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 :).
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.
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?
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.
your voice, encapsulating
your hair, immaculate
your teaching, incomparaple
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!
what an excellent lecture, you've made my course so much easier. I love you
This series has been extremely helpful thank you so much!!!
+Alana Esty You're welcome Alana! :)
you made my studies easier.... I got my perfect and complete notes... thank you so much sir!!!
You make everything so understandable!
thank you !! you really explain so well close to perfection thank you so much!!
SOMEBODY
PLEASE
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AN AWARD!!!!! 😭🙏🏆
Seriously massive thank you for all your videos. Getting heaps out of them !!! :)
your videos genuinely make me more hopeful not only to pass biochemistry but also gain more interest in it thank u !!
really helpful series of lectures that reduces reading and understanding line by line, word by word....
U just awesome.👍.... Explain all biochemistry topics pls... It's a request .... 😊
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 :).
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.
thanx a lot . all the protein structures mentioned is very helpful and easy to understand
these series is very amazing thank you
Went from a d to a b with these helpful videos. What a lad 🙌🏻
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 are invaluable.
waooo u r genius i can say ur videos help me a lot in order to understand to concepts of biology thankyou sir
Wonderful, God Blessed.
That's really awesome. Thank you so much! May God gives you happines, as always :)
incredibly super, clear and understandable.
Excellent series. Thanks a lot😍😍
Really helpful...thanks a lot!!!
Really Helpful, Thankyou 😊
you are amazing!!!!
Awesome work
You are an amazing teacher
Thank you. These aree amazing.
great work... helped a lot...:)
Thank you a million 😭😭😭😭😭😭😭😭😭u just saved my life
well understood...thank you so much
Very well explained :)
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?
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.
These videos are litttt!!!
awesome, thank you sir
YOU ARE AMAZING!
Without you I wouldn't be able to a doctor
Thank u so much
what is your reference books
Endless thanks
Excellent work ..biochemistry made easier
I love your accent!!
But I have a doubt this fibrous protein is tertiary not quaternary?
Kya ya lecture urdu ma mil skta hai
why is a disulfide bond considered covalent? I thought a bond between two same molecules is noncovalent bond'
no
Why could not a sub unit work on its own.?
QUITE GREAT 👌👌👌
Please add subtitles plz
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.
ur a frikken god
Purple gang checking in
awesome
whos here 2024
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 🫠