The great thing about your videos is the repetition. Normally, I stop videos and relisten to some parts over and over again. But you repeat it, with different words, to make sure one really gets it. Thank you so much!
Thank you for the very informative video! A quick question: Does myoglobin's affinity to oxygen change as a function of the availability of oxygen in the exercising muscle? In other words could myoglobin release oxygen at a different rate if the muscle becomes hypoxic?
Unlike many of the other educational videos that I've been seeing on RUclips, yours always seem to have hardcore information that I truly appreciate. Not only do you slam the overall gist of the video, but you also try your best to add every single component of that topic in a relatively short video. Thank you.
I love your videos the most out of any lecture channel on youtube, you explain everything so straightforward and easy to understand it's like i can read your mind. You are the best.
When you superimpose the structures of hemoglobin and myoglobin, they look very similar in their overall fold. However, hemoglobin functions as a tetrameric molecule (composed of 2 alpha and 2 beta chains), while myoglobin is happy as a monomer. Why?
+AK LECTURES (Andrey K) I figured but I just wanted to make sure I understand correctly. Thanks for getting back so quickly. Your lectures are awesome! Wish my professor taught as well as you do! :)
Sir, I didn't understand one thing, please clear my query. In case of myoglobin, 1% myoglobin unload oxygen and In case of hemoglobin, 21% of hemoglobin unload oxygen But both Hb and Mb unloading same amount of oxygen (100-40). So this conclude less Mb unload more oxygen in comparison to Hb ??
7:20 to 8:10 hemoglobin binds O2 in a non co-operative fashion argues against the written conclusion on that white board which is the correct statement.
Hemoglobin binds O2 in a cooperative fashion and Myoglobin binds O2 in a non-cooperative fashion. The sigmoidal curve indicates hemoglobin binds in a cooperative fashion because it readily gives up the O2 and has a lower affinity.
Great video. I had a question. While I understand that myoglobin is preferred for storing oxygen, how can the cell ever access that oxygen molecule? Even at ppO2 of exercising tissue it isn't able to unload oxygen! That's confusing.
The great thing about your videos is the repetition. Normally, I stop videos and relisten to some parts over and over again. But you repeat it, with different words, to make sure one really gets it. Thank you so much!
Thank you for the very informative video! A quick question: Does myoglobin's affinity to oxygen change as a function of the availability of oxygen in the exercising muscle? In other words could myoglobin release oxygen at a different rate if the muscle becomes hypoxic?
At 7:39, doesn't hemoglobin have a cooperative manner? And myoglobin doesn't? Is it a mixup or did I understand you incorrectly?
7:38 , correction; hemoglobin binds in a cooperative fashion
yupp
100 times better lecture than my bio teacher
imagine AK scolding his kid, hed set up a whole presentation to tell him what he did wrong
underrated comment XD
I watched all the videos about hemoglobin and myoglobin. Great videos deserved to spend time. Thank you
Unlike many of the other educational videos that I've been seeing on RUclips, yours always seem to have hardcore information that I truly appreciate. Not only do you slam the overall gist of the video, but you also try your best to add every single component of that topic in a relatively short video. Thank you.
I love your videos the most out of any lecture channel on youtube, you explain everything so straightforward and easy to understand it's like i can read your mind. You are the best.
When you superimpose the structures of hemoglobin and myoglobin, they look very similar in
their overall fold. However, hemoglobin functions as a tetrameric molecule (composed of 2 alpha
and 2 beta chains), while myoglobin is happy as a monomer. Why?
"... In just a moment" favorite line
Learning with you is amazing!!!!!! Greetings from Puerto Rico!
Thank you! thank you!
At 7:38 you said hemoglobin binds oxygen in a non-cooperative fashion. But in the previous video you said hemoglobin binds cooperatively.
+Wendi Clanton You're right! I meant to say "it binds it in a cooperative fashion" ! Thanks for the catch !
+AK LECTURES (Andrey K) I figured but I just wanted to make sure I understand correctly. Thanks for getting back so quickly. Your lectures are awesome! Wish my professor taught as well as you do! :)
you should make your videoes independent from youtube like khan academy.
he does have website like khan academy. check the description
damm that was really good
Thank you so much! I just love your lectures. They are very helpful!!!
Thank you soooooooooooooooooooooooo much 🥺♥️♥️♥️
Not All Heroes Wear Capes🔥🫡
That helped TREMENDOUSLY, thank you so much!
Sir, I didn't understand one thing, please clear my query.
In case of myoglobin, 1% myoglobin unload oxygen and
In case of hemoglobin, 21% of hemoglobin unload oxygen
But both Hb and Mb unloading same amount of oxygen (100-40).
So this conclude less Mb unload more oxygen in comparison to Hb ??
Thank you so much Sir,this was very helpful, I understood this very well,when I see this in my exam tomorrow,I'd be able to write. God bless you.
OMGGGG you are amazing! thank you so much for doing this and for your effort. i totally understand this better now for my biochem exam!
Great Videos on Biochemistry!!! Keep it up!!! Blessed
You always clear my doubts, thank you sir😊
7:20 to 8:10 hemoglobin binds O2 in a non co-operative fashion argues against the written conclusion on that white board which is the correct statement.
Hemoglobin binds O2 in a cooperative fashion and Myoglobin binds O2 in a non-cooperative fashion. The sigmoidal curve indicates hemoglobin binds in a cooperative fashion because it readily gives up the O2 and has a lower affinity.
goat
Graet!
Great video. I had a question. While I understand that myoglobin is preferred for storing oxygen, how can the cell ever access that oxygen molecule? Even at ppO2 of exercising tissue it isn't able to unload oxygen! That's confusing.
when the levels of o2 drop very low myoglobin unload all the oxygen as seen in the downward steep of the curve
ابدعععععععععت🥰🥰🥰🥰🥰
Very clear and concise explanations. Thank you!
Beautifully explained
I love his video so much!!!!
thank you sir
Thank u so much......
Amazing ✌️
Amaazzziiing
Hatss off
THANK YOU!!
thank you sir