Out of all the things you could put on your face, bugs are probably
not high on the list. There are much better things to feel–cotton balls,
soft textiles, face creams and lotions, etc. Makeup is another common
thing that goes on our faces, and most people wear some form of it at
some point in their lifetimes. Here's something you may not realize: if you've ever worn red lipstick or most blushes, you've had bugs on your face. Surprise!
We got to demonstrate the power of natural dyes ourselves at last week's Science on Main event. These are ground-up cochineal bugs! PC: Jessica Noviello.
Many
natural products are used in makeup, and have been for years because of
their bright colors. The specific bug used to make red, for example, is
the cochineal bug (Dactylopius coccus), which are native
to northern South America and into the American southwest region. The
cochineal bugs are mostly immobile parasites that live on the undersides
of prickly pear cacti pads, which means these bugs are technically an
Arizona export product too, just like copper is. These bugs are scraped
off of the cacti and eventually dry out in the aridity and high heat
once removed from their homes.
Once the bugs are dried, they are then ground up to extract a chemical called carminic acid (C22H20O13),
which can make up as much as 25% of their total body weight. While they
were alive, these bugs produce the carminic acid to deter predation
("don't eat me! I taste really, really nasty!"). Unfortunately tasting
bad does nothing to deter humans who want to use the carminic acid to
make things a beautiful bright red color. The carminic acid is then
mixed with aluminum or calcium salts to create the compound carmine dye, also known as cochineal after the insects it came from, and is then used
to make food and makeup a bright red shade. Next time you're looking at
makeup or red food, look for the words "Natural Red 4" or "E120;" both
are made from cochineal bugs. We got to demonstrate the power of natural dyes ourselves at last week's Science on Main event.
The picture above shows ground up cochineal bugs that we, the SoM Team,
were using to demonstrate how colors are made. We first mixed the
cochineal bugs with water, which has a neutral pH. pH is a chemical
property that measures how acidic or basic a liquid is. Something with
many H+, or hydrogen ions, is more acidic than something with more OH-
ions. Something like water, which has equal amounts of H+ and OH-
combined into H2O, has a neutral pH, right in the middle of the pH scale.
A visual pH scale. PC: https://neptunecoffee.com/is-coffee-acidic
The
total range of the pH scale goes from 1 to 14. Things that have a pH
lower than 7 is an acid, and things with a pH higher than 7 is a base.
The farther away a number is from 7, the stronger the acid or the base
is. Most things close to 7 are okay to eat, but things like bleach (pH =
13) or battery acid (pH = 1) are potentially deadly if swallowed. This
is why you should never eat something in a chemical laboratory! When
we mixed the cochineal bugs with water, the mixture was a light red.
When mixed with vinegar, a medium-strength acid, they turned more
orange, and when the bugs were mixed with a base (sodium carbonate),
they turned a beautiful purple. The cochineal bugs' shells were reacting
with the different chemicals and creating different colors. This is one
example, but there are thousands of these small chemical reactions that
go into creating makeup, paints, foods, and all kinds of colorful
things that humans use.
Take a look at your common household items. Are there any natural dyes there? Let us know!
In the American-English spoken language, there are many metaphors for that member of the family that seems just a little bit more different from the others–the black sheep, the odd duck, the bad apple, for example. One often heard specifically with twins is that of an "evil twin." The idea of an evil twin is ancient and based in some of the oldest mythologies that folklore still knows of, including Native American creation myths and those from the Mandika people of southern Mali, but for the most part it has always been more of a fictional tool than a reflection of reality. The one major exception (because there's always one) is in chemistry.
An approximate visualization of what the glucose molecule looks like.
PC: Jessica Noviello
Every chemical has a chemical formula that shows how much of every element is in it. For example, the formula for glucose, a basic sugar created by cells for energy, is C6H12O6. This formula tells me, a definitive non-chemist, that there are 6 atoms of carbon (C), 12 atoms of hydrogen (H), and 6 atoms of oxygen (O) in every molecule of glucose. Unfortunately, this is only half of the story when talking about chemistry.
As small as atoms are, they are still three dimensional, which means the molecules they create are also three dimensional. Every molecule has a specific structure of how the atoms are arranged that give it a particular shape. It's hard to see in the two dimensional approximation of the glucose molecule that I made (above), but glucose has a slight twist in the molecule, and the loosely connected carbon to the top-right is more underneath the rest of the molecule than I've shown here
There are many different molecular structures. Some shapes look like a triangular pyramid (tetrahedral), a starfish (seesaw), and even two x's merged together (octahedral), but these are only some of the many shapes that molecules can have. Sometimes the only thing that's different between two molecules is the shape. The same chemical formula but a different molecular shape means that the two molecules are totally different. In special cases, the molecules are the same in both formula and are almost identical in structure, but they are mirror images of each other. These molecules are called enantiomers.
To visualize how enantiomers look, just look down at your hands. They each have five digits, palms, and fingernails. They both do the same thing (more or less) and allow you pick things up, move things around, write, type, hold, and touch. Even though they look very similar, you have a distinct left and a distinct right hand, and they are not the same. They are mirror images of each other, and though you may try to put one on top of the other, it will never be a perfect fit.
These "two" pictures are actually only a single picture! I took a
picture of my left hand, copied it, and flipped the image. It looks
pretty much like my actual right hand! PC: Jessica Noviello.
Chemical enantiomers are the same way, and chemists even refer to them as "right" or "left" handed molecules. Another word for this is chirality. There are many known chiral pairs in chemistry, and the differences in chemical effects between the two members of the pairs range from relatively harmless, such as things smelling different, to downright dangerous.
Oranges smell like oranges because of + limonene, but
its cousin would make them smell like lemons!
PC: Wikipedia, used under the Creative Commons license.
On the harmless side, there are plenty of good examples in the food world. One chemical, limonene, smells different depending on the handedness of the molecules being smelled. The right-handed (+) limonene molecule smells like orange, but its left-handed (-) counterpart smells like, as you may have guessed from the name, lemon. Another example, and one that we had at our November Science on Main table just a couple of weeks ago, is that of another chemical called carvone. L-carvone (-) smells like spearmint and is often used in essential oils products, and its counterpart D-carvone (+) smells like caraway seeds or rye.
A pack of thalidomide capsules. PC: Steven C. Dickson.
Used under the Creative Commons license.
On the more dangerous side, the best example is also a tragic one, a true chemical evil twin. Before chirality and enantiomers were understood, pharmaceutical companies and scientists didn't know that the almost-identical chemicals could produce very different outcomes. In the late 1950s, many doctors in Europe prescribed pregnant women a drug called thalidomide to ease morning sickness, anxiety, and trouble sleeping. It really did a great job doing all of that, but it also caused serious birth defects in babies whose mothers used the drug. 40% of these babies died at birth.
Doctors made the connection between thalidomide and the birth defects in 1961, and the drug was immediately pulled from the market. It turns out that one of the enantiomers caused the beneficial effects of a sedative that relieved the symptoms of pregnancy, but the other caused the birth defects, and both were present in the medicine prescribed. Once chemists figured this out, they also figured out how to isolate the helpful molecule from the dangerous one. Today, thalidomide is still used to manage and treat serious illnesses such as cancer, tuberculosis, leprosy, and HIV/AIDS. It is a drug with a terrible history and still is risky to take, but it is significantly safer than what it was in 1961.
This Thanksgiving, be thankful that your family isn't as bad as chemistry's evil twin!
This
is a special guest blog article by Joel Lusk, a third-year PhD student
in Biological Design at Arizona State University and a member of the
Science on Main group. His research involves the study of photoacoustic
contrast agents in the imaging and detection of cells. He can be reached
at jlusk@asu.edu.
Have you ever seen the
stories in the news where scientists make plants or animals glow? These
stories are fascinating and amazing, and scientists accomplish these
feats by using a protein that was originally found in a jellyfish! This
protein is called Green Fluorescent Protein (GFP for short), and the
story of its discovery and the scientists that originally pioneered its
use is an interesting one. The protein itself has been used in science
in a wide variety of applications to study plants, biological processes,
and even the things that make up our cells.
Two mice expressing enhanced GFP with one non-GFP mouse in the center. Source: Moen et al., 2012, BMC Cancer 12.1: 21.
In 1960, a scientist named Osamu Shimomura started studying the bioluminescence of the jellyfish species Aequorea victoria.
When the rings of these jellyfish are squeezed, they produce a glowing
liquid. Shimomura claimed to have squeezed over a million jellyfish to
collect this liquid and study it for his research. In 1962, he and his
colleagues was the first to identify a protein in this jellyfish that he
named aequorin. The aequorin first emits blue light, which is then absorbed by the GFP, causing it to glow.
The Aequorea victoria jellyfish. Copyright: Sierra Blakely.
Now
that the protein that was responsible for the jellyfish's glow was
identified, several other scientists became interested in cloning the
gene responsible for it. If the gene for the fluorescent protein could
be cloned and inserted into other organisms, it could revolutionize
biology. In 1992 a biologist named Douglas Prasher suggested that this
glowing protein could trace the way proteins moved in cells and was the
first to clone the GFP gene. Unfortunately, the funding for his lab ran
out and he left academia. Before he left, Prasher sent several samples
of GFP to other scientists so they could continue his work.
After
the genetic sequence was found for this glowing protein and it had been
successfully cloned, the doors opened to a world of new possibilities
for GFP. Prasher had predicted that this protein could be used as a
reporter molecule in cells. This means that when a scientist wanted to
know if a cell was producing a protein, they could just add the gene for
GFP next to the gene for the other protein into the genetic code. When
the cell produced that protein, it would also produce GFP, causing the
cell to glow. This allowed scientists to undertake all sorts of amazing
experiments, including the work of Martin Chalfie, who produced these
proteins in E. coli bacteria and worms called C. elegans.
Neurons imaged from a "Brainbow" mouse. Source: Smith (2007), Opinion article in Neurobiology 17.5: 601–608.
Another
scientist, Roger Tsien, took the GFP and augmented it to be many
different colors. He did this by changing the shape of the protein so it
absorbed and emitted light at different wavelengths. This allowed
scientists to not just label cells and animals with a green protein, but
with an entire rainbow of colors! This has been applied to every part
of the field of biology, allowing scientists to understand and see
processes they never could before. Shimomura, Chalfie, and Tsien all
shared the 2008 Nobel Prize in Chemistry for their work with GFP.
Unfortunately, Prasher, the man who first cloned the protein, was not
awarded the prize as three people maximum can share the prize. To honor
him, all three recipients mentioned him in their acceptance speeches as
even invited Prasher to the ceremony.
So now we know
the history of GFP, but what are some of the cool things that scientists
can do with it? Mainly scientists have used the protein to tag and
visualize processes in cells. One amazing application of GFP and other
fluorescent proteins was the production of a "Brainbow" mouse. This
mouse produces a variety of colors in its neurons, allowing scientists
to see the way the neurons interact with each other. Not only does this
tell scientists a lot about how the brain works, it also creates a
beautiful image!
The story of GFP is one that shows the
usefulness of a fundamental science. Who would have thought that a
protein first found in a jellyfish would go on to revolutionize the way
we understand and see cells? Research into fluorescent proteins is still
going strong, and scientists are currently looking at new fluorescent
proteins that have been isolated from other sources such as bacteria and
coral. Further work with the fluorescent proteins might reveal even
more about the inner workings of our cells and our bodies. In the
meantime, we can have a little fun with these proteins, and even paint
pictures using bacteria who produce these fluorescent proteins across
the visible light spectrum!
A picture painted on an agar plate with bacterial colonies expressing a variety of fluorescent proteins. Source: Tsien Lab. Artwork: Nathan Shaner. Photographer: Paul Steinbach.
Chalfie, Martin, et al. "Green fluorescent protein as a
marker for gene expression." Science 263.5148 (1994):
802-805.
Moen,
Ingrid, et al. "Gene expression in tumor cells and stroma in dsRed 4T1
tumors in eGFP-expressing mice with and without enhanced oxygenation." BMC
cancer 12.1 (2012): 21
Tsien, Roger Y. "Constructing and exploiting the
fluorescent protein paintbox (Nobel Lecture)." Angewandte Chemie
International Edition 48.31 (2009): 5612-5626.
Smith,
Stephen J. "Circuit reconstruction tools today." Current opinion in
neurobiology 17.5 (2007): 601-608.
This blog article was written by Dr. Christina Forbes, co-founder of Science on Main. She earned her PhD in chemistry and is currently a post-doctoral researcher at Arizona State University.
I was recently matched through Skype a Scientist with a 6th grade classroom at St. Hubert Catholic School in Minnesota. Some 40 students and their teacher got a chance to Skype with me while I was in my lab in Tempe, Arizona. I showed them around the lab a bit, but we spent most of the time just chatting about my work. I met with 3 different class periods, and all three classes asked me a question that is surprisingly hard to answer: "What's your day like?" Since it was one of the burning-est questions these students had for me, I wanted to bring it up to Science on Main. After all, our aim with Science on Main is to answer your questions! This question sometimes follows the classic "What do you do?" that comes up in polite conversation. I've learned that the attitude towards my accurate-but-short answer, "chemist," can range from excitement to disgust. Some people think that's cool, others think that sounds pretentious, and even others seem uncomfortable or unsettled with my answer. Only the very curious, or confident, have asked me the follow-up: "So what's your day like?"
Indeed, this is just my job, and it's a job I like and I worked hard to get to, but it doesn't endow me with any particular superpowers. I don't know how much people in other professions are asked this question, but I hope everyone is. There is so much fascinating stuff that can go into one person's workday. What does a software engineer do on a day-to-day basis? Or an investment banker? Or an event coordinator? Nonetheless, these 6th graders were very curious. If you are also very curious, then I can give you a detailed approximation of my answer to "What's your Day Like?"
[Get on with it!] On an average day, I don't function well for the first hour, so I sit at my laptop with my coffee before I attempt any chemistry. Yup, even scientists have morning commutes and laptops. I deal with emails, follow up on other emails, check my calendar for scheduled meetings, update my calendar based on the emails I got that morning, and other desk-stuff that I have to do to keep my life in order. I might edit a peer's manuscript for a paper they want to publish, or I might finish writing a draft of something that I'm working on. I might catch up on reading recent literature, like reading the news but it's only the chemistry section, written with all the jargon. When the coffee has kicked in and I think I'm a little more ready to face my day, then I'll pull out my lab notebook, put on safety glasses, and go into the lab. My day in lab will focus on a different part of a project that I might be working on. To save chemistry jargon, I will use an analogy for my project: making a batch of THE BEST cookies for a friend. Let's say I chose, with some reasoning, to make chocolate chip cookies for my friend. Troubleshooting a reaction: I'll need a good recipe for the cookies. I probably looked up recipes online, maybe chose a few recipes based on reviews or ingredients that I have on hand. Maybe I asked a buddy in another lab what recipe they use, or if they have feedback on a recipe they tried. Once I have a recipe I feel good about, I do a test reaction, or a small batch. I look at the product (in this case, the cookies) to see if I could have done the reaction differently, or if this recipe is terrible and I need to try a completely different one. I'll do a series of these test reactions until I obtain the cookies I want, then I scale up the reaction and try a larger batch. Sometimes I'll have to adjust the recipe a bit more when I make a larger batch, like a longer baking time or less salt. All the while, I make notes on how I set up each batch of cookies, and how the cookies came out. What was my baking time? Baking temperature? How much sugar? Should I use honey instead of sugar? Were the cookies undercooked? Burned? Too salty? I might spend a month or more testing and perfecting a recipe for cookies in these batches. For those of you trying this at home, this might look like running reactions, refluxing reactions, distilling materials, running a purification column, mixing chemicals, etc. Synthesizing a molecule I need: In the midst of testing my cookie recipe, I run out of chocolate chips. Nope, the store doesn't sell any chocolate chips, but the store does have a lot of cheap cocoa beans. After a little more internet searching, I learn how to make chocolate chips from the beans, and find that I have the equipment to roast, winnow, grind, and, generally, make chocolate. Since I've never done this before, I may have to borrow some techniques I know about about making coffee from the beans, or borrow equipment from a neighboring group. Much like the cookies, I practice making the chocolate from the beans in small batches, but it comes out gritty and yucky. I work on refining my chocolate to get the grittiness out before I can make it into chips. Once I have a few chocolate chips that are right for putting into cookies, I'll make a bigger batch so that I have plenty to use for testing out my cookie recipes. All the while, I've made notes on each step of the process to make the chocolate. That way, I've built a recipe that I can follow if I need more chocolate chips. This might look a lot like troubleshooting reactions. I bring this up because sometimes there are materials that I can't buy, and I have to take a step back in my project to make what I need for myself. So much of this stuff is self-taught.
Something as simple as removing liquid from a solution requires this contraption.
Drying a purified product under vacuum. Imagine chocolate chips, I guess.
Characterizing: Remember, I'm trying to make these cookies so that my friend thinks they're THE BEST. To do that, my friend will need some other cookies to compare against mine (think control experiments). Maybe they have another friend with jerk chocolate chip cookies, and another friend that made some ginger snaps. After trying all these different sample cookies, my friend thinks that mine are THE BEST, but we should probably check again another day, just to be sure. More cookies are made, and each sample cookie is brought to the friend the next day, and they still think mine are THE BEST. But, there's a rule of three in replicating results, so we should check again next Monday. I'm using a person and their sense of taste as an analogy for taking a measurement for making comparisons. This is where the edge of science really happens, and it can depend on the project. It could be taking a spectroscopic measurement, or it could be comparing different reaction rates. This is often in front of a computer that it attached to some very expensive instrumentation. Knowing if your method or product is THE BEST is revealed by a number that the instrument tells you. It could be a simple as taking a measurement of a sample, and the number 550 means that a month's worth of tireless hours of work has paid off. It's very exciting, but it probably doesn't look as exciting as other parts of my work.
Sample preparation for a spectroscopic measurement.
Measuring pH in a series of samples. UV-Vis spectroscopy came a little later.
Squiggly-lines and peaks coming from instruments is sometimes the most exciting part.
Fixing equipment: Naturally, the following Monday, my friend has the flu, so I spend every day for a week with my friend. I need to get them back to good health so they can try all the cookies a third time. When my friend tries the cookies a third time, they think those other jerk chocolate chip cookies are THE BEST. This seems weird, since it's not consistent with our earlier tests. I have my friend try the sample cookies the next day, for a fourth time. My friend now likes ginger snaps, and they seem very confused and disoriented. I might spend a few days studying human anatomy, and realize that my friend probably has a blood sugar problem, and now it's time to call a doctor. Since doctors can be really expensive, my boss asks me to correct my friend's blood sugar problem myself. I might have to study human anatomy for two more days, only to realize that my friend is having a calcium deficiency, which effects their ability to taste anything. I give them milk, and my friend is immediately feeling better. My friend tries the cookie samples, and mine are THE BEST. For good measure, I ask my friend to try the cookie samples three additional times over three different days, just to be extra sure of the result. A frustrating part of my job is when I've had to spend whole days away from my projects just fixing instrumentation. We need our instruments to be accurate, well calibrated, and well maintained. In my lab, these instruments include spectrometers, chromatographs (gas or liquid), or potentiostats. A service technician can be expensive for on-site service (e.g. house call), so we often learn how to do repairs and maintenance ourselves. These repairs can range from cleaning sample holders to needing replacement parts that you can only describe with picture messages.
That time we had a problem with a part that isn't normally part of the wear&tear kit and doesn't have a part number... 20 emails, 3 manuals, and many pictures later, I managed to communicate to the service tech that I needed a new needle port tube.
Because a degree in chemistry sometimes means that you've had to figure out how to disassemble, diagnose, and service an injector for an HPLC. (Really, what does that even mean?!?)
The tube had been mangled--not sure how, or how long it was like this. The guide did not fit on the old tube, thereby ruining the fluid seal, thereby disrupting sample injection for analysis, and grossly ruining the data. A reminder that scientist does more than just experiments and mixing chemicals!
Publishing: Since my cookies are THE BEST, now I need to publish my recipe. I write out my recipe, with pictures of what they look like and a picture of my friend eating each sample cookie (they're happy only when they're eating my cookies). I attach a supplemental document that describes how I made the chocolate chips from cocoa beans, with some information about my friend who tried and judged the cookies. I send all of this to a bakery owner, and they send my recipe to other bakers. These other bakers submit feedback about my recipe, asking me to have my friend try some other cookie types. These other bakers also think that my cookie baking time is a little weird. I spend some time doing what the bakers ask, subjecting my friend to more cookies, and refining the cookie-making process. I send a revised recipe and more photos of my friend eating all these other cookies, and the bakery owner agrees to publish my recipe in their next book. This is a very broad brush-stroke of the peer-review process. This is often a background think to my work, but dealing with reviews and doing new experiments can become part of my average day.
Copyright prevents me from posting my papers, so instead you get a picture of my dissertation. For the record, a doctoral dissertation should not be this long.
Training new colleagues While I'm working away at perfecting my cookie recipes, my boss walks in with a college student and says "this new student wants to learn how to make cookies. By the way, they've never been in a kitchen before, but it would be great if they had a batch of cookies by the end of the week." My boss leaves, and the student looks at me with excitement and fear. We may as well start with the batch I'm working on, and I show the student how to use a spoon to stir the dough. I step out of the kitchen for a moment, and when I return, I find the dough on the floor. Maybe this new student was stirring the batch too fast and lost control of the spoon and the bowl. I tell the student that it's ok, but now they'll have to help me start over. It's a part of the learning experience, andif they pay attention, they'll get better with time. As I explain the recipe and how to stir the dough, the student seems to think I know everything about cookies. I explain that I wasn't born with cookie knowledge, but I just worked with cookies for a long time. I tell them that if they work with cookies long enough, and learn from their own mistakes, then they'll know a lot about cookies, too. As you gain more experience in your project or techniques, you're expected to help train new people. You learn a lot of patience when you train new people, but it's crucial to the learning process. I sure know that I tested people's patience when I was still learning this stuff! Each day in lab can be very different, since each day might be part of this overall process of making and testing THE BEST cookies. At some point during the day, I eat lunch (maybe). Sometimes I might meet briefly with my boss, and we talk about how cookie-making is going. Maybe not; I've earned some independence with cookie-making. By the end of the day, and when I've brought my work to a natural close, I catch up on my emails or whatever else happened at my desk while I was in lab. I write out a new to-do list for the next day, hopefully with notes to myself like "make another lb. of chips" or "try the recipe on page 42 with more butter." I close up my laptop and go home. I try throw together dinner. Maybe I look at a colleague's manuscript while my husband works on his own homework, or maybe I work up and analyze some new data that I can't wait to see the next day. Or maybe I'll just read a book or watch Netflix. Scientists just need to chill sometimes, too.
The bottom of the ocean is one of the most unknown places on Earth. Deep canyons and high seamounts dominate the landscape. There are black smokers, small vents in Earth's crust, spewing hot water and toxic chemicals into the water. There is no plant life; sunlight cannot penetrate water that deep. The animals that live down there come in odd, pliable shapes, and some use their own bioluminescence to lure prey in. Even though it is on the same planet, the deep ocean is not of this world.
The Papahānaumokuākea Marine National Monument.
From: https://www.papahanaumokuakea.gov/
It is because it is so unknown that marine scientists are so eager to explore it, and one current mission is doing just that. The Nautilus Expedition is a massive effort to characterize and study the geology, biology, and archaeology of a few key areas of the Pacific Ocean between Hawaii, California, and Alaska. Currently, the ship is west of Hawaii, in the Papahānaumokuākea Marine National Monument (MNM), the largest marine conservation area in the world. The mission is operated by the Ocean Exploration Trust, a non-profit organization founded in 2008 to engage in pure ocean exploration. Its founder, Dr. Robert Ballard, is the man is credited with discovering the remains of the ill-fated Titanic, and is current a National Geographic Explorer in Residence. If something is going to be discovered, this is the team to do it.
So what are they looking for? For one, they are now looking closely at the underwater geology around tectonic plate boundaries, and the western coast of North America is an excellent place to do it. Multiple tectonic boundaries, including the Cascandia fault line of the subducting Juan de Fuca plate, are responsible for creating the landscape of the west coast. The Nautilus is there to photograph and map areas of the seafloor that have been missed by previous studies, and to measure the chemicals in the ecosystem around it.
Dr. Marc Fries examines this fragment of fusion crust that
may
have come from a meteorite that fell in March 2018.
Picture by Susan Poulton, Ocean Exploration Trust.
Its trek began in Southern California, where it studied the deposits of underwater landslides caused by movement along the San Andreas fault, and traveled up to the Cascadia Margin near Washington and Oregon. As it moved from Astoria, WA to Sydney, British Columbia (Canada), the Nautilus also looked for fragments of a meteorite that fell in March 2018. Preliminary findings indicate that they did indeed collect two small pieces of the fusion crust that forms on meteorites as they burn up in Earth's atmosphere, and it's all because of the Nautilus mission.
The Cascadia Margin is not just of geologic interest; the large volumes of methane gas and hydrate stored in the area makes it an interesting spot for studying the chemistry of the area as well. According to the Nautilus website, "establishing a baseline by documenting and characterizing these sites is
timely because geological events, such as earthquakes or submarine
landslides, could result in important environmental impacts due to
sudden methane release." Over the past two years of research, the Nautilus team has discovered over 2700 bubble streams at 1000 distinct locations along the Cascadia Margin. Before this mission began, it was unclear exactly how much methane was near the Cascadia fault, and how (or even if) it was being released.
As impressive as the geology and chemistry are, perhaps the most awe-inspiring is the biology discovered. At almost every location, the Nautilus stayed for at least two weeks, taking pictures and streaming live video narrated by the crew and scientists on the expedition. One of the best parts of exploring is being surprised by what is found, and this video is an excellent example of this. Taken by the Nautilus crew on September 20, 2018, this video is rare footage of an animal called the pelican (gulper) eel in Papahānaumokuākea MNM. And this was only one of the animals observed!
As it traveled to Hawaii, the Nautilus also studied multiple
geologic features called seamounts, which are undersea volcanoes that
have not breached the ocean's surface yet. Before the Hawaiian islands
were, well, islands, they began as seamounts. Over a long period of
time, the underwater volcanic eruptions built up the seamounts until
they became a large island. These eruptions still happen, but because of
the "hot spot" volcanic activity near Hawaii, the volcano's position is
not constant. A new seamount, and future Hawaiian island, is being
formed right now off the southeast coast of the large island of Hawaii.
Its name is Lō'ihi, and its exploration has the potential to tell us
about the habitability of other places in our solar system. From the
website:
"The expedition of Lō'ihi marks the beginning of the multi-year SUBSEA (Systematic
Underwater Biogeochemical Science and Exploration Analog) Research
Program, a partnership between NASA, NOAA, and various academic centers.
Bringing together both ocean and space exploration teams aboard E/V Nautilus,
SUBSEA blends ocean exploration with ocean worlds research to address
knowledge gaps related to the habitability potential of other planets in
our Solar System."
A "gripper" used for collecting samples from seamounts. This novel
tool
was developed by the Jet Propulsion Laboratory, and is mounted
on the
ROV Hercules, one of the robots on the Nautilus expedition.
While it was around Lō'ihi, it documented the biological communities that live around the seamounts it observed. Because Lō'ihi is an isolated seamount (one that is not near any tectonic plate boundary), it is considered a strong analog for any kind of venting system that might exist on an ocean world like Europa, an icy moon of Jupiter. By collecting samples from fluid venting locations, geologists and biologists will be able to study the interaction between a seamount and the life that survives there. How cool is it that studying the environment around seamounts in the Pacific can tell us about potential life on other planets?
It is impossible to put the full scope and findings of the Nautilus mission into a simple blog post, but these are just a few of the highlights that happened in the past few months. If you'd like to read more or follow along with their live-streaming, the website is here: http://www.nautiluslive.org/
