Thank you very much for taking the time out of your day to create this video. I hope you know that you are helping so many of us! Especially those of us who are plagued with terrible professors reading off their extremely confusing and wordy powerpoint presentations. You're a pure gem!
Mariam Hussien our so called professors and hods can never make the topic so easy to understand..they will dismiss your questions and feel challenged..I am talking about India and Pakistan.
An intelligent person doesn't mean someone who knows everything,it means someone who knows a difficult concept so well that he can make everyone understand it. Thank you for the time and effort you have put in to making this video. I never thought the day would come when I would say yeah man, i know the concept of 2'3 BPG and the ODC😊
So from my understanding and summary, The 2,3-BPG is an allosteric effector in the RBC and it’s very negatively charged molecule. The T state of the haemoglobin (deoxyheamoglobin) is very unstable, has lower affinity for oxygen and positively charged, in the absence of 2,3-BPG allosteric effector the T state would shift to the R state by equilibrium and the R state is a stable and has high affinity for oxygen. But in the presence of BPG allosteric effector, it would fit into the T state because it’s very small and negative and it would stabilise the T state and cause it to lower oxygen affinity making it difficult to bind to protein. This way it would shift it back from the R state.
I've said it so many times already but I have to say it again your video is amazing and it's just 太伟大了, saved me from all the boring lectures. Thank you.
Cannot thank him enough for the way he is always helping me with my biochemistry degrees. There are only few professors like you in the entire world and the way you teach is so freakin sick like HOW?!!!! you are so amazing and like a god for real.
Hats off to you. Such a great teacher you are. May God bless you with all happiness. You are doing a great work. Thank you so much. I am really lucky to come across your videos.
Hello doctor I have a small question Please What is the effect of pH on 2-3DPG synthesis? Please help me because when I think about this I become confused specifically in the points of ( metabolic , respiratory alkalosis and acidosis) Help help 🙏 I am sorry my English is not good because it's not my mother. language
Great videos, one question though. If 2,3-BPG only binds to deoxyhemoglobin which stabilizes its T-state (lowers the affinity for O2), how does that deoxyhemoglobin molecules become oxidized? if the oxyhemoglobin molecule pushes out the 2,3-BPG it would revert back to the R-state (higher affinity for O2). Main question, how does the deoxyhemoglobin molecule with the 2,3-BPG attached become oxygenated in order to deliver the O2 to the tissues with (lower affinity) if when oxygenating it, it reverts to the R-state?
In oxyhemoglobin, the pocket in which 2,3-BPG binds to hemoglobin is too small for 2,3-BPG to fit in. This implies that the bonds between 2,3-BPG and hemoglobin have to be broken when deoxyhemoglobin becomes oxyhemoglobin. For this to happen, more than one of the heme groupes have to be _occupied by_ oxygen (occupied by =/= bound to). This requires a certain threshold concentration of oxygen in the surrounding tissue. I'm not sure that fully answered your question. I don't fully understand it myself. The book I use (Biochemistry 7th ed., Marieb) is a bit diffuse on this topic. It states that the more than one heme groups have to be "_occupied_ by oxygen" in order for oxygen to bind to deoxyhemoglobin.
One may interpret in the following way: The T-form is more stable than oxyhemoglobin with simply one oxygen bound to it. Therefore, in order for deoxyhemoglobin to bind to oxygen, thereby breaking its bonds with 2,3-BPG, it has to bind to several oxygen molecules simultaneously. Naturally, the question of whether oxyhemoglobin with only one oxygen bound to it even exists, arises. I'm fairly sure it does, which might be explained by the fact that not all deoxyhemoglobin binds to 2,3-BPG? Deoxyhemoglobin not bound to 2,3-BPG is in fact much more unstable than oxyhemoglobin.
why does the 2,3-BPG ever have to leave the pocket at the center of the hemoglobin, it seems that both pure Hb and Hb in Red Blood Cells both have an equal affinity for oxygen at the lungs because of the high O2 pressure so removing the 2,3-BPG would not appreciably increase its ability to bind to oxygen, if it stayed in there forever then the only effect it would have is to decrease Hb's affinity for oxygen at lower pressures like muscle tissue. I guess my question is how do we know that 2,3- BPG leaves the site, is it an observation thats been made or is it an assumption?
In your other videos you draw the 2 ab dimers one beside each other which makes the two beta units side by side. how come they are opposite to one another in this example?
Great video but you talk so fast and it sounds like you are screaming all the time, got headache. Please think about it next, don't dream or talk too fast
Thank you very much for taking the time out of your day to create this video. I hope you know that you are helping so many of us! Especially those of us who are plagued with terrible professors reading off their extremely confusing and wordy powerpoint presentations. You're a pure gem!
Truth
Mariam Hussien our so called professors and hods can never make the topic so easy to understand..they will dismiss your questions and feel challenged..I am talking about India and Pakistan.
These videos are amazing. You explain every topic of Biochemistry 100 X better than my textbook. Thank you!
I wish you would teach my professor how to teach. I've learned more from these videos than I have from the hours and hours spent in class.
agreeeed
An intelligent person doesn't mean someone who knows everything,it means someone who knows a difficult concept so well that he can make everyone understand it. Thank you for the time and effort you have put in to making this video. I never thought the day would come when I would say yeah man, i know the concept of 2'3 BPG and the ODC😊
Seriously, the way you transform a relatively complicated concept into something easily to understand for me is just insane. Thanks a lot.
So from my understanding and summary, The 2,3-BPG is an allosteric effector in the RBC and it’s very negatively charged molecule. The T state of the haemoglobin (deoxyheamoglobin) is very unstable, has lower affinity for oxygen and positively charged, in the absence of 2,3-BPG allosteric effector the T state would shift to the R state by equilibrium and the R state is a stable and has high affinity for oxygen. But in the presence of BPG allosteric effector, it would fit into the T state because it’s very small and negative and it would stabilise the T state and cause it to lower oxygen affinity making it difficult to bind to protein. This way it would shift it back from the R state.
I can't believe there are people who disliked this video. This is very helpful. Thank you for this!!
Idk if I should call u a professor or a savior. Honestly, u are awesome. It scares me how good u are. Thank you very much!
I've said it so many times already but I have to say it again your video is amazing and it's just 太伟大了, saved me from all the boring lectures. Thank you.
Cannot thank him enough for the way he is always helping me with my biochemistry degrees. There are only few professors like you in the entire world and the way you teach is so freakin sick like HOW?!!!! you are so amazing and like a god for real.
hey man u just made the multiple 2 hour lectures so ez for me , respect
This is what's saving me while going through online learning. I really am so thankful :')
Same here. I watch his videos more than my online lectures
What a great video! He makes things so clear
well, u're a hero ... keep doing this extremly usefull videoo...respect sir (y)
Big thanks from Africa😊
Sir your lectures are clearer than crystals !!!!! THANK YOU SO MUCH !!!
You deserve ALL my tuition money!
Thank You so much, may God bless you, because this should be paid content. You are the man!
Hats off to you. Such a great teacher you are. May God bless you with all happiness. You are doing a great work. Thank you so much. I am really lucky to come across your videos.
Greetings from Ghana... You are simply a genuis
Thank you so much
I really appreciate 🙏 💛
You have saved me woooow ❤
You are the BEST!!!!! Please take my professor's Job!
This is best lecture l have come across on this topic! Thank you so much 🙏
Jesus Christ you are actually good at explaining this! Thank you!
I fall in love with your explanation , plz keep going
*This is the best explanation ever🙏🙏🙏🙏.. thanks sir..*
I am a physician and love how you teach. Tremendous.
u sir are a hero
I appreciate your precise teaching method, Keep it up!
I thank this day to having found AK LECTURES!
Truely grateful for these videos! Thank you sir!
OMG Marry me, your videos got me through biochem! Thank you!
This was fantastic! Thank you sincerely!
Big thanks from india.😃
thank you sooo much, you saved my life! i've just found out this channel, but right in time to my test tomorrow morning
Thanks a lot. You saved me.
Thank you so much always the best
all needed informations in a short time the best teacher ever 💕
Thaaanks so much for explaining this point ... I completely understand it now ^_^
Outstanding! Thank you Sir!
Sir these lectures are soooo helpful ❤️
Wow, you got my yoni steamin'!
Great lecture.
This Guy is Awesome!
Holy shit this is life changing
Haven't found a better explanation!
very much useful videos.
Excellent video👌
Great explanation!
thanks ...your lectures rock
Perfect! Thank you for posting the video!:)
Hello doctor
I have a small question Please
What is the effect of pH on 2-3DPG synthesis?
Please help me because when I think about this I become confused specifically in the points of ( metabolic , respiratory alkalosis and acidosis)
Help help 🙏
I am sorry my English is not good because it's not my mother. language
thank you this was extremely helpful. btw love the accent
You are amazing! Thank you so much!
From Jordan ❤❤❤❤❤
Question: I understand how the hemoglobin transforms from the T state to the R state. When does hemoglobin transform from R to T?
Did you ever understand this?
Thanks for this video!
very clear . Thanks a lot
great great videos !! Thank you
when o2 binds to deoxyhemoglobin how it will detach to allow 23BFG to bind and then to be transported to tissues
Thank you king
Amazing
in the video where you compared the myoglobin to the hemoglobin curve, was the hemoglobin curve representing pure or RBC hb?
The molecule is 2,3,-bisphosphoglycerate NOT 2,3,-biphosphoglycerate
as we know oxygen binds only to the r state of hemoglobin so how does oxygen binds to the t state of hemoglobin which is stabilized by 2 3 bpg
Great videos, one question though. If 2,3-BPG only binds to deoxyhemoglobin which stabilizes its T-state (lowers the affinity for O2), how does that deoxyhemoglobin molecules become oxidized? if the oxyhemoglobin molecule pushes out the 2,3-BPG it would revert back to the R-state (higher affinity for O2). Main question, how does the deoxyhemoglobin molecule with the 2,3-BPG attached become oxygenated in order to deliver the O2 to the tissues with (lower affinity) if when oxygenating it, it reverts to the R-state?
In oxyhemoglobin, the pocket in which 2,3-BPG binds to hemoglobin is too small for 2,3-BPG to fit in. This implies that the bonds between 2,3-BPG and hemoglobin have to be broken when deoxyhemoglobin becomes oxyhemoglobin. For this to happen, more than one of the heme groupes have to be _occupied by_ oxygen (occupied by =/= bound to). This requires a certain threshold concentration of oxygen in the surrounding tissue.
I'm not sure that fully answered your question. I don't fully understand it myself. The book I use (Biochemistry 7th ed., Marieb) is a bit diffuse on this topic. It states that the more than one heme groups have to be "_occupied_ by oxygen" in order for oxygen to bind to deoxyhemoglobin.
One may interpret in the following way: The T-form is more stable than oxyhemoglobin with simply one oxygen bound to it. Therefore, in order for deoxyhemoglobin to bind to oxygen, thereby breaking its bonds with 2,3-BPG, it has to bind to several oxygen molecules simultaneously. Naturally, the question of whether oxyhemoglobin with only one oxygen bound to it even exists, arises. I'm fairly sure it does, which might be explained by the fact that not all deoxyhemoglobin binds to 2,3-BPG? Deoxyhemoglobin not bound to 2,3-BPG is in fact much more unstable than oxyhemoglobin.
Dylan Chandiram I have the same question, how does R state (high affinity) allows oxyhemoglobin unload oxygen to the tissues? Please help!
You are a GENIUS!!!!!!!!!!!!!!!!!!!!!!
you are awesome thank you
thanks ALOTTTTT!!!
Thank you sir!!
Tnx a lot
why does the 2,3-BPG ever have to leave the pocket at the center of the hemoglobin, it seems that both pure Hb and Hb in Red Blood Cells both have an equal affinity for oxygen at the lungs because of the high O2 pressure so removing the 2,3-BPG would not appreciably increase its ability to bind to oxygen, if it stayed in there forever then the only effect it would have is to decrease Hb's affinity for oxygen at lower pressures like muscle tissue. I guess my question is how do we know that 2,3- BPG leaves the site, is it an observation thats been made or is it an assumption?
Thank you AK!!!
In your other videos you draw the 2 ab dimers one beside each other which makes the two beta units side by side. how come they are opposite to one another in this example?
I love you
💗💗💓
It's almost not fair to be able to watch these videos.......
feel sorry for others relying only on the textbook.
Thankkkkkk yoooouu so muchh
Great video but you talk so fast and it sounds like you are screaming all the time, got headache. Please think about it next, don't dream or talk too fast
كفو
GOAT
Cytochromes AK lecture
liked :3