Amino acids and protein folding
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- เผยแพร่เมื่อ 20 พ.ย. 2023
- What are amino acids and protein folding? A protein is a very long chain of amino acids bound to each other by peptide bonds to form an amino acid chain. To make a protein, we need to get to know two things - the “ingredients”, which are the amino acids, and the “recipe” - or how the finished amino acid chain folds into the protein. Find our full video library only on Osmosis: osms.it/more.
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im watching this video and my exam is actually in 2 hours. im feeling a little confident thanks to this vid!
We hope the exam went well! ❤️
😂😂@@osmosis
Lol how was the exam?😂
Mine in next seven hours
I'm gonna make it 🤣
This video helped me a lot to figure out also how particles might form those 100+ different atoms, and how atoms might form these amino acids to begin with.
Nice 👍 work Dr . I really need these kind of concepts and concise covered a huge contents
This is such a great content to understand the topic 💯
These videos are invaluable, thanks so much, I have been watching many videos for biochemistry and all of them helped me a lot 👏
We're happy that we're able to help, Marlo! Best of luck with your studies 🙏🏼
진짜 최고..우리 교수님 강의는 하나도 못알아먹겠어서 이 동영상으로 독학하는중 .. 무한 감사
❤️ ❤️ ❤️
I am very pleased with what i've just watched ❤
Awesome! 💖
Regarding 0:45, An amino acid three letter symbol should start with a capital letter, with the subsequent letters being lowercase. E.g alanine is Ala not "ALA". Would you write the symbol for mercury as Hg or HG?
Awesome video thanks for posting! Quick question: Tyrosine is called both hydrophilic 3:40 due to the aromatic side chain, and hydrophobic 4:18 due to hydroxyl group. How can that be?
I was wondering this too!
I did some quick chat GPT "research" and this is what it responded:
Yes, tyrosine can exhibit both hydrophilic and hydrophobic characteristics, depending on its environment and interactions with other molecules.
Tyrosine contains a hydroxyl (-OH) group in its side chain, which can participate in hydrogen bonding with water molecules, making it hydrophilic. This hydroxyl group can also engage in hydrogen bonding with other polar molecules, further enhancing its hydrophilic properties.
However, the aromatic ring structure in tyrosine's side chain can also contribute to its hydrophobicity. Aromatic rings tend to be relatively nonpolar and can interact favorably with other hydrophobic molecules or regions within proteins. In certain contexts, tyrosine may be involved in hydrophobic interactions, particularly when buried within the core of a protein away from water molecules.
Overall, tyrosine's behavior can vary depending on its surroundings and the specific interactions it forms. In some cases, it may exhibit hydrophilic properties due to its ability to form hydrogen bonds, while in other situations, it may contribute to hydrophobic interactions because of its aromatic ring structure.
That's pretty interesting.
8:13 how do you know😭😭