I liked. I just would like to correct in 7:49 (time of lecture) which was mentioned that hemoglobin takes oxygen as a oxi-reduction reaction. This is not the case, because the iron remains in ferrous form (+2) when receives the oxygen, When oxidation occurs it forms methemoglobin (Fe+3), not fuctional, which should be reducted by reactions of redox to recover the functional form.
Thank you so much, I love all of your biology videos and wish I had found them sooner! I also want to complement you on your handwriting and drawing skills (way better than mine :).
For alpha-keratin, the interaction between two strands is due to the hydrophobic effect -this leads to non-traditional left-handed turn. Disulphide bonds are formed in cross-linking alpha-keratins; I don't believe they hold the alpha-keratin together.
Could Asp sidechain create an extra peptide bond with for example Lys side chain? Aspartate has an acidic sidechain with a carboksyl group whilst lysines´ sidechain is basic NH3+ group. Could those sidechains react together and create an extra peptide bond?
your voice, encapsulating
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my tears are bursting...
Excellent series! Crystal clear and detailed. Easily the best on youtube and better than my Biochem professor!
what are you pursuing after your college now ??
You make everything so much more understandable, my notes actually make sense to me now
You are awesome. You are better than my lecturers :)
Seriously your explanation is understandable!
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This series has been extremely helpful thank you so much!!!
+Alana Esty You're welcome Alana! :)
I know this video is kinda old, but thank you a lot for these videos, because they are very helpful and easy to understand
your videos genuinely make me more hopeful not only to pass biochemistry but also gain more interest in it thank u !!
incredibly super, clear and understandable.
I liked. I just would like to correct in 7:49 (time of lecture) which was mentioned that hemoglobin takes oxygen as a oxi-reduction reaction. This is not the case, because the iron remains in ferrous form (+2) when receives the oxygen, When oxidation occurs it forms methemoglobin (Fe+3), not fuctional, which should be reducted by reactions of redox to recover the functional form.
You make everything so understandable!
really helpful series of lectures that reduces reading and understanding line by line, word by word....
Thank you a million 😭😭😭😭😭😭😭😭😭u just saved my life
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thank you !! you really explain so well close to perfection thank you so much!!
thanx a lot . all the protein structures mentioned is very helpful and easy to understand
Went from a d to a b with these helpful videos. What a lad 🙌🏻
Without you I wouldn't be able to a doctor
Thank you so much, I love all of your biology videos and wish I had found them sooner! I also want to complement you on your handwriting and drawing skills (way better than mine :).
Wonderful, God Blessed.
Excellent work ..biochemistry made easier
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U just awesome.👍.... Explain all biochemistry topics pls... It's a request .... 😊
waooo u r genius i can say ur videos help me a lot in order to understand to concepts of biology thankyou sir
these series is very amazing thank you
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Thank u so much
well understood...thank you so much
Awesome work
For alpha-keratin, the interaction between two strands is due to the hydrophobic effect -this leads to non-traditional left-handed turn. Disulphide bonds are formed in cross-linking alpha-keratins; I don't believe they hold the alpha-keratin together.
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Really Helpful, Thankyou 😊
Really helpful...thanks a lot!!!
Very well explained :)
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Could Asp sidechain create an extra peptide bond with for example Lys side chain? Aspartate has an acidic sidechain with a carboksyl group whilst lysines´ sidechain is basic NH3+ group. Could those sidechains react together and create an extra peptide bond?
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why is a disulfide bond considered covalent? I thought a bond between two same molecules is noncovalent bond'
no
what is your reference books
Kya ya lecture urdu ma mil skta hai
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Please add subtitles plz
Why could not a sub unit work on its own.?
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I've been sitting here like ughhh this guy goes so fast and as i go to slow the video down I realize that i have it sped up 🫠
what an excellent lecture, you've made my course so much easier. I love you
you made my studies easier.... I got my perfect and complete notes... thank you so much sir!!!
The teaching method is effective taught in white board . Many people teach through power point which is boring
I agree completely. If it ain't broke don't fix it.
That's really awesome. Thank you so much! May God gives you happines, as always :)
But I have a doubt this fibrous protein is tertiary not quaternary?
Seriously massive thank you for all your videos. Getting heaps out of them !!! :)
Excellent series. Thanks a lot😍😍
Thank you. These aree amazing.
awesome, thank you sir
great work... helped a lot...:)
You are an amazing teacher