end, I took them to the fume hood and washed them with acetone, chloroform, ethanol, and petroleum ether (oh my). Why I was trusted with these chemicals, I'll never know. But the lab is still in one piece! For now, anyways. Then, I turned around and saw this lovely sight.

"If you kill these slices, be prepared to donate your own brain cells for today's experiments."

Ah, I feel welcomed already. On a side note, I was able to see the last frog surgery on Monday. They wanted to collect oocytes for further testing of the M2 channel. It's similar to what I'm doing, but they use mRNA to make the M2 channels, while I'm artificially making liposomes with M2 channels.

Next, I add around 150 μL of lipids, which are suspended in chloroform, to each vial. After placing parafilm (how is that stuff so stretchy?) on three of the vials, I place the other vial on the rotavapor, which spins the vial while pumping a continuous stream of nitrogen gas. Eventually, the chloloform is gone, and the lipids are stuck to the end of the vial. I repeat this with the other three vials. When I'm not using the vials, I always put parafilm over them; the oxygen in the air can react with the lipids, making them unreliable in the testing phase. It'd be rather unfortunate if I labored over these lipids and liposomes for hours, only to have the liposomes be leaky during the test (although, I'm sure this'll happen eventually).

Then, I add around 180 μL of both chloroform and wildtype M2 (meaning that the M2 channel has not mutated) to two of the vials. And then I repeat the rotavapor phase, but I sit there longer, staring off into space, because the M2 channels were suspended in methanol. Methanol takes much longer to evaporate off, although adding the chloroform makes it go a bit faster for some reason. Now that I think about it, I could probably read during this time. Or I could be efficient in making more. Decisions, decisions....

After adding about 150 μL of internal buffer to each vial, I put them on the vortexer and sonicator, and then repeat this until there aren't any more lipids on the sides of the vials. Finally, I store these mixtures in the fridge. Viola! We have liposomes. And thus, my day one of this process is complete. (I know, I know. I'm sorry, this is going to be a long post.)

On day two, my fingers get a work out. I have to heat up the internal buffer, the vials, and the extruder (this sounds kind of ominous) to 57 degrees Centigrade. However, before I heat the extruder up, I have to assemble it. To do this, I wash the pieces with methanol, then place filter supports, a 0.2μ filter, and more filter supports, into the chamber. Here's what it looks like when it's all assembled with the syringes.

It's not so scary now, is it?

The heating just makes the extruding process easier (or so I'm told). In this process, I first put some internal buffer into the syringe on the right. Then, I push that syringe in, and the liquid (somewhat magically, to me at least) goes into the syringe on the left. I repeat this ten more times, so that the liquid ends in the syringe on the left. Because of this, the filter absorbs some liquid and makes extrusion easier (easier is better, trust me).

After I remove the internal buffer solution, I put all of one vial into the right syringe. Usually, I use a vial without the wildtype M2 channels first. Next, I'll push that through the filter 21 times, so, again, the mixture ends on the left, and I'll deposit that into an Eppendorf tube (such a big name for a small vial. The picture actually shows the final products after extrusion, when the mixtures are in the Eppendorf tubes.). Since I have another vial that is also a blank (that is, it has no M2 channel), I can filter that through as well. Then, I repeat this whole heating-and-assembling-extruder process (which is harder than it seems, since the filters and filter supports are so small), just so I can extrude the mixtures that have the wildtype M2 channels. (And, let me tell you, extruding liposomes with the M2 channel is a lot more difficult.) Finally, I let the liposomes sit for about a day in room temperature.

Why do we extrude the liposomes, you might ask (well, I asked, anyways). Although we can get better signals (I'll explain later) from bigger liposomes, having liposomes completely different sizes makes the signals a bit unreliable. By extruding the liposomes, they will be roughly the same, small size, so this makes it easier to replicate the experiment. 

And all of this prepwork leads up to day three! You'd think that we'd have some really awesome experiment that takes a while to run and is extremely satisfying, but that's not exactly the case. For the test, we use the pH meters I showed you in an earlier post. These pH meters don't actually read the pH, though; they read a voltage, which can then (somehow) be converted to a pH. 

First, I add 3 mL (pretty much the only measurement that isn't in μLs) of external buffer and a stir bar (small magnets that spin based on a current going through a coil of wire) to a different, smaller vial. The actual test only lasts about 10 minutes per sample. I start by adding 30 μLs of 0.1 M HCl and 30 μLs of one sample to the external buffer (and I add 30 μLs of a drug solution to two of the mixutres), then I start the pH meter. Throughout the test, I add valinomycin, CCCP, 0.001 M HCl (twice), valinomycin, and CCCP. I'll explain what these molecules do and why we add them in a later post.

Finally (for real this time), I upload the results into a floppy disk (this was, actually, my first time using a floppy disk. Nice to know that I'm learning how to use old technology as well as new technology.), so I can transfer them to a different computer that has a magical excel spreadsheet that makes sense of all the numbers. Again, I'll explain more about this later.

Tada! I found some results. And an old computer.

Okay, that was a mouthful! It was a good review for me, too. Somehow, I managed to replicate this process mostly by myself, and my results were good! (This was, of course, after I transferred the wrong data and accidentally got a flat pH of about 3. But you live and you learn.) So now I'm trusted to run actual experiments (because this was just to see if I could do it), and I have to do it with six vials. I had four vials this time: one blank without drug, one blank with drug, one wildtype M2 without drug, and one wildtype M2 with drug. I'll need two more so I can test drugs on a mutant strain of the virus. (And, since we have colored tape, I decided to make them rainbow colored to keep track of them. Because I could.)

Let me know if you have any questions, because I sure do (but this isn't really unusual).

Until next time!

- Lauren

P.S. After I wrote this, I learned that most of my concentrations and numbers were off. Thankfully, it's not my fault, since this is what I was told. But most of my numbers will change, although the process will remain the same, so I'm not going to edit what I've already written.

All About That Place

Good news: I was officially approved by a BYU committee, so I can work in the lab now. More good news: I've taken a bus back to the house a few times, and I haven't gotten lost (yet). If you had told me last week that I'd be taking the bus back from BYU, I would've scoffed. I've never taken a bus by myself before, let alone wander a city that I've barely been in for a week. However, this week was full of new experiences, and I'd like to think that I've learned how to use public transportation (ie. bus drivers are not mind readers - you actually have to pull the yellow wire to request a stop. Who knew?)... at least a little bit. I'd like to thank the bus drivers for helping me throughout this process. Additionally, I managed to walk through buildings on a college campus without feeling like I stuck out. All in all, I'd say it's been a successful week.

On a different note, I finally started learning my way around the lab. The names of the equipment are apt; the vortexer mixes solutions in vials by creating a mini vortex, and the sonicator mixes solutions in submerged vials by sending sound waves through water (and, as the person training me said, it literally sounds like a dying bat). But don't let this simplicity fool you. Even though the name may be easy, using the equipment is not. Especially when the equipment you're using has, for all intents and purposes, a pressurized cannon connected to it. For those skeptics out there, I give you this proof:

No, it's not a death ray, although it looks like one. It's called a rotavapor.

That tank is filled with compressed nitrogen. It's chained to the wall because, if it fell over, it'd literally blow through a wall or two. Or maybe three. I'm actually going to be using this piece of equipment (yay, lucky me). The rotavapor rotates the vial while pumping in nitrogen gas, allowing the solvent to evaporate off and leaving the lipid evenly distributed. I think I'll post about my experiment process later, since it's rather lengthy. However, I will say that working in a lab requires patience. Preparing the liposomes took hours, and the actual test at the end took minutes. Most of those minutes, furthermore, were all controls, so those results didn't mean much, since they were expected.

I've enjoyed working in the lab so far. I'm a bit nervous for next week, however. My uncle says I'm going to replicate this mostly by myself, although I will receive help if I ask for it. My uncle is also the one that pushed me to take the bus. I think his plan is to make me more independent (and it might actually be working). Maybe I'll use this independence to walk over to the UVU library. Unfortunately, I don't think the library will allow me to check out any books unless I have a card - which I don't have. But my cousin has one....

Until next time!

- Lauren

First Thing's First, I'm a Chemist

I'm happy to say that I arrived in Utah in one piece! Unfortunately, my brain didn't like waking up at 4 am, and I consequently forgot to pack my laptop charger. I knew I'd forget something, and I'd like to thank my parents for shipping my charger to me.

On another note, yesterday I was introduced to the lab that I'll be working in, and,despite running on three to four hours of sleep, I managed to remember most of the equipment names. I'm particularly fascinated by the pH meters, of which there are four. Sadly, three of the meters are broken. On the other hand, three of the meters are broken. This means that I can practice using these pH meters without too much stress, especially since the bulb on the end of the meters is extremely fragile and thin (in the order of nanometers). I'm excited to begin working in a lab with actual equipment, since I didn't get a chance to do many experiments in high school.

Here's the counter-top that I'll mostly be working on, complete with the pH meters and Windows 2000.

In addition to this lab space, I'm also supposed to wear a lab coat while in the lab. Now, I look like an actual chemist, but I don't quite feel like one yet. This may be because of the paperwork that I've had to complete - I basically had to sign my life away. No big deal. In addition to the waivers, I just completed an online course in lab safety, which was helpful. I learned about the plethora of chemicals that could main and/or kill me (including a strain of influenza that was decently lethal in the early 1900s. Luckily for me, that virus isn't being used for testing at this time). I don't think I'll start working on my project until early next week because a committee at BYU needs to officially authorize me to use the equipment. 

Nevertheless, I've researched more on the mechanism of the influenza a virus and its usual vaccines. Most vaccines are manufactured months in advanced, and they target viruses with specific glycoproteins (hemagglutinin and neuraminidase). The influenza viruses are named based on these glycoproteins; for example, H1N1 and H5N1 are both influenza a  viruses, but with different humagglutinin molecules. Most vaccines are ineffective over long periods  because these glycoproteins mutate so rapidly. However, the M2 protein channels are consistent in the influenza a virus, and so a drug that blocks this channel would (hopefully) prevent all mutations of the influenza a virus from replicating.

I hope that I'll be able to work in the lab next week, so I can start making my own liposomes and testing some of the amantadine derivatives. I'll post later on the actual mechanisms (on both the influenza replication process and drug blockage) once I understand it more. For now, I'll continue waiting for approval, learning, and looking for a library (you can take me away from my books at home, but you can't take books away from me).

Until next time!
- Lauren