FBC Adult Sunday School – February 13, 2022

them to have a certain amount of shape. In these proteins, just see what happens here.

It is very important to note that the T -City has a constant motion inside of itself.

Destruction, desolation, burning, transporting goods from one place in the cell to another.

It sells all kinds of goods, plus several roadways. Transportable on these roads.

It sells these proteins. Humanity is one of these organisms. All the cells in your body depend upon these tiny, large proteins to organize, to dominate, to multiply, and to communicate with other cells.

Let's start with how we began. Development requires molecular motion and motor proteins.

Every cell in your body requires them to survive. What we know now is that a human practically has two legs, and these legs are able to coordinate a walking motion along a track.

That track is called a microtubule, and the mechanism of the microtubule is called micrographed walking action.

While the kinesin is walking along this track, the other end of the kinesin gets a little bit of cargo.

These microproteins are perfectly conditioned relative to their size. They move as fast as a car on a freeway, but they're four times more efficient than your car in converting chemical energy into motion.

I remember a case in 1984. I was 25 years old at the time of the graduate school.

I was interested in the transportation system inside the nerve cells. What makes nerve cells so interesting is that they're extraordinarily long cells.

For example, part of the nerve cell, that's the nucleus where the DNA is, is located in your spinal cord, but it can extend all the way, for example, to your foot.

All of the building blocks for that nerve cell are made in your spinal cord, and all the building blocks have to be shipped to the very end of that nerve cell a meter away.

There had to be some kind of transport system that was moving these building blocks inside the nerve cell, and I wanted to know how that transportation system worked.

After we got this transport to work in this test tube, the hunt was on then to find the key molecule that was responsible for that movement.

We eventually found it, and it turned out to be something completely new that no one had ever discovered before.

Watching these movements under the microscope was fascinating, again, to figure out how does this motor actually work?

How does something that's a millionth of an inch in size generate that motion? I've been at UCSF for about 10 to 20 years trying to figure out the answer to that question.

We know about kinesin now. We know a lot about how it moves, but there's still so many fundamental questions that we don't know about how all this motility is regulated, and it's how all the growth happens around the nerve cell.

... Kinesin is a protein.

Yes. Mitochondria.

Okay, kinesin is a protein. If you caught some of what he said, it took them how many years to kind of get their head around this?

20. They discovered it circa 1985. Did you hear all the questions that he said we still don't know what regulates this?

Yes. Do you think that we still need to develop a super -micron telescope?

I mean, have we seen everything that's... It's kind of like a... Isn't it like a telescope or a

Hubble telescope we've seen so much now that James Webb... Have we seen all of this?

Has God created all of this? I think the answer to that is yes.

They have so refined the tunneling and scanning electron microscopes, we can get down to the resolution of an atom.

If we can get down to the resolution of an atom, then we can basically determine all of the little structures inside a cell.

The problem is figuring out what they do. Because when you look under a regular microscope, you can actually see live organisms.

When you do tunneling and scanning electron microscopes, those are all fixed.

So in other words, rather than bouncing light off of them on a regular microscope, they're using electrons.

To make that, that has to be a fixated specimen. So it's not moving or live.

So one thing that I'm not going to talk about is how DNA split and get pulled off by little structures called the centrioles.

Because it's just too hard to get it across and we would just spend an inordinate amount of time talking about it.

That structure, those centrosomes and centrioles are made of nine sets of three microtubules that kind of looks like a sheriff's star.

And they spent about 15 years looking at thousands and thousands of pictures, slice, slice, slice, slice, slice, until they finally figured out what it does.

And the answer, how did those things work? Evolution, silly people.

So this, that's an excellent question. When I was, if you go back to about the 19, well, if you go back to the time of Darwin, there were, at that point in time, about 180 vestigial organs.

Does anybody know what the word vestigial means? It means that they thought it was something that was there for no reason at all.

No reason, yes, it's part of the throwaway, the ongoing thing of evolution, right?

And that was proof for evolution. Those 185 vestigial organs, how many of those 185 are left today?

Zero. The appendix was vestigial, the thymus gland, which is arguably the most important gland of the immune system, was vestigial.

The pineal gland, I remember in school, they said the only purpose for the pineal gland is that it calcifies, it helps them find things in the brain.

Okay? So we were pretty stupid. So that list has gone from 185 to zero.

Okay? That's organs. Now we're talking about new discoveries. So now as we look at, as they look at these little objects, they've got to figure out, what does this do, how does it work?

And he was working on that 20 years. Did you see this, folks? The amazingness of all of this.

So anyhow, mitochondria. Good question. And by the way, on some of the things that we're going to be looking at, there's several videos that I want to show you.

Hopefully we get that today if I don't talk too much. You'll see little things called nanometers.

A nanometer is a billionth of a meter. So again, really, really tiny stuff as we look at these.

The mitochondria. So the mitochondria are responsible, and the average cell has 1 ,700 of these.

Muscle cells have 3 ,400 of these, plus all those other little structures that we talked about.

These things are responsible for producing a chemical known as ATP or adenosine triphosphate.

Very simply, ATP is a rechargeable battery. ATP breaks down into ADP and gives off energy.

And then the mitochondria take the ADP, adenosine diphosphate, put energy into it, stick a phosphate group back on it, and make

ATP and recharge the battery. Do you get it? So rechargeable battery. If you are active during the course of a day, you produce roughly your own weight in new

ATP molecules. Is that like just walking around, breathing?

Is that like running a marathon? Well, if you're like Kevin, if he's out there on a really, really busy week doing a lot of lifting, he's going to do his own.

The Slobovian who's kind of walking around and sitting, they might produce a third to a half their body weight in ATP.

But the idea is, again, you average 1 ,700 per cell, and these things are kicking this out left and right.

I was going to give you the number of molecules a day, but it's too hard to remember.

In other words, 1 ,700 of these per cell kicking this stuff out.

Rechargeable batteries. Just going and going and going. Glycosomes.

This is another organelle. I have to apologize for the notes, not these set.

But previously, you guys do have these, right? Every time I go to print, you will get a number 1 on the bottom of the page.

Go page 1, 2, 3, 4. Don't pay any attention to page numbers. Follow this, and this is number who?

Slide? 54. If we run out of slides today, let me know,

I got the third handout up here. And if you need stuff from previous, let me know, I'll get those to you as well.

So lysosomes. These are little sacs inside your cell that contain digestive enzymes.

Now catch this idea. So your cell has the ability to kind of open its cell membrane one layer at a time, and pull stuff down in, right?

So it can catch stuff because it's sitting in intracellular fluid. It can reach out and catch stuff and just pull stuff in.

If what it pulls in is basically liquid, we call that a vacuole. But if there's a little chicken wing going by, you know, chicken wings don't go by, but if it's pulling in stuff, and it's hard to digest, okay, so it reaches out and the pasture is swimming by, and it pulls it in, and he's a hard nut to crack.

So this lysosome will come over to this vesicle, and it will literally dump out digestive enzymes on that structure, and dissolve it so that you can use the nutrients of it.

So there's over 40 different kinds of digestive enzymes contained in these little sacs.

All those digestive enzymes are proteins, which means they had to be made.

Where did all those come from? Evolution is a wonderful thing, people. It just gets deeper and deeper.

Cytoskeleton. Okay, here we go. So what they're showing you out here, this is that phospholipid bilayer on the outside, okay?

So you have this great big circle going all the way, just a couple of millions of an inch thick.

Then, inside, there's basically two components. You have these tubes called microtubules made of protein, and then you have cables and ropes called microfilaments.

How many of you old people remember Tinker Toys? Just think

Tinker Toys, guys. And who's running up and down these microtubules?

The motor proteins or the transport proteins. So this is a schematic of what it looks like.

This is a photomicrograph from an electron microscope.

Do you see the... Keep doing that. So do you see these larger guys?

Those are the big tubules, and then those smaller green structures are the microfilaments.

Are your cells loaded with that stuff? Yes. Along with how many mitochondria?

1 ,700. Along with that membrane that goes back and forth, the endoplasmic reticulum, along with the vacuoles and the vesicles.

Just are your cells full of it? They are stuffed with stuff.

Got it? It's just crazy, folks. Okay, irreducible complexity.

Are we still good? Find it? Okay. So here's the idea, and this has been, if you get into the evolution creation debate, this has been kicked around.

This was essentially developed by a guy named, by the name of Michael Beatty, and this is it.

A term used to describe a characteristic of a certain complex systems whereby they need all of their individual parts in order to function.

And I'm going to give you some examples of some of this. It's the idea of this.

You can go back to the old engine. Now, do you need a piston and a block and connecting rods and all of that stuff for the engine?

Yes. If you take any of those, it won't fail. Now, do you need an oxygen sensor for an engine to run?

Not necessarily. You know, it just helps with emissions. So the idea is you can take things, and you've got all these parts, and if you take a single part out, it's not going to work.

And so Michael Beatty, I think it was, used the idea of a mousetrap. So you've got your base plate, and you've got this, and you've got the hook, and you've got the spring.

And it actually, when this whole thing was being debated, and it got to the court systems, whether public schools could teach evolution, creation, whatever, some guy had his little, he came in, and he had his, he took out one of the clips, but he used the mousetrap as a tie holder.

And he said, see, I took a part out, so irreducible complexity doesn't exist. He was just being really, really foolish.

He missed the point. I love to hike. If you're walking down the path, and you come across a rock on the path, do you think anything of it?

No, other than don't trip on it, right? And a rock is pretty neat.

But if you come to an area, and we've all probably experienced this, and you see an area where you have like four flat rocks stacked on top of it, does that pretty much prove that somebody was there?

Yeah. How much work power did that take? Don't have to be a mathematician to figure that one out.

But even something that simple, you will say that there is a design to it. Do you follow me? Everything we've looked at is a little more complex than that.

So that's the idea of the irreducible complexity. So then, in my absence last week,

Pastor opened up a whole other can of worms. So I'm sitting down there thinking,

Oh no! No, actually, if you didn't hear the Sunday school lesson of last week, you can listen to it.

And I think you've got this accurate, Pastor, so if I don't, don't say anything until afterwards.

But basically, he went in and did a phenomenal exegesis of Psalm 139, and he looked at several of the verbs there.

He looked at a couple of them. So, in verse 14, it talks about being wonderfully made to make distinction.

Make distinction. Now, is that applying to us individually, that I'm distinct in certain regard than all the rest of you?

For you, for me, fortunately, right? Or could it also apply to species? The Hebrew's not overly clear, but we'll talk a little bit more about that.

Being made to craft an intricately woven instinct

DNA. So we're going to expand on this, but do you follow me? Those are the three verbs, and I hope

I didn't do injustice to that. So, being made to craft. Of the crafting of the structures in the next few slides.

Again, we're talking at the cell level, 125th the diameter of the human hair. So, let's talk about the hemoglobin molecule.

We still good? If I run out, let me know, and I'll get to the next one, but I think that's up to the flagella. So, the hemoglobin molecule.

So, those chemists, that's the chemical formula for a hemoglobin molecule.

You have four times 738 carbons, 1166 hydrogens, 312 nitrogens, 203 oxygens, two sulfurs, and a little iron.

So you take four of those groups, and you have a hemoglobin molecule, right there.

So that's just a rough schematic, and then what they do, over here, they enlarge it, and those four little iron molecules, that's the actual hemoglobin.

That blood cell in your body has 250 million of those in it.

This is red blood cell strokes. This is red blood cells. All proteins.

What's a ball protein? I said, I found them. No, I said, I don't know what they are.

So, I'm looking at these things. Now, does this ball protein, and we've got a great little video, did you see this video?

Just phenomenal. Some grad student put this together. I love stealing other people's information.

So, do you see how this looks like a basket that opens up? And you see all this stuff?

It's like crochet. Kind of. Okay, so here we go.

Don't write notes down on this. We won't keep up. Because it's resemblance to molten cathedral sealants is one of the largest rapid nucleoprotein structures ever discovered.

Although it is one of the largest structures of this kind, at nearly twice the size of the eukaryotic ribosome, ball organelles were not discovered until 1986, and new information is still being gathered about its function.

A ball organelle is a barrel -shaped structure consisting of two symmetrical halves, with a total content of 96

FEP chains forming the outer shell, 10 minor ball proteins, and 6 copies of small non -translucent

DNA molecules. All of these components come together to form the organelle, with the minor ball proteins holding the major ball proteins together in a loose, flower -like structure with 8 petals of 6

FEP chains each. These loose structures then hold tightly together to form the structure of the large hollow center cavity.

This cavity, large enough to hold a eukaryotic ribosome, suggests a function related to the transport of cellular materials, but the precise function has yet to be experimentally defined.

We will go over the most popular theories of ball function later in this video. A study recently revealed that ball structures can form solely from the major ball protein without any of the minor ball proteins or the untranslated

RNA. This finding supports the theory that the major ball protein plays a vital role in ball formation and structure, so let's explore how the

MPP creates these ball structures. The MPP is an asymmetrical protein chain consisting of N -terminal domain with 9 small repeating units and a

C -terminal domain containing one alpha -helical shoulder unit. The C -terminal domain of the MPP holds each of the peptides together at the tips of the ball structure using coiled -coil interactions between the alpha -helical shoulder units of two

MPP strands. These coiled -coil interactions are similar to those in the keratin structure that we studied earlier this year.

The MPP strands are held together by hydrogen bonds between the backbones of 32 amino acids involved in each alpha helix.

This creates a section of tight coiled -coil associations between MPP units that sub -wind around each other and allows for the close association pattern of the

N -terminal domains that form the outer ball shape. The N -terminal domains with P -domains each contain 5 to 7 beta -strands and these repeatings are strung together in a linear fashion that allows the beta -strands of each

MPP chain to interact with those next to it and cross beta -shapes on top of each other. The beta -strands of the

N -terminal domain form the main outer barrel shell of the ball structure as well as what are called EF hand loops.

EF hand loops are alpha helical structures with two finger -like branches that coordinate to calcium ions.

The calcium -binding EF hand loops are formed by a 40 amino acid alpha helical structure on the N -terminus of the

MPP chain. Calcium's role in ball formation is not entirely known but it is predicted that it assists in closing the loose flower -like ball intermediates into the tightly closed ball barrel by coordinating with the oxygen atoms of the

EF hand loop side chains. Overall, it is a combination of the intramolecular coiled -coil associations and the intermolecular

EF hand loops that allow MPP to form the tightly packed ball shell. Although the exact function of ball structures is not yet known, the structure of the major ball protein implies a transport function as the coiled -coil interactions between MPP peptides allow the ball to form open and closed conformations, which in turn allow it to encapsulate or release molecules for transport.

The tight association of MPP strands is essential in forming the outer shape of ball structures so that these structures can encapsulate molecules for transport that would otherwise be too large or too toxic to be transported by vessels.

This structural analysis of the major ball protein as well as experimental data showing that over 90 % of ball structures have been localized in the cytoplasm suggests a role in cytoskeletal and nucleocytoplasmic transport.

Faults in the cytoplasm have specifically been located in cytoskeletal elements and cyclotron vesicles, which suggests a role in transport of cellular materials through the cell for excretion.

Perhaps a more interesting function of ball structures is their ability to relocate from the cytoplasm to the nuclear envelope.

This relocation combined with ball's ability to form either a barrel shape or two separate halves suggests a mechanism for encapsulation of cargo to be transported to and from the nucleus by docking at the nuclear pore complex.

This theory is the main concept behind the current association of ball particles with multi -drug resistant lung cancer cells.

In 1993, ball structures were found to be overexpressed in multi -drug resistant lung cancer cells, which makes balls a target for chemotherapy research.

Ball researchers proposed that balls prevented chemotherapy drugs from reaching their targets by removing the drugs from the nucleus and excreting them from the cell via nucleosidoplasmic transport.

Later experiments using ribozymes to break down MPP particles showed increased sensitivity to some chemotherapy drugs, which makes balls a current target for improving the efficiency of chemotherapy drugs in resistant tumors.

Although more research is needed to determine the normal function of balls, whether or not they can bind to drugs, and whether or not balls transport drugs out of the cell or simply dissociate with exocytotic vesicles, the discovery of balls and the major ball protein has led researchers to determine a new clinical marker of multi -drug resistance and provide a possible new avenue to sensitize resistant tumors to chemotherapy treatment.

As more research unlocks the potential of ball structures, we may see a new and more effective...

I swear people don't want to sell biology. Any questions?

Hearing none, we'll move on. I mean, the way that things stick together, is it like before it gets better?

No, not like Chinese handcuffs. No, when was this discovered again?

Okay, so when you were looking at those pictures of the actual photomicrographs, that's electron microscopy.

Really, really tiny stuff. And they're looking at these little blobs and they're saying, what is it and what does it do?

So that was about 1985 or something like that.

So we are 20, almost 20... Yeah, a lot of years, thank you

Matthew. We're a lot of years and they're still saying, what doth it do?

So they're thinking... Did you see all the structure there? All those... So they were talking about proteins with the alpha helix chain, that just means it's got a little curve with a beta or alpha curve to it.

And then how all those little guys get together and form bigger things and then they start doing the little long crocheting or whatever you want to call it.

And you end up with this barrel that evidently has the ability because they can see that.

Now, one of the theories is that what it will do is a vesicle or a vacuole are very, very thin.

They're made of a phospholipid bilayer. So possibly because these are much stronger structures they have the ability to transport noxious or cytotoxic substances out.

They can also potentially go to that nucleus, we'll talk about that with nuclear membranes, and take stuff out of the nucleus and get rid of it because your cells are constantly dumping stuff it doesn't want right into their backyard.

So are vaults a hindrance to chemotherapy? What they're saying is potentially what was happening is these vaults were grabbing some chemicals from drug therapy and getting rid of that stuff because it was noxious.

Normal stuff does about the only thing that will go through those nuclear pores and get out to the rest of the cell is

RNA which we'll eventually talk about. And so now what they're saying is let's use these for our advantage, let's design chemicals that the vault proteins will grab at the surface and take and dump in.

Do you follow me? Look. How crazy folks.

How crazy is that? Just amazingly. And you can share that with people and they'll say would you explain how a vault protein or a flagellum develops?

And what will they say? What's their bumper sticker? Hi, man.

Chance. And sometimes they just want to say, but that's coming actually from a position of pride if you do that, right?

Because these people, they don't know. So just be patient with them.

Share a few of these things. I mean, you can Google this with somebody and say, by the way, and if you want any of these references on the videos, let me know.

Try to remember next time to include them in. Good questions. Or comments.

So let's, as we wind down this morning, let's look at the flagellum. The flagellum.

But do you get the idea of crafting? Did you see the crafting in the vault?

Now we're going to see crafting here. How many of you have ever made an electric motor? Just two weird people.

So when I taught physical science out at Faith, this was a ninth grade course, and what we did is we actually had them made little motors.

So you know electric motors? Yeah. They power the vacuum cleaners and everything else basically.

Okay. So you've got this little part right here. So here is the cell membrane of the cell.

You with me? So down here would be inside the cell. Out there is outside the cell. Remember that here is your phospholipid bilayer right there.

So you've got a hole in the cell membrane. This whole thing spins. You with me?

And this part here and this part here stay stationary. So you've seen a motor before.

You've got the part in the middle that's spinning. That's called the rotor. And then the part on the outside is called the stator.

And basically in a regular motor you will have either AC or DC current.

And you will change the polarity and oops, sorry. So we go back to here.

What you will have here is this thing because in electric motors it's surrounded by magnets generally fixed.

And then you have alternating current to the inside to reverse it. But it just keeps spinning. This little bar here, this flagella, now in humans only mammals have these and of course they're found in the sperm, right?

Bacteria also have that. These little guys have the ability hang on to your hat, have the ability to spin at between 100 and 150 ,000 revolutions per minute.

They have on -off switches and reverse switches. They can stop and reverse in order of a turn at speeds of over 100 miles per second.

They can stop and turn at speeds of over 100 miles per second. They can stop and reverse in order of a turn at speeds way out.

You about. Maybe Ma 'am The knitting together, just incredible, so let's pray.

Father, we just have to pause and reflect again on your magnificence.

The incredible structure and creation of the cell, and it took us so long to even discover, and who knows what else is there for us to discover to see your handiwork.

So Lord, use these thoughts and use the truth of your word to spur us on to even greater appreciation and more true and acceptable worship.

Thank you for the technology that allows us to see this stuff. Help us to use this information also to be more bold in our witnessing as we come into the lives of people.

So I ask that you'll go with us in time of worship to follow. That it would be just a wonderful time worshiping together, we pray in your son's name, amen.