Wow I wish you were my professor. Something I was supposed to learn during the week you taught me in 12 minutes. Thank You. Not everyone has the ability to teach but you got that talent.
Made more sense then my instructor and reading books. You are god-send thank you for this valuable information. Now I understand what Glycosylation actually is.
this was absolutely amazing, im researching hep b for a highschool internship at a biotech lab and i wanted to know more about the actual concepts we were exploring and this video was absolutely perfect. thank you so much this answered all of my questions (:
I am currently taking biochemistry and cell biology at the same, and it is kicking my butt. But you seem to have a video for every concept and topic that I am/have been confused about. Your videos are extremely helpful!
It was awesome absolutely helpful, I have tried watching all the step 1 lectures none could help me to understand as much as I did after watching this tutorial!
👍.I found two video ak videos really helpful and also another channel biology and genetics just it is new and has made one video about DNA topology supercoiling concept it really helped me.
very helpful! you're lecture was actually too in depth, but the writing on the white board help me understand the general concepts, and the rest filled in the gaps. Thank you!!
@@gloriagmail3561 Bullshit, I learn from khan academy and get 90s in my exams at university. They are so thorough that it just sticks. Stop bitchin y'll.
Thank you so much. Your videos have been helpful to me since high school and now that I'm a sophomore in college and I find your videos very clear and straight to the point which reinforces the concepts I learn at school. I have one question though, why is it only Asparagine that is capable of forming the -N linkage, aren't Glutamine & Arginine -NH2-containing amino acids as well?
The cis face of a Golgi stack is the end of the organelle where substances enter from the endoplasmic reticulum for processing, while the trans face is where they exit in the form of smaller detached vesicles. Incase, anyone else was revising too!
thanks, was quite helpful. But sadly not enough. Can you make a video on the actual process of the formation of the N-glycosylation in detail? That would be awesome!
I guess there are to things that can be misintepreted. 1st, the formed protein doesn't just move to the Golgi complex. Instead, it is packed into a versicel and activly transported to there. 2nd, the transmembrane proteine are already formed into the membrane and then transportet as a vesicle to the Golgi or cell membrane. So they are not put into it later...
Question: Im looking at my BRS Biochemistry book and it says that both N-linked and O-linked bonds are both the ER and the Golgi. Why does the video say that O-Linked happens only in the Golgi?
Great video. However, collagen is glycosylated to form an O-glycan and that occurrs in the ER so that bit where you say O-linked glycosylation only occurrs in the Golgi apparatus is not 100% true.
as one of the major significance of carbohydrate is protein modification, attachment of carbohydrates gives functionality to the proteins, so are those oligosaccharides used during protein modification, obtained from our diet? the glucose intake, does our cell polymerize the monosaccharide into oligosaccharide?
q: when the golgi complex modifies the proteins by adding carbohydrates through the o-glycosidic bond, it doesn't "modify" the work the ER already has done by changing the N-bonds to O-bonds right? By modify you mean it adds new o-bonds?
manyyyy thanks ....I was wondering about how organic molecules become glycosylated inside cells .. so could you please wright me an explanation about it or could you tell me where can i find the answer please
Isn't asparagine an amino acid ? So why should it be made by the ribosome of the endoplasmic reticulum... isn't the ribosome for making protein not the amino acids?
If the asparagine allows for glycosylation because of the amino group then could you do the same thing with glutamine since it also has an amino group? And then with regards to the other kind of glycosylation why wouldn't other amino acids like tyrosine, glutamate, and aspartate also work since they have hydroxyl groups available in their structures just like serine and threonine.
Only asparagine can form a N-glycosidic linkage? What about glutamine? Glutamine has the exact same functional group so why it can’t form N-glycosidic linkage??
I believe he uses the textbook by Berg, et al called Biochemistry. I say this because I have this textbook and use it as reference and notice sometimes his language is exactly the same as the book. It is also a very well regarded book for biochem.
