Saturday, April 30, 2011

"Even our brightest students suffer with % point systems rather than #sbar"

I wrote my last post while sitting in my hotel room between "workshops" at the Colorado state FBLA conference, so I ran out of the room before throwing it onto Twitter. Then, two of my favorite edu-people out there did it for me, adding their own comments:



 
Then came:








Ever since the small discussion that ensued, in which I stated that I wasn't certain that students would really embrace this change, thoughts on these ideas have been bouncing around my head. And the more time I spend on this, the more certain I am that not everyone would be won over by the idea of SBAR.

Here's the two main reasons I can think of:

Reason 1: At first glance, it translates to more work and more accountability.

An example: I'm in a certain points-based class in which an assignment was supposed to be completed over spring break. It's a pretty important assignment--much of what we have done since then has revolved around it.

I have an "A" (insert eye-roll here) in this class.

And I never did this assignment.

We have accumulated enough points since then that the impact of this missing 25 points has been diluted. From looking at a grade sheet, you'd never know that I was anything but an exemplary worker.

Now, from the way I understand SBAR, there's no way I could pull that off.  My missing work wouldn't have been absorbed by everything else--and students know that. I've often heard someone say, "Oh, I already have all of the points, so it won't matter if I don't know what is going on for the rest of the year." (And that's almost a direct quotation.)

Because kids know that they can hide things they don't understand, many wouldn't want to give this up. After all, grades have become so important to many people (and I have to plead guilty) that often times we resort to "what gets me the best grade is going to be best."

Reason 2: It's new.

There. I said it. Students, at least around here and including myself, tend to be pretty conservative when it comes to massive changes. There was essentially unanimous disappointment ("Oh, man! That is so stupid!") about merging the high school and middle school. Even though it would make practical sense, many students do not want to merge the eight tiny school districts in a thirty-mile radius of La Junta. And multiple times this year, I've heard comments along the lines of, "I hate that new grading system of Ludwig's!" (Of course, then I typically jump in and ask why. I'm then often met with, "I actually have to work.")

The point is that, simply because we've been going along with this system for twelve or thirteen years, able to hide our weaknesses and our struggles, I don't think that we would embrace a change in the opposite direction.

Of course, I could be wrong. Let's hope so. 

Monday, April 18, 2011

Why I'm Glad I'm Doing This

Hopefully, by this point, the posts that I put up here seem to be somewhat thought out. Believe it or not, I do try to spend some time thinking about what goes on here and how efficiently and effectively it communicates with what I'm trying to say.

With that said, I do write these posts in two different ways. There are those that are triggered by some external event, which seem to be written as I watch this event happen, and those that I spend quite a bit of time developing because they explain my preexisting feelings about something.

But as I spend that time thinking about how to communicate my ideas, it's led to a complete paradigm shift. I can't just walk into a classroom anymore; I walk into a classroom thinking, "Oh, boy. Here we go. I get to not really learn anything and watch everyone else do the same."

Is this a good thing?

I suppose, in many ways, it is. After all, if I don't spend any time analyzing learning, I'm not going to be able to shift my own learning/teaching style. Of course, it would probably be preferable for me to find some nice way to tell the teacher that this is my impression of his or her class, but then...how do I tell someone that what he's been doing for longer than I've been alive isn't really that effective for me? I've been able to hide any sub-par learning behind the mask of points for so many years that it is expected that I will be able to excel in any class. Am I really the person to bring this to a discussion?

The answer is probably yes, but I haven't been assertive enough to do this yet.

With my little rant for the day out of the way, however, I really would like to say that I am glad that this year has turned out the way it has. I know so much more now than I did a few months ago--and I know there is a titanic amount left for me to discover.

So why am I here?

I like to think that, first off, I can provide my thoughts. I think that it is important to consider both sides of the desk in education. By doing this, I hope I can provide the perspective of someone who has not been to a teacher's college but still wants to know what can be done to aid students.

This brings me into my next point: Looking around the edublogosphere, I can't help but be a little jealous at what quite a few other students have. I really hope Frank Noschese's students know how lucky they are not to be in a classroom where their itinerary for every day is to watch videos. But because I have this knowledge, if I do end up as a teacher, I will have the tools I will need to avoid this in my own classroom. It's a miniature PLN for a sophomore in high school.

I already do some tutoring, mostly in math, my forte. And in the last month, my style's changed completely. I've gone from, "So here's what you do next" to "So what do you do next?" Although I'm not Dan Meyer yet, I think I've helped a lot more kids in this way--and hope be able to continue refining my ideas.

And that's why I do this.

Thursday, April 7, 2011

Graduating: It's Nice

Well, today, I had to make a few quick decisions, the long term effects of which will be, hopefully, my own high school graduation. To make a long story short, I was supposed to take our school's "World History" class this year, which is, if you want to be nit-picky about it, required for graduation. Somehow, I slipped through the cracks and this class was not on my schedule.

Today, in my monthly meeting with our district's GT advisor (which has, over the year, been christened "Nerd Lunch"), I pointed out this minor technicality and gave what I thought was the best solution. I felt that, since one of the seven classes I would be taking next year would be a class at our community college instead of one on our school's campus, I could then use the open hour this produced to take World History. Basically, I thought I could take eight classes in a day instead of the regular seven.

But of course it couldn't be that easy.

Instead, we ran into more and more scheduling conflicts, and eventually decided that the "best" outcome would be for me to take a "hybrid" course (which, being a different course, is theoretically far more rigorous than World History) through our community college--OJC. This means that, although it would primarily be an online course, I would also have occasional contact with the professor.

So, at this point, I have two main reactions:

Reaction 1:  What will this be like? 


Over the last year, I have learned an incredible amount simply by reading around various edublogs. I have started analyzing every moment I spend in a classroom to see if I am really learning. Of course, this may be getting to the point where it becomes a distraction--but it's a distraction I can live with because it is providing me with the tools I will need if I hope to, one day, be a halfway decent teacher.

Now, as I try out this new medium--a "hybrid" course--I'll be able to carry this newfound insight with me to see how effective it really is. It'll give me a firsthand chance to experience what I try and think about every day, and I'll be able to write about it without having to worry about hurting anyone's (read: a teacher's) feelings because I won't be "learning" from a teacher.

Reaction 2: Is this really the best way?



Bill Ferriter actually said pretty much everything I've been thinking in this post, but I'll go ahead and rehash it. Throughout the entire conversation, we were looking at what I absolutely had to get in before 2013--and it meant a lot of time spent in classes that would probably not be beneficial. Now, we did start to take steps in this direction--we're going to ask the department chair to waive the World History credit for the hybrid course.

But it's not far enough.

If we could keep going in this direction, somehow customizing the curriculum for each student's individual needs and preferences...that's when I think we could get some real work done.

Now, I recognize that, logistically, that's a borderline ridiculous statement. As far as I can see, there's no way to pull that off in a way where every student is in a class beneficial to them--after all, who gets to decide which classes are "beneficial"? Then, even if that could be worked out somehow, we'd have to find a way to actually create a schedule for which that actually worked.

Am I on to something, or am I just an idealistic idiot? 

Structures, But Not Architectural

WARNING: Biology post ahead!



Recently, we've been discussing the components of DNA and how they fit together to create the genetic code. I also found this nice, although admittedly outdated piece [from the University of Arizona ;) !] that aided me in these discoveries.

First off, we have to understand that DNA is a polymer, meaning that it is comprised of several smaller pieces (the monomers) that have joined together. DNA, however, is special, so we can't just call its components monomers--they have their own names. Each monomer is called a nucleotide, and when combined, you get a polynucleotide.

Make sense so far?

Now, there are four nucleotides, and they're all mostly similar. Each one has a 5-carbon sugar (deoxyribose), a phosphate group, and a nitrogenous base. The only difference between the four is in that nitrogenous base. You're probably familiar with the notation for these bases:

A=Adenine
T=Thymine
C=Cytosine
G=Guanine

Let's take some time to examine the bases themselves in more depth.  Two, A and G, are purines, while their counterparts in the DNA sequence, T and C, are pyrimidines. (After a few minutes of Googling...I'm not even going to try to define those terms. I like going in depth, but there's a limit.). Adenine and guanine both have 5 carbon atoms and 4 nitrogen atoms, these atoms are both numbered according to their positions, and both have an NH2 molecule attached to the rings of carbon and nitrogen. The only real difference between these two is that guanine also has an oxygen atom attached to the C6 atom and that the NH2 is at the C6 atom in adenine, while it is found at the C2 atom in guanine.

Cytosine and thymine have are also quite similar to each other, but only consist of one C/N ring, instead of two as the other two bases did. They both have 4 carbon and 2 nitrogen atoms. In fact, the only difference between the two is that thymine has an extra NH2 molecule instead of two oxygen atoms and that guanine has an additional CH3.

We've been focusing on the bases, so let's take some time to examine the backbone, if you will, of DNA--the deoxyribose phosphate. This structure has 5 carbon atoms, two hydroxyl groups, and one lone oxygen atom. These two hydroxyl groups bond with the phosphate groups to build the backbone. This means that there is a polarity to the chain--it goes from 5' to 3'. (Interestingly, compared to ribose, deoxyribose lacks one hydroxyl group, hence the name "DEOXYribose.")

Ok. So, now, we have one side of the DNA chain built. But DNA has a double helix shape, as Watson and Crick discovered. To explain how these sides join and why they twist, we have to examine the bonds within the DNA molecule. First off, when two of the sugar-phosphate "sides" we've been discussing combine, they do so in opposite directions--the two 5' atoms are at opposite ends of the combined chain. Now, along this backbone, the phosphate and sugar are covalently bound--pairs of electrons are shared between the two molecules. The base pairs, however, use hydrogen bonds (remember them? They're caused by charge differences between hydrogen and other atoms.) to join. This is particularly useful because when it is time for them to be separated for RNA synthesis (more on that soon!) these bonds can be easily broken. It is also interesting to note that, although adenine and thymine bond with two bonds, cytosine and guanine use three bonds.

More coming soon! 

Wednesday, April 6, 2011

Synthesizers: They're in Your Cells

This marks two posts in a row for Biology! Don't worry...I have a few personal ones stewing away.



Pretty much everyone knows that DNA is in your cells. That's a well known, widely accepted fact.

Not as many people know that proteins do the dirty work of the body. When you look in the mirror, you are seeing the result of the work of proteins.

But this means that, somehow, the information encoded in your DNA has to be used to make proteins. How is this done?

The answer to this question is the RNA molecule. RNA is somewhat similar to DNA, but it has a few important differences. First off, uracil is used as a base instead of thymine. (Both uracil and thymine are pyrimidines, but uracil is missing a methyl group.) Then, the sugar used in its formation is ribose instead of deoxyribose. RNA also only has one strand instead of DNA's two.

Now, there are three classes of RNA. Let's take some time to examine each.

Messenger RNA (mRNA)


Messenger RNA is what carries the information from DNA to the ribosomes to create proteins. It's almost like the photo negative--every base in RNA is the complement of the base in DNA. For example, a DNA sequence of

ATGTGCA

would be transcribed as

UACACGU

(Remember, RNA uses uracil instead of thymine.)

Then, the strand of mRNA exits the nucleus and heads to the ribosome. Here, it meets up with...

Transfer RNA (tRNA)


Transfer RNA is a single strand of RNA that curls back on itself, with a location for an amino acid. It's typically portrayed in textbooks as a cross-ish shape, like


This isn't the actual shape of tRNA, but this particular representation is useful for several reasons. First off, it shows the "intramolecular base pairing" in the arms of the cross--G and C, U and A. It also is a "charged" RNA, meaning that it is carrying an amino acid. Finally, below the molecule, we can see the "codon," and at the bottom of the molecule itself, we have the "anticodon." Codons are groups of three bases that each have their own specific meaning. (Because there are four possible bases and three bases in a codon, there are 43=64 possible codons.)

Let's track a certain sequence of three bases through transcription (where DNA is transcribed to RNA) to translation (where mRNA is used by tRNA to create an amino acid sequence). Imagine that the sequence AGT is sitting on a DNA molecule. When transcribed to mRNA, it becomes UCA (remember, RNA becomes the complements of the bases in the DNA). This mRNA exits the nucleus and goes to the ribosomes. In the ribosome, it is paired with the tRNA carrying its anticodon, AGU. (As a matter of fact, this would result in the protein serine being added to the chain.)

Then, this general process continues for all of the codons. A series of amino acids is compiled, and finally a protein is made. Now, remember, all of this is happening in the ribosome, and an important part of the ribosome is

Ribosomal RNA (rRNA)


The ribosome is comprised of two subunits, both composed of rRNA. These two components are creatively known as the who on earth named these things large subunit (LSU) and the small subunit (SSU). When mRNA enters the ribosome for translation, it slides between the two subunits. Ribosomes have three binding sites for tRNA to enter as the mRNA is translated (known as A, P, and E). The A site binds with a charged tRNA--one that is carrying an amino acid. At the P site, another charged tRNA is waiting--and the amino acids of the P tRNA and the A tRNA bond. The tRNA that was at the P site moves to the E site, leaving its amino acid behind, and the molecule occupying the A site moves to the P site. Another tRNA molecule comes in to the A site, and the cycle continues.

That's a brief overview of the various types of RNA!



I have a confession: Over the past month, my writing on science stuff has seemed increasingly dry. I haven't liked it, and I don't know why. Has anyone else noticed this?
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