Episode 12: A Familiar Journey

Hi everyone, welcome back to the meme blog with a little bit of protein research on the side. To start off today I would like to introduce you to a Youtuber than turned into a meme god, IdubbbzTV. Originally a man with humble beginnings, Ian Carter started off his career in Kickstarter reviews and Bad Unboxing. But with the introduction of Content Cop, Ian's jokes and gags reached a new height as he dived into sewers and started throwing things erratically.

In terms of today's research blog post, I will have to provide a timeline accurately displaying my plan for the implementation of my research. I just turned in my research proposal, so now would be the perfect time to expand on the timeline I have.

First off I am meeting with Dr. Ozkan, PSF 3rd Floor fam and my consultant. In an Ideal world my research would start like this.
Jan 2: Meet with Dr. Ozkan
Jan 2: Gain access to the ASU supercomputer, select proteins, prepare them, and start the initial REMD trials through the ASU supercomputer with PRS (brownian kicks)
Jan 3-5: Troubleshoot the failures in the computer program that will arise due to a lack of knowledge or bug in the system. (Has happened almost every time I have ran trials)
Jan 10: Download the data from the computer and meet with Dr. Ozkan again to verify the results. Analyze the DFI profiles and determine the functional sites of the protein and how they change with mutations. The analysis will be managed here. DFI tracks the movement of each amino acid after a perturbation is run through the molecule. A matrix is generated, and then I analyze the changes in structure to determine the most important mechanisms. I am a little unclear on how to search for these mechanisms, so I will have to reread the ending of a couple of papers and consult with Dr. Ozkan, but I do know that it is mainly determined by the computer so there won't be a need for quantitative analysis.
Jan 11: Repetitions if necessary, and maybe more active sites (determined by Rheostat Toggles)
My research should not take too long. However, this is based on the assumptions the trials will run smoothly and end under a week. There may be technical difficulties, but I believe the trials can be finished by late January, early February.

Episode 11: Pitching fast balls

This week we had to pitch our ideas, so here is mine. My pitch is 3 minutes the rest is just some comedy.

Episode 10: Returning Legend

Welcome back to the blog, we will first begin with the dankest of memes. Today I have the legendary rapper Yung Lean. Lean rose to fam with his bucket hats, AZ iced tea, and general meme filled raps. An example is a line from Kyoto, "I got an empire of emotional, Squad see me crusin', crusin' in my go kart, I'm War ho, I'm Warhol, I'm Wario when I'm in Mario Kart" Although he is now far removed from his meme days, he is still a figure within the dank community.

My methodology will be pretty chill probably. I gonna start off by preparing LacI with several different mutations determined from other studies I've looked at. Then I'll run an REMD simulation on these proteins, simulating the mutated protein at several different temperatures. REMD is just the program I will be using. After that, I will introduce a random brownian kick which will send a reaction wave down the molecule. After the wave is sent through the molecule, I will use a DFI analysis to evaluate the change of molecule positioning. Then I plan to define what changes I am looking for in order to better understand the procedure. It shouldn't be too bad, but who knows anything is possible at this point.

But I am also looking to include a lay audience so I will have to avoid many of the pitfalls of the research papers I have read, which includes technical language, reliance on credentials, no limitation discussion, and a lack of explanation and justification.

Overall, I am very confident in my method because it is similar to one of my professor's papers. The random brownian kick and DFI analysis will help me analyze the reactions of the LacI protein. Hopefully i will be able to obtain meaningful results. However, I will have to justify and explicate the methods thoroughly because the technical information can bog down the reader and hurt the understanding of the project. I am also unsure of what I am going to define as a "significant change" within the protein structure. I will have to consult with my PSF 3rd floor professor because she has a good understanding of the changes in protein functionality. I am also unsure of the timeline required for my project, but I am sure the data will be collected in a timely fashion. Another challenge I face is converting technical terms into readable sentences for the everyday man. I hope to correct the short comings of science professors with an understandable paper.

Episode 9: MIA 2 months

What is actually happened after I redid my sources

Hello fam, I'm back after not blogging for like a solid month and a half. And of course I am bringing the dankest of memes. Today I have the one the only living legend, Filthy Frank. Filthy Frank is a legendary internet superstar. He is the person who started the Harlem Shake, but he is also responsible for many diverse and very dank memes with topics ranging from Japan to Vegans.

My literature review was the solving of what seemed to be endless doubts. At the beginning of the process I'll admit to being very cocky. The topics I initially researched were on the general topic of protein folding, but not actually on the focus of mechanisms. And I never really realized it until I met with my Professor, Dr. Ozkan PSF 3rd Floor Fam. I had been focusing too much on some unfolding techniques I heard vaguely before in my lab and I left out some of the basic biology required to understand my topic. So for my annotated bibliography I scrapped a solid 14 sources, and found new ones, resulting in a completed base for my literature review. This was probably one of the hardest parts of the project because creating the foundation of my research is the most abstract task in AP Research. For similar reasons my first outline almost no relation to my final outline, which is probably why it was better. The outline was one of the highlights of the first trimester. I finished that thing hours before the deadline and slept well before the due date. It included around 4k words and plenty of depth into protein folding.

Ozkan when she saw the first outline

When cutting down the outline, many subtopics were cut out. This narrowed the focus of the literature review, saving the word count and the methods section. Writing the literature review really helped me translate my ideas for a general audience. Although I knew what I would be doing in my research, I did not know how to grasp the literature surrounding my topics. The whole process of the lit review helped me understand the concepts behind protein folding.

With the base of all my research completed, it is now time to shift into second gear and tackle the methods section. I am pretty confident about my methods section, as I know what I am going to pursue. However, the details need to be ironed out and I have to understand all the programs I am going to be using. Now that the most difficult task is over, it is now time to complete the second hardest section of my research paper, the methods.

TIME TO STOP PANICKING

Episode 8: Let the proteins fold, Energies flow, It feels cold, Going real slow

The meme world has been rocked by the Anti Defamation League. Pepe the frog has been branded as a race symbol by the ADL, due to alt-right individuals using it in a hateful way. However, in the definition provided by the ADL itself they specify that most Pepes are unbigoted. So is it unnecessary to brand Pepe as a hate symbol if a small group of people use it in a racist way. RIP Pepe 2010-2016.

I was asked a few questions about where I am on my research project. I thought I'd answer them here. I am feeling really confident about my method of analysis, excited about researching, and happy that I have useful sources. I am super confident about my method and my project after Oct 22nd. I am very informed on the protein I am investigating and the historical progression of protein folding. I'm pretty excited to get to the work and run the trials, but I got this lit review in front of me. This is something scientists don't really do unless its a giant report, so it is intimidating to finish.

Driving in neutral is the significance of the project and my research question. I feel like I can make a decent significance for my analysis of mutations of LAC1 affecting its dynamic structure (if I mutate this protein how does it affect its flexibility, and how does that flexibility affect the function of LAC1). My research question is also in neutral again, because I need to figure out the metrics of my analysis methods and why I am looking at certain positions. I probably need to manage my time slightly better, but I am juggling my college apps with my other homework right now. I need to buckle down and knock this things out this week.

I feel terrible about the literature review. I need to make a connection between what a protein is and why it matters. Then I need to connect that to the history of protein folding and the introduction of dynamics to the study. I am pretty terrified of how to organize my literature, but I guess that is what the outline is for. Hopefully I can talk to someone this week sooner or later, because I am terrified of that also. I plan to finish a decent outline of what I currently have by Tuesday, so I need to get feedback on this so I can carry on without doubts about my foundation. Because I don't wanna be that guy a week before its due realizing that half of the work I did is useless (like how I felt leading up to the bibliography (I scraped at least 11 sources)).

Episode 7: Snapback to Reality

This week a Japanese music video has taken flight. PPAP has taken the internet by storm. Pen Pineapple Apple Pen is simply the best. Memetastic. This old man is balling out of control.

Hours after axing like 12 sources and literally gathering another 14 from scratch over the weekend (exaggerating). My paper looks better.

My research question is 

Do certain changes at the conserved positions of LAC1 significantly change the function and dynamics of the protein?

1. Scope: My scope is narrowed to LAC1 and the position I will mutate is at 52 on the LAC1 chain. I chose 52 because it is the most conserved position on the protein according to one of my studies. I will consult with my professor on the position number. My scope is manageable, I can even look at more positions in different levels of conservation.

2. Definitions: I need to define, LAC1, conserved, dynamics. I do define them in my literature review.

Certain proteins block the DNA transcription. These molecules are called repressors. The function of the genes that lac suppresses is to code for proteins that break lactose into glucose, galactose, and other sugars. Lac 1 is a repressor. Lac repressor prevents the creation of Beta-galactosidase, which is the enzyme that performs the first step in lactose metabolism, making glucose and galactose. Conserved positions are segments of a protein that are essential to the structure of a protein. Dynamics are the movements of the protein. An assumption may be that conserved positions are important to look at, but its justified in the definition.

3. Variables: The function and dynamics are variables that I will analyze

4. Researchability: 100%

I am going to work with the people who created DFI, and I will use DFI to analyze the proteins. DFI will show the changes in the dynamics of LAC1

5. Gap: LAC1 has not been computationally analyzed with DFI. And understanding the dynamics of LAC1 is significant because of its function of breaking down lactose. Also DFI has not been used that often, and using it again to possibly justify or corroborate with other methods can help support the method.

6. Significance: The larger real world implications include solving protein folding diseases, and understanding how changing protein code leads to human diseases.

And with that I can finally sleespflpcm,va.gagaregf.....

12 hours of sleeping later, I am posting this blog.

Episode 6: Into the Darkness

The meme of the week is definitely gonna be grinds my gears. A classic from family guy where people express their discontent.

Subtopic 1: Protein engineering and folding history.

Start with this because it sets up the background and creates the significance for my research. This topic will explain the goals of protein folding and how it has progressed through the years.

1. Protein engineering’s end goal is to make new proteins or new functions out of existing proteins or from scratch
1. Directed Evolution is a way to achieve that goal
1. Lutz discusses the process of directed evolution and the history of directed protein evolution. They talk about the computational tools for the evaluation of protein data sets. The methodological advances in semi-rational enzyme engineering and de novo enzyme design in recent years provide researchers with powerful and effective new strategies to manipulate biocatalysts. Directed evolution represents an obvious strategy to improve existing designer enzymes and to potentially “break” the performance cap.
2. Packer talks about pioneering studies in the field of directed evolution sought to improve the wild-type activity of enzymes through the enhancement of solubility, thermostability, affinity for substrate or catalytic turnover in simulations. The future of new directed evolution studies is bright.
2. In order to create new proteins, we must correctly predict the structure of the protein, which is no easy task.
2. 60 years ago, there were no discernable methods to figure out the specifics of protein folding, through Moore’s Law the methods will be more advanced in the future
1. Dill talks about Moore’s Law and the benefits of folding in the future, including the possibility of solving folding failures like Parkinsons and Alzheimers
3. Currently, there are many methods but experimentation and computer modeling are leading the way.

Subtopic 2: Different prediction methods Computer Simulation vs Experimentation.

1. Experimentation in labs is more Accurate
1. This only results in a small amount of structures because it is time consuming (2500)
1. Kumar
2. Computer analysis methods are less accurate now, but have the potential to create much more structures in a much faster manner in the future
1. They are also currently the most accessible form of analysis
1. Need to back this up
3. Thus computer models are the future of this field
1. CASP competition
1. Recently the computer based prediction models are more accurate than other methods
1. Kumar and CASP
2. Because computer based models are the more effective long term solution, I will be using them
2. REMD, SIFT, FIRST
1. I need to look into this some more and compare these methods, I just found some articles for this
2. FIRST, and REMD
1. De Graff
1. Crack Propagation
2. Thorpe
1. New methods for protein folding by using short-range forces in proteins modeled by constraints. Forces included in the analysis are the covalent bond-stretching and bond-bending forces, salt bridges, and hydrogen bonds. They used colored mapping to provide a visualization of the motion of the protein.
2. FIRST stands for Floppy Inclusion and Rigid Substructure Topography.

Subtopic 3: LAC1 Repressor, why look at it?

1. Definition of LAC1 Repressor
1. The crystal structure of the lac repressor is a bent structure with all 4 of the DNA binding portions pointing in one direction.
2. The DNA sequence has 3 lac repressor recognition sites within 500 base pairs. In the quaternary formation of the repression loops, the repressor interacts simultaneously with 2 genomic DNA sites.
3. Lewis
2. The repressor is important because it suppresses the coding for proteins that break down glucose, galactose, and other sugars.
1. Prevents the creation of Beta-galactosidase, which is the enzyme that performs the first step in lactose metabolism, making glucose and galactose. Galactoside acetyltransferase, which actually doesn't really do much in lactose metabolism (its unclear). And lactose permease transports lactose through membranes.
2. LAC1 plays a key role in lactose breakdown, understanding exactly why the protein functions the way it does will provide insight into diseases such as Lactose intolerance.
3. Goodsell from the Protein Database
4. Possibly engineer the LAC1 into not repressing those enzymes

Subtopic 4: Conserved vs Nonconserved positions

1. Certain parts of protein are essential to function, others are not
1. There is a dispute on whether or not all segments of the protein are essential to function
2. Conserved positions control major folding points that change the entire structure. Nonconserved positions control less important points in the protein that do not contribute to major structural problems.
1. However the function may be affected by Nonconserved position
3. Over many years scientists have attempted to change nonconserved positions to fine tune function.

Subtopic 5: The significance of Structure for Function

1. The structure of the protein is essential for understanding the biological role of the protein. Structural genomics aims to structurally characterize most protein sequences by a combination of experimentation and prediction
1. Baker
2. Could be placed after Subtopic 1

Combining both the significance of protein folding and prediction with the protein of LAC1 leads us to investigate the importance of Conserved vs nonconserved positions. Thus the question: Do nonconserved positions, when mutated, affect the function of the protein more significantly than conserved positions in LAC1.

Purpose: Understand definitions and the methods for testing LAC1. And understanding the future implications of the results whether it corroborates common evidence or not.

So I got a lot of subtopics, but I feel like the order could be moved around, if you could help me out that would be great. Help me out friends.

Episode 5: RIP Keenan Allen

Fantasy football just started, and my best wideout Keenan Allen just tore his ACL. I actually can't stand this, also I hate the snapper for the Cardinals right now. The meme for this week is Squidward Dab. This a classic where a dude in a squidward costume dabs in the middle of a children's parade. I actually can't stop laughing every time he hits the dab. It's lit. Anyway for this task its the Academic Conversation.

This week on Academic Conversation Death match, in corner A we have Swint-Kruse, L. with his work Using Evolution to Guide Protein Engineering: The Devil IS in the Details. In corner B we have Zahn, H. with his work, Subdividing Repressor Function: DNA Binding Affinity, Selectivity, and Allostery Can Be Altered by Amino Acid Substitution of Nonconserved Residues in a LacI/GalR Homologue. The topic of today's death match is whether or not mutations at non-conserved residues significantly impact protein function.

SK: Protein Engineering has always attempted to edit nonconserved residues and lead us towards new proteins with new functions. However, the scientific community has been blinded with this primitive assumption. I have found in my study that mutations at nonconserved positions could completely impede the function of proteins, just like mutations at conserved positions completely alter the folding of the protein.

Z takes a blow to the right side of his head.

Z: While the community has been dead set on nonconserved positions having a minor impact on protein folding, there is a reason that assumption is true. It would only make sense that insignificant coding regions in DNA won't change the overall structure of protein created. In my study, we tested several different residue sites, both conserved and nonconserved. We found a varied range effects on the function of the protein. Surprise? I think not. There is always a varied scale.

SK kneels to the floor and gets kicked to the floor.

SK: You must at least consider my studies, because they show a flaw with in silico experimentation. There are limitations associated with the prediction models and mutations at all locations may not even be altering the structure. But rather the folding itself may be inaccurate.

Z: That is a point we can agree on. We must take into account the limitations of our style of experimentation and work to increase the accuracy of these programs.

SK and Z shake hands, showing the true power of academic conversation.

But Z backstabs SK and the side I supported prevails.

(I wrote most of this last night)

Episode 4: I'm Ashwath, and this is my research blog

The meme this week is pretty fresh, only 20 days old. It's the I'm Rick Harrison and this is my pawn shop. I work here with my old man and my son, Big Hoss. Everything in here has a story and a price. One thing I’ve learned after 21 years – you never know WHAT is gonna come through that door. I don't understand myself why this is so funny, but the internet is going crazy replacing this classic intro with other people. I’m Harambe, and this is my zoo enclosure. I work here with my zoo keeper and my friend, Cecil the lion. Everything in here has a story and a price. One thing I’ve learned after 21 years – you never know WHO is gonna come over that fence. This cracks me up every time, but anyways back to AP Research. I've read more sources, so that's cool.

First, I'm Ashwath, and this is my research blog. I type here with my dax and my teacher, Mrs. Haag. Everything in here has a story and a meme. One thing I've learned after 4 weeks - you never know WHAT is gonna come through the works cited section. OK I'm done. But Literature reviews am I right? For my literature review, I need to set up the significance, any relevant information, and my gap in the research. So to build the significance of my protein research, I need to set up why finding a difference in conserved mutation function and non conserved mutation function matters. To show this I plan to talk about the history behind protein folding, and why it has always been a struggle to properly predict the folds a protein makes. Whether these mutations change the function (folds) can lead to further research techniques for large proteins like LAC1 in the future. There will probably have to be a large amount of defining or watering down in the literature review because a science background is practically required to decipher the research papers. But hey if I am able to understand it (which I am), I can translate into more layman terms. But as of now I don't know too many of the terms that need to be defined. Finding a gap in my research is relevant for A) moving towards a more efficient computer based prediction model over lab based procedure that are long and expensive and B) LAC1 which could help guide research in understanding the ways to fix the folding problems associated with its diseases. BUT the number 1 goal of my lit review is to have the reader understand what I am writing.

Second, I'm Ashwath, and this is ... OK I'm actually done. But an important source is probably the one from the Protein Data Base Databank describing the LAC1 protein function. This is probably the most important gap I have, which is the uniqueness of the LAC1 repressor. It is not only linked to specific diseases such and Lactose intolerance, it is also a large protein sequence, which computer simulations have struggle with. The source described the function of the genes that LAC1 protein represses. The genes code for proteins that break lactose into glucose, galactose, and other sugars. The LAC1 repressor prevents the creation of Beta-galactosidase, which is the enzyme that performs the first step in lactose metabolism, making glucose and galactose. It also doesn't produce Lactose permease transports lactose through membranes. These details describe its function. The crystal structure of the lac repressor is a bent structure with all 4 of the DNA binding portions pointing in one direction, showing the largeness of the structure, 333 amino acids long. So yeah this source is pretty useful. This source doesn't have a real academic conversation surrounding it, but there is more conversation with computer simulations vs. lab results, and conserved/non-conserved positions existing or not. That is where the other gaps will come, however I think this is the strongest gap I have and thus I talked about it. I have the sources describing my methods and the computer simulations on the way, so I'll get some more controversial foundational sources soon.

Third, I'm John Oliver and this is my comedy show. I work here with my writers and my inspiration, Harambe. Everything in here has a story and a price. One thing I’ve learned after 2 years – you never know WHAT is gonna be corrupted. Ok actually I'm done. I love John Oliver and I watch him every Monday morning, even though I don't agree with him every time. Discussing this baller in class is chill with me, although I hope we don't get too hung up on him to keep paper on time. I watched the charter school segment and I agree with Oliver on most points, but I am happy to argue from a BASIS point of view.

Fourth, IM BILLY MAYES AND THIS IS MY OXI-CLEAN STAND. I WORK HERE WITH MY OLD MAN, MR. CLEAN, AND MY SON, BARRY B. BENSON. EVERYTHING HERE HAS STAIN REMOVING POWERS.. AND A LARGE PRICE. ONE THING IVE LEARNED AFTER 21 YEARS- YOU NEVER KNOW WHAT LIQUID WILL RUIN YOUR CARPET/CLOTHES/ETC NEXT. Actually I ran this meme into the ground at this point. (871(theres defn 400 relevant words in here i promise))

Episode 3: I don't know how to change the title of this blog.

So today on the meme enlightenment blog with some research on the side, we got a real classic here, Gnome Child, or Slayer. From the old Runescape days, the slayer arises into the Dank Meme mascot we all love and know today. Andy Salad has a terrible song with this Gnome Child. But on the topic of subtopics, dividing my area of inquiry is a difficult task.

This week I explored why LAC1 repressor, what does that even mean? Should I even care about it? That was basically this weekend. So LAC1 is just a protein that binds to DNA to prevent the coding of 3 proteins. Beta-galactosidase, which is the enzyme that performs the first step in lactose metabolism, making glucose and galactose. Galactoside acetyltransferase, which actually doesn't really do much in lactose metabolism (its unclear). And lactose permease transports lactose through membranes. LAC1 is called a repressor, because if it binds correctly lactose breakdown is stopped. But if the binding is off, the proteins are created and lactose is digested. The genes used for lactose utilization are negatively regulated. LAC1 binds and prevents the transcription of the genes that are used for lactose utilization. Also the protein is made of 4 subunits, and one side of the protein is a mirror of the other.

In terms of the subtopics, I don't really have a guided opinion of where to break the subtopics. In the papers, its written in english but you know its kinda not written in english with all the scientific terms so it takes forever to read through the literature. But I have vague idea. One subtopic would be the function of LAC1 and why its important. Another would be protein structure prediction models. Another would be the methods associated with testing. But I am not sure about the subtopics in my particular field. I need help here the most. For know I just looked into LAC1. I choose these topics because they are the most pertinent to the paper, why am I using this protein? what will this project be using? why look into protein structures?

I think my paper will be based around the history of folding proteins, and the significance of determining whether folding is altered by certain residue positions in LAC1. To end the blog I'll bring back the classic Gnome child in this beautiful track by Andy Salad.

https://www.youtube.com/watch?v=ldN9fNhZcsQ

Episode 2: Hopefully I'll get a meeting

 

This week on the meme team, 2EZ4RTZ is the meme of the day. But in all seriousness this week has kinda been awkward for me. On one hand I read deep into the literature of my topic and realized the real world implications of it. On the other hand I really wish I could arrange a meeting with my professor to help me confirm my research and hopefully give me some guidance. I’ll talk about the first topic first.

So I read the literature I had available to me, and I figured out the real world implications of my research. Protein folding is not an easy process and nature has created all of the most efficient working proteins. All man made proteins have only been done on a small scale and these proteins are significantly less efficient then the wild types (originals). Eventually scientists were like wtf we can’t create any proteins we gotta find a cheat for this process. Then probably some genius in the protein lab was like dude lets just take a natural protein and guide its evolution to serve a purpose that we want it too, its just 2EZ4RTZ. That genius was definitely Artour Babaev. Jokes aside they actually did that and it worked on large-scale proteins unlike the smaller scale ones from before. However Mother Nature was one step ahead of them, and the manufactured proteins were no where near as efficient as the wild types. The way they guide these proteins is by introducing mutations to change the proteins function. This is my angle, I one up the Artours and figure out whether these mutations actually significantly affect certain areas over others. However this is where topic two is gutting me.

My professor, greatest person in the world btw (I mean what professor is kind enough to let a 15 year old join her lab), has been sick all week. This means she definitely isn’t in the office taking care of her grad students. So she’s coordinating emails with them and me. We tried to set up this Saturday morning but it didn’t work out, so I sent her an email about her second available time this Monday afternoon. She is usually godspeed with anything I do, so this illness is pretty serious. I know the general area of research, hell I even know how to do my primary research with the ASU Supercomputer, but I really need the help with my research topic and why LAC1 and other questions. Also I kind of need her original research paper, the paper closest to my topic. It’s kinda like not free online. But maybe she even has an entirely different topic of research ready for me to dive into (in the protein folding field of course).

So to recap, I figured out real world applications and the surrounding field, but I really need to organize this meeting with my professor. My plan moving forward is look into the research on my own and organize the meeting. In terms of struggling, the field is pretty specific with some studies in academic conversation with each other, so I plan to expand my search area into protein folding in general to set up the significance of my future research. So like fingers crossed this meeting happens SOON.

Episode 1: Starting in the middle of nowhere and R.I.P. Harambe

Unlike AP Seminar from last year, this year in AP Research I intend to research something that truly interests me. So my goal for the class is pretty simple: Leave with a paper and presentation in a field that I like and be happy when I'm inevitably grinding out the literature review or presentation at 1am. Being happy is a pretty vague goal, but I want the class to feel like it’s a part time job as a writer. So it still feels like work, but I enjoy it at the same time.

My starting point in this class is paying respects to Harambe, and then finding a suitable topic. A suitable topic for me personally, is one that is backed by tons of specific literature that I can draw from. But I can’t just have the topic of American history because it is way too broad. At the same time, researching the physics of the bullet that killed Harambe the gorilla is probably too specific. On top of the so-called Goldilocks compromise, there needs to be an academic conversation surrounding the topic so that I can contribute to the field and actually make a contribution. Authors and contributors to the topic must have supporters and dissenters who engage with each other. I also have to feel like my research is significant in someway, again tied to my interest in the topic.

My process of finding a topic is kinda messed up, because I already have my research area and research methods from day 1. Due to aggressive under scheduling in tenth grade, I have an opportunity with an ASU professor to expand on her research. And my opportunity really seems safe, likely, and enjoyable. However, every plan needs a plan B (Harambe wasn’t prepared with a plan B). My secondary plan is to investigate some type of corruption. Previously I really enjoyed exposing the flaws of the pharmaceutical industry, Maryland gambling laws, and North Dakotan fracking laws. 3 days in and I have managed to grasp the academic conversation surrounding my plan A. I still haven’t described my plan A yet for some reason so here it goes: when mutations occur at so called functional sites, the protein folding is significantly altered, but other studies are showing that it doesn’t matter where the mutation occurs because they all result in defects in the protein. My professor, Dr. Ozkan, has already disagreed with them on a special protein. My gig is to see if the LAC1 protein is significantly affected by functional site mutations. The LAC1 protein is linked to lactose intolerance so there is a significant impact to the research at hand for me.

Plan B isn’t really developed, so I better look into that this week (or else RIP Harambe and Ashwath). Thanks for tuning into Episode 1 of Ashwath’s Journey to the center of AP Research. Tune in next week to see if Ashwath changes his meme theme from Harambe to something else.

R.I.P. Harambe