I have to watch your lectures before I try and understand any concept my lecturer is trying to explain because I know you're going to explain it in a way I can understand, you are an incredible teacher!
just for information aminoacids for synthesis, are purchased with t-boc or Fmoc protecting group already attached to backbone amine. Also side chains have protecting groups. DCC is a good activator for backbone carboxylic acid, there are also other activators that could be used.
Brilliant video! What is it about TFA that makes it so effective at removing t-butyl derived protecting groups? Also, why does the HF added at the end target the phenyl specifically at the C-terminus, and not the other phenyl moieties in amino acids such as phenylalanine? Thanks!
Btw on that top DCC molecule your nitrogen has 2 lone pairs, 2 sigma bonds, and 1 pi bond - though it should have one less lone pair as a group 5 element if it's neutral as you've indicated
Hii there, nice video. I am bit confused on my synthesis as I got a sequence using phage display library against a pathogen for example: STFSQNG (N to C) and I want to synthesise it using Fmoc SPPS. But as the FMOC SPPS using Rink amide resins generate from C to N, should I use Glycine as first amino acid (reverse) or use S (serine) as first amino acid and then T,F,S etc.
I think it's important to learn the mechanisms of these reactions instead of just the products. My professor makes us memorize the reaction mechanism for protection with F-moc, DCC, etc. Even the mechanism of the deprotection of F-moc with treatment of mild base.
Simpel and straightforward explanation. However, using "actual" ever 5-10 s is a little annoying. If you could reduced it and only use it, when you want to underline something it would improve your point :) All in all, good work bud! Keep it up.
I have to watch your lectures before I try and understand any concept my lecturer is trying to explain because I know you're going to explain it in a way I can understand, you are an incredible teacher!
just for information aminoacids for synthesis, are purchased with t-boc or Fmoc protecting group already attached to backbone amine. Also side chains have protecting groups.
DCC is a good activator for backbone carboxylic acid, there are also other activators that could be used.
Excellent lecture. I am a newby to this branch of chem, the clarity and step by step explanation is outstanding.
2 hours class explained in 12 minutes....Thank You very much!!!!
Amazing explanation! Covered the exact right amount of information to follow along all the way.
You explain it so logically! Thank you! 😍
Thank you so much! this was so helpful! i have my orgo 2 final in 6 hours and am nervous as hell
Thank you so much, this will help a lot!
And to all students, godspeed you!
Best explanations ever, and Great video quality!
I'm really glad I found this video. Thank you so much.
Please dude, apply to professor at Aalborg University, you have my support!
Brilliant video! What is it about TFA that makes it so effective at removing t-butyl derived protecting groups? Also, why does the HF added at the end target the phenyl specifically at the C-terminus, and not the other phenyl moieties in amino acids such as phenylalanine? Thanks!
TFA is also amazing at removing skin from a person, don't spill it on yourself in the lab LOL.
An expansion on this would be useful, I.e different conditions and protecting groups
Hiii
Great explanation 💙
Awesome explanation!!
Btw on that top DCC molecule your nitrogen has 2 lone pairs, 2 sigma bonds, and 1 pi bond - though it should have one less lone pair as a group 5 element if it's neutral as you've indicated
Very well explained.
Thank you Sr ♥️
Hii there, nice video. I am bit confused on my synthesis as I got a sequence using phage display library against a pathogen for example: STFSQNG (N to C) and I want to synthesise it using Fmoc SPPS. But as the FMOC SPPS using Rink amide resins generate from C to N, should I use Glycine as first amino acid (reverse) or use S (serine) as first amino acid and then T,F,S etc.
Great explanation thanks Andrey
What is the net energy used in synthetic synthesis of polypeptides
Omygod thankyou so much.
You're the best❤
brilliant. Thank you so much for this excellent lecture. Brilliant.
What’s the name of the “solid support” you used in this example?
Thank you this is really helpful.
Is there a limit as to how many amino acids you can synthesize into a polypeptide using this method?
I think it's important to learn the mechanisms of these reactions instead of just the products. My professor makes us memorize the reaction mechanism for protection with F-moc, DCC, etc. Even the mechanism of the deprotection of F-moc with treatment of mild base.
agent475816 But that will be a 45 mins class then... Here only the concept has been discussed.
thank you
best lecture
well explained!
Laila Samadi Thanks!
how will you add second amino acid in peptide
this really helped
Ngozi Okwuosa great! :)
HF is extremely corrosive, would this be used in an industrial setting that is safe for workers?
that is why Fmoc protecting groups are used instead of tboc so TFA is used instead of HF for cleaving. peptide synthesis is not easy
Can you please make a video on synthesis of oligonucleotide ??
Simpel and straightforward explanation. However, using "actual" ever 5-10 s is a little annoying. If you could reduced it and only use it, when you want to underline something it would improve your point :) All in all, good work bud! Keep it up.
thanks you your lesson!
GOAT!
I wonder what the future of bioinformatics and 3D printing could do to alter this process
how would those fields help
In step 1, there should not be a negative charge on the nitrogen in DCC
Clear af
Good
thank you (Y)
i love you.
Can't see what you're writing