Between lectures, lab, gym and regular life (yes, I have one of those!), there wasn’t much time to produce creative content for Steemit lately. The fact that I have to hold a presentation on [this publication]( https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3676657/) on Friday, together with someone who doesn’t understand English that well made it even worse. This morning, I started researching for a post on what chemicals in our brain are responsible for our happiness. After an hour, I deleted everything, because I just *knew* that this post would be incredibly boring. Not because the subject was boring but because *I was bored*.<sub><sub><sub><sub><sub><sub><sub><sub><sub><sub>@suesa</sub></sub></sub></sub></sub></sub></sub></sub></sub></sub> At first, I considered not posting today (as I did yesterday) but then I thought to myself, why not explain some things to you that I’ll have to present on Friday anyway? So, let’s talk about *disulfides*. In your body, there are proteins. Proteins are made up out of amino acids, which are made up out of carbon, oxygen, hydrogen, nitrogen and sometimes sulfur. After the amino acids are put together in a long string, the protein needs to be folded in complicated structures, so it can do what it’s supposed to do. <center>![1.jpg.png](https://steemitimages.com/DQmTdA8FiWagCdb5XnEqQhXwRbc9D6cWPK44KmFansHdkPz/1.jpg.png)</center> That’s the part where the sulfur comes in. If there are at least two amino acids that contain sulfur (the amino acid in question is called *cysteine*), the sulfur parts form some sort of “bridge” which folds the protein a certain way. <center>![2.png](https://steemitimages.com/DQmZ2e45Ud1DB7fwS2LjYk2ZVLhhpUhzdwrQpKdkmqr2ywR/2.png)</center> There are other ways a protein can be folded, but we’ll concentrate on this one because it’s very … extensive. Connecting the parts doesn’t just happen by itself. It involves 4 Proteins, called DsbA, DsbB, DsbC and DsbD (in *E. coli* bacteria, that’s what the paper is on, in case you haven’t clicked it. I’m talking about bacteria here. The process of disulfide formation is slightly different in humans). I’ll call them A, B, C and D (Dsb stands for *disulfide bond*, DsbA means *disulfide bond protein A*). It happens like this: The protein encounters A and gives it an electron, which causes a sulfur of A to connect to a sulfur of the protein. Another protein sulfur gives an electron to A, which leads to the release of A from the complex and forms a bridge between the two sulfurs inside the protein. <center>![3.jpg.png](https://steemitimages.com/DQmVXdGbXZtKRDN1nk4aocghJb4V1ZysqZvEVfTjuVb4R2R/3.jpg.png)</center> This process is an *oxidation-reduction reaction*, where A gets *reduced* and the protein is *oxidized*. Reduction is the *gain* of electrons, while oxidation is the *loss*. I’ll be using these two words from now on! The protein is oxidized now and the disulfide is formed. But there’s a problem now: A needs to be in an oxidized form to function, but it’s reduced now! That’s where B enters the stage. B takes away the electrons from A (oxidizes it) and then moves them to a molecule called *ubiquinone*, which has several jobs inside the cell. Here, it just transfers the electrons, until they end up being transferred to oxygen (if there is air available) or to nitrate (if there isn’t). Both A and B are now in the form they’re supposed to be and can get back to work! Yay! <center>![4.jpg.png](https://steemitimages.com/DQmPURqRYRTdyuKSfyNJoJJgfU5TfqsiDeXmf6dfHM6WqLa/4.jpg.png)</center> But wait, something is wrong, I told you that there are *four* proteins at work, we only discussed two so far! This is because A doesn’t always do a good job. You see, A is only good at connecting two sulfurs that are next to each other, but sometimes, you need to skip one to get the proper form. When A tries to do that, it fails. <center>![5.jpg.png](https://steemitimages.com/DQmRuzVkNiCDZ86jrt5PAuPvk6fTLPc9CFcwzzJ22ukedvx/5.jpg.png)</center> For that, we have C. C can open the bridge up and form a new one. It can also just break the bridge apart *without* forming a new connection. If the second version happens, it’s effectively *reducing* the protein and gets oxidized in the process. <center>![6.jpg.png](https://steemitimages.com/DQmUkqZHk7CZYTFbU65fSU4emPTA4K5ghXYmetC11ZaXJ49/6.jpg.png)</center> But it needs to be reduced to work. So, again, we have something to help: The protein D. D does a lot of things. It moves around electrons throughout the cells in ways that aren’t fully understood yet. What is understood is, that it gives electrons to C, to return it to its reduced state. And everyone is happy again. Of course, there is a lot more behind the mechanisms than I explained. The 3D-structures of the proteins A, B, C, and D are complex and, in the case of D, not yet fully discovered. But I thought it might be interesting for you to learn something that not everyone can find out via a simple google search. Isn’t that what makes Steemit special? You can learn stuff you never even thought about. --- *As @thi-js hit 1000 SP now, I’m adopting a new minnow! His name is @emilclaudell and I will vote him until he reaches 1k SP.* --- *Pictures are all made by my incredibly artistic self. I finally got a tablet which allows me to draw on!* --- <center>![SteemStem](https://steemitimages.com/0x0/https://steemitimages.com/DQmRnvyXDCTdnMS9KnyhZ5y7a6o5LywP56njG2yziB6qQhz/Suesa_Steem-Stem_Banner.gif)</center> <center><sub>GIF was created for me by @saywha and @atopy , rest of the signature by @overkillcoin</sub></center>
post_id | 26,274,683 |
---|---|
author | suesa |
permlink | disulfides-in-proteins |
category | science |
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created | 2018-01-17 17:32:33 |
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like your life style,not bad
post_id | 26,275,025 |
---|---|
author | liam99 |
permlink | re-suesa-disulfides-in-proteins-20180117t173445726z |
category | science |
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It's work, work, work, like a good German minion :P
post_id | 26,275,549 |
---|---|
author | suesa |
permlink | re-liam99-re-suesa-disulfides-in-proteins-20180117t173807237z |
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created | 2018-01-17 17:38:09 |
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chemistry education is the best ever i see science education is best also carry on with science
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author | iqbalhossin |
permlink | re-suesa-disulfides-in-proteins-20180117t173508580z |
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It is an informative post of proteins.It is an educative value for all steemians. thanks for sharing that educative post.
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permlink | re-suesa-disulfides-in-proteins-20180117t173703790z |
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Thank you for these valuable info !
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permlink | re-suesa-disulfides-in-proteins-20180117t173827692z |
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Damn !! Now I understand why being happy is so complicated 🙆🏻♀️🤣
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author | himshweta |
permlink | re-suesa-disulfides-in-proteins-20180117t173922065z |
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>[...] what chemicals in our brain are responsible for our happiness. After an hour, **I deleted everything** [...] This post is not about happiness. I first considered writing about that topic, but then decided against it and wrote about something else.
post_id | 26,276,588 |
---|---|
author | suesa |
permlink | re-himshweta-re-suesa-disulfides-in-proteins-20180117t174445319z |
category | science |
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Oh !! All the time i was thinking that how weird is it that proteins makes us happy 😝😂
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> Between lectures, lab, gym and regular life (yes, I have one of those!) Wait until you become a PhD student ;)
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What will I drop, gym or regular life? Probably regular life.
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You have empirically proven record of good social skills (the most important). Concerning the posts you are way above an average student, thus you will finish it in 2 - 3 years easily with a lot of good time on conferences. And now it's time for my workout. Reading the papers requires serious core strength and endurance.
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https://steemitimages.com/DQmXXsXchD7Gkvwc3WR199A4amK35gcryzVfGy71KnrBtRJ/image.png Error 404: Regular life not found XDD
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What would your life be like without a regular life?
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Hello @suesa I couldn't help but chuckle at your sketches all the way through. I regularly workout at the gym and have some basic knowledge of protein and amino acids. Was nice to get a more technical break down of how they function. Question/Suggestion: I guess protein supplements like whey, specifically the "Gold" brand work in a similar fashion when consumed? If not I think it would be an interesting post to read. :)
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Protein supplements just provide you with amino acids that you need (and sometimes can't produce yourself). No relation to disulfides. You eat the protein, it's broken down in amino acids and those are used to form new proteins :)
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Yep, sounds about right. Thanks for the clarification :)
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You know about it,, I personally never been to Gym and I dont know anything at all about Protein or amino acids. But Seriously have huge muscles just like a Champion. . . . I am just kidding: No gym= No muscles looool
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Haha, maybe one day? ;)
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"No gym = No muscles" Have you ever seen a black person?
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Welcome to Steem, remember me when you are rich :]
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hey @xodan, I recently wrote a [post](https://steemit.com/health/@sco/food-supplements-2-collagen-does-it-make-you-beautiful-and-tough) about collagen supplements, which is also a protein, and general protein supps will be a topic of mine in the next 2-3 weaks. Let me tell you a spoiler: If you take up enough proteins via your regular nutrition, there is absolutely no need to take supplements - not even if you want to gain muscle mass.
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Perhaps if i can use the word oversimplified , you oversimplified disulfides. And this was far away from being boring. Your idea of using A and B even made it more easier to understand. I do envy your way of interaction with readers through your post. Kudos
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Oversimplification is sometimes necessary when explaining things to people who don't have the same educational background. It's actually hard to decide what can be left out and what is absolutely necessary. Happy you seem to have enjoyed the post :)
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Sure
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thanks for sharing that educative post.
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You know where I'm confused? It's the relationship between the mechanism you explained above and free radicals. If these are natural processes that happen in the body, can we be right to say that they also deposit reactive oxygen species in the body?
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Actually, DsbD and reactive ocygen species *are* connected! I just left it out to not make it too technical, not everyone has a background in chemistry or biology. But yes, if you read the paper I linked, it even specifically talks about the connection.
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Awesome. I'll check it out, and l I'll be looking forward to your posts. I guess this is a refreshing way of studying chemistry without going through those boring voluminous books.
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This post was resteemed by @surajkumarsharma Good Luck! [Use 'helpingbuddy' as tag to get a free RESTEEM] | Want to Know More! Check out [introduction post on how to use HelpingBuddy](https://steemit.com/helpingbuddy/@surajkumarsharma/helping-buddy-a-resteemer-for-you) The @surajkumarsharma users are a small but growing community. Check out the other resteemed posts in HelpingBuddy's feed. Some of them are truly great. Please upvote & comment for helping me grow.
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Thanks for your valuable post.
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Nice lecture, thanks for sharing.
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Wow, this post was very technical, definitely need a biology degree to understand what is happening here....
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Can't tell if sarcasm or actual criticism
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My background is so far from Biology/Science so that's why I had commented, its a very good post for those students studying that field who want to learn more
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Your posts are very intrsting I liked it very much .I request you plzzzzz visit my blog
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Visited your blog, determined that you're a spammer, thus you're receiving a flag. ![](https://steemitimages.com/DQmXPcvvkrFu4hAFmHRN9Af1MKywD1R973dCjKQt34oo5UR/grafik.png)
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You have the nicest way of saying fuck you!! I read it all, and mostly I love your drawings..and your ability to teach, and keep things interesting!
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Disulfide bonds in proteins are formed between the thiol groups of cysteine residues by the process of oxidative folding. The other sulfur-containing amino acid, methionine, cannot form disulfide bonds.
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Good job quoting wikipedia. https://en.wikipedia.org/wiki/Disulfide
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Probably writing about something else... :D
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I was dusting up an old poem about DNA, when I read this, so now it doesn't seem so nerdy to post it
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Start of this post is amazing, it made me read complete post... nice work
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That was an awesome read, thank you! I love how you started out this piece. "This morning, I started researching for a post on what chemicals in our brain are responsible for our happiness. After an hour, I deleted everything, because I just knew that this post would be incredibly boring. Not because the subject was boring but because I was bored.@suesa" As a person who used to deal with a great deal of depression, reading your words was like looking into a mirror of my own thoughts and realizations. What does cause depression? Is it DNA, RNA or boredom? For me the answer was boredom or to phrase it better, not doing the things with my life that make me the happiest. This is the coolest part of Steemit because through this platforn, I have been able to learn what things truly make me happy and I have also been given an outlet for sharing and learning about these things. As individuals and as a community we can learn and explore so many new things and talk with so many people from so many different cultures via Steemit. A tool bringing into the light, so many more prospective. Like a set of cameras set up to capture every angle of a shot, this platform appears to be boundless. Thx for sharing!
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Queen of science... Your sketches prove that art ain't your strength! :D Thank you for breaking down proteins for us. Question; Was recently told by a doctor that my body or blood (not sure) is full of proteins so I should reduce them. What does that mean? Are they harmful? He said they are.
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Hey, my drawings are magnificent, ok? :P I'm not sure what your doctor might have meant by that. Technically, your blood is full of proteins. But it's possible that there are elevated levels of the *wrong* proteins, or byproducts of protein breakdown. Can't say much about it from afar.
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Lol. Okay :p I am thinking elevated levels of 'wrong' proteins because he suggested I stop consuming them for a while.
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permlink | re-suesa-re-tezmel-re-suesa-disulfides-in-proteins-20180118t101133734z |
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> breaking down proteins for us Vote for best pun 2018
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https://steemitimages.com/DQmW38tbXN52JBFqFogn7Esis2A2PLyr3qPA595eTd9mW5r/image.png
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nice art,, ha ha
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I LOVE the illustrations - the happiest proteins on Steemit! Great post, explained simply but accurately. I'd use this to study for exams if I still had any in this field :-) Upvoted!
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Konten yang sangat bagus, saya menantikan yang selanjutnya
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I enjoy visiting your blog, though this is not my field of study, but when ever I discuss what I have learnt from your blog with my best friend who is a nurse she always marvel at where I get my knowledge from. Thanks @suesa for always sharing. And oh please the post on what chemical in the brain makes us happy ain't going to be boring as a matter of fact, I am already anticipating it
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Your sketches brought life to your words. Now I know what disulfides in protein are.
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It suddenly felt like I was back in school studying biochemistry all over again. Nice sketches although one looked like a car. Nice post. The human body is an amazing structure with so many activities going on. We can never exhaust it. Interesting piece. I learnt something new today
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permlink | re-suesa-disulfides-in-proteins-20180117t191336084z |
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Maybe I *wanted* it to look like a car. It's art. You'll never know :P
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permlink | re-zizymena-re-suesa-disulfides-in-proteins-20180117t192447967z |
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Oh okay but nice drawing.
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permlink | re-suesa-re-zizymena-re-suesa-disulfides-in-proteins-20180117t194028415z |
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Lol. What a coincidence, we happen to be studying about protein and its functions relating to its 3D structures. Even learnt the disulfide bond is a more stronger bond as compared to the hydrophobic bond, vander waal's forces etc. As to why protein A doea not do a good job in connecting. It is because protein are specific as to what substrates they bind to. "Structural complementarity"
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author | donaldpete |
permlink | re-suesa-disulfides-in-proteins-20180117t192243669z |
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excelent vlog
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author | edwuadr |
permlink | re-suesa-disulfides-in-proteins-20180117t200203145z |
category | science |
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this was really an interesting and easy way to understand disulfide bridges in protein structures.....i will really appreciate if you could come up with some more ideas and stuff to other macro-molecules and make them simple through your meticulous way of posts.
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author | bingobazenga |
permlink | re-suesa-disulfides-in-proteins-20180117t193446255z |
category | science |
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I'll see what I'll come up with. Thing is, breaking it down that simple is really hard. I've spend hours reading and understanding that paper for the presentation I have to hold. On that basis, I was able to extract the most important points and post them here.
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permlink | re-bingobazenga-re-suesa-disulfides-in-proteins-20180117t194007899z |
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hmm still it was a really good effort and whenever you come across such topics so do give them a try because you will also be working for easy understanding of complex processes for students and science lovers so keep the good work
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permlink | re-suesa-re-bingobazenga-re-suesa-disulfides-in-proteins-20180117t200334340z |
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When I see your drawings to illustrate your points so eloquently it makes me think that perhaps ,where you a teacher in the past ? or even now ?
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author | sbyse |
permlink | re-suesa-disulfides-in-proteins-20180117t194804746z |
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I'm a 21 years old biology student ^^ But thank you :) I wouldn't be a good teacher as I don't have enough patience.
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permlink | re-sbyse-re-suesa-disulfides-in-proteins-20180117t195529107z |
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I'm happy that you stated that regular steemians do have a life and not just some 1s and 0s in an algorithm :) Reduction and oxidation or redox reactions are one of my high points in high school classes. Happy to be reminded of some of my high school biology/chemistry classes.
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I'm just trying to hide the fact that I'm actually a *very* sophisticated bot
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We love a bot with a human touch :)
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hahhah i like ur drawing, the smiley are cute :) :D
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:3
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As I have to do another f*cking Western Blot tomorrow, I'm momentarily more interrested in cracking disulfide bonds that building them.^^ But nice sketches ;-)
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Break them open! Western Blots suck so hard, I'm so sorry
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ty for your sympathy, I am used to it anyway...
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I could lie and say that my handwriting is only so bad because I'm not used to drawing on a tablet but... I mean, my handwriting is *better* on paper, but still pretty bad. I assume the reason is that I only wrote cursive until I was 14 and then forced myself to switch. Never really developed the "typically pretty" handwriting most girls have xD
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Its a great knowledge sharing. Good informative post. Thanks for sharing the post.
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You got to think more when you really are bored. Hey you have cute drawings! Hahaha It is so good to learn while having fun.
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# *Warning I am going to critique this post...@lemouth style* LOL! Okay, here we go (don't get mad, my comments are just for fun). >the sulfur parts form some sort of “bridge” which folds the protein a certain way. It's probably better to say that the disulfide bond **Holds** the protein a certain way, rather than folds it. Though it may be involved in higher level structural organization and formation (tertiary and quaternary structures certainly). I like the smiley cysteines and cystines. > It involves 4 Proteins, called DsbA, DsbB, DsbC and DsbB (in E. coli bacteria, that’s what the paper is on, in case you haven’t clicked it. I’m talking about bacteria here. The process of disulfide formation is slightly different in humans). You only listed three proteins (DsbB you listed twice) Poor DsbD... :) There are also more then just those four! There is also a [DsbE](http://www.uniprot.org/uniprot/P0AA86), and [DsbG](http://www.uniprot.org/uniprot/P77202). DsbG is like a bigger, redundant DsbC! Nothing like ole Escherichia to have some redundant isomerases, one isn't enough for these little buggers. Furthermore, disulfide bond formation doesn't necessarily *require* all of those proteins to form the disulfide bonds, they are just catalytic, disulfide bond formation can occur anywhere depending on the oxidizing potential. Many prokaryotes use only homologous proteins to only DsbA and DsbB (I think its called the [DsbAB pathway](https://www.sciencedirect.com/science/article/pii/S0167488907002753)). B oxidizes A which Oxidizes the protein in this pathway, yup you're right. I don't know that a homologous protein disulfide isomerase (PDI) is found in all prokaryotes (keep in mind some prokaryotes don't really even have disulfide bonds in their proteins at all!) So not too bad so far! > B takes away the electrons from A (oxidizes it) and then moves them to a molecule called ubiquitin, which has several jobs inside the body. Wait a minute *E. coli* express ubiquitin? There is a prokaryotic homolog found in a couple of organisms, but I don't recall *E. coli* being one of them. Okay, so DsbB isn't shuttling electrons off to ubiquitin in the *E. coli,* but where are they headed? They are going to the [electron transport chain](https://en.wikipedia.org/wiki/Electron_transport_chain). DsbB dumps the electrons off into the somewhat similarly named compound **ubiquinone** which is more commonly recognized as CoenzymeQ<sub>10</sub> or CoQ<sub>10</sub>. Which looks like this: ![](https://steemitimages.com/DQmVwwgRGh4DcE3Vb5F9DdZoL1EYFUsHL5PpvVRbvNstwh1/image.png) > ![](https://steemitimages.com/DQmVTjNjCGvRmfuAHujkfBkFex1GFatBBtx8ezgZveNGN4K/image.png) Why are these cystines so sad? They don't know they are improperly bonded! They are having the time of their lives until DsbC comes in there and tears the party apart. > D does a lot of things. It moves around electrons throughout the cells in ways that aren’t fully understood yet. Yeah, not too much is known about the underlying mechanism of DsbD/DsbC electron transport chain. Yet. Cheers!
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Gotta correct the DsbD thing. The ubiquitine thing ia weird, gotta check the paper again if I just read it wrong. And yes, I know all that other stuff :P left out the homologes and most other things to make it less complicated for the average non-scientist. You should see the presentation... Although it's in German so there's to point. So overall, I agree with your criticism :P wouldn't present it like this to scientists, going to vote your comment further to the top for those who *are* scientists.
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>by transferring the electrons to an ubiquinone molecule. So, I obviously misread "ubiquinone" as "ubiquitine", you're right, need to correct that in my presentation too. But it's there. And it seems like it's generally *supposed* to be there. https://www.ncbi.nlm.nih.gov/m/pubmed/4192611/
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Ubiquitin (there is no e at the end of the word), is a protein, which the eukaryotic cell uses for a variety of purposes. Most notably for signalling that a worn out/misfolded protein be degraded by the proteosome (in this case the ubiquitin protein is attached to the broken protein through a process called ubiquitination, there are some other enzymes involved in this process too!). Ubiquinone is not a protein, it is an enzyme cofactor (I would classify it as a small organic molecule), and is involved in the electron transport chain. Ubiquinone is surely supposed to be there, it's an essential part of cells metabolism/redox pathways. Ubiquitin as you originally stated in your post, would NOT be in a prokaryotic cell ( there are a few homologues found in a few interesting bacteria/Archaea but not many as of yet have been observed ). I restate these things as you still appear a tid bit confised, based on the reply. You just have to be careful with your nomenclature, the two things (ubiquitin and ubiquinone) are not even remotely related. :) Hope this helps.
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I am not that ugly! Come on!
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:p
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@suesa : Hi.. this article gives me motivation to write on the research work and articles I read about. Keep up the good work. But my concern is that since I am a newcomer to the arena it is very difficult to reach out to people. Even quality works gets unnoticed. 😥
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permlink | re-suesa-disulfides-in-proteins-20180118t043818831z |
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You should reach out to steemSTEM, either on steemit.chat or on Discord https://discord.gg/smd26A
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In very short the amino acid doesn't just going and connect to a line of amino acid, but there is a DNA molecule that becomes RNA and mRNA to make the protein. There are 4 different structures to protein: 1. Is the line of amino acids that connected to each other. 2. In the structures, between specific amino acids form hydrogen connection. Those structures called Alpha Helix \Beta Sheet. 3. This one is a 3D structure that gives the protein the ability to do its job in the cell. this structure contain the disulfids bonds, ions bonds, Hydrogen bonds. 4. This is the last structure, in some cases the final protein can be build from a few protein in the 3D structure that connected to each other. one example is the Hemoglobin that build from 4 sub protein in the 3D form.
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Yes. But I really didn't want to explain transcription, translation and protein structures too.
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I understand, but still think that some background info even very basic can help here. I gave my mom read the post and she asked me about who decided what amino acid will be connected first and second and so on...
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Your in a great cycle of life. @suesa
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Fun stuff and I agree, posting about something you have to learn anyway is always an amazing way to keep the stress levels under control.
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Greetings from a Biologist, Venezuelan. These are definitely the topics that I like to read, those that expand my mind, those that make me remember because I am a scientist. Definitely a magestral class of proteins.
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Very nice post m'lady I tip my fedora at you (no sarcasm really god post) damn good stuff ma'am
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Hello @suesa. Your posts are about science and this one about acid helpfull for me. My exam will come on next Saturday and the topic is "Acid-Base". I have some preparations of my exam. This is my post about it:- https://steemit.com/science/@pradeeprajora/theory-s-about-acid-base
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great work!
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Interesting explanation of the relation of sulfur and electrons getting transported to the folding of proteins. Sulfur is the source of our bad odors yet, as you explained, is essential for the 3D shapes and thus the functions of our many different proteins. Interesting that CoQ10 (ubiquinone), a very important molecule necessary for converting sugar energy into usable ATP energy for our muscles and heart, also helps, as you explained, the process of shaping proteins. CoQ10 deficiencies are much too common in elderly people resulting in weak muscles and weak hearts. Thanks for the informative science post. Resteemed. Looking forward to your future post on brain molecules for happiness.
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