Protein folding mechanism biochemistry
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- Опубліковано 7 лют 2025
- This lecture explains about the protein folding mechanism. The protein folding is most important to form an active site that is used for the enzyme catalysis. Proteins can never be functional without proper folding. In this video I explain how protein folding is done with the help of chaperone and protein folding assisting proteins and it also explains the puzzle behind the protein folding.
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Thank you for watching the video lecture on protein folding biochemistry.
Your Lectures are always crystal clear in making understanding topics. You are gift to all biologist. Thank you for sharing your knowledge sir.
Thank you so much for appreciating my efforts
you really did it with all your heart,sir .Words fail me to say thanks.I'm a pharmacy student form Myanmar and looking forward to seeing you in many more lectures,sir
I am glad to hear that you're getting benefit from my lectures
InstaBlaster.
Shomu is a scientist deserving recognition. IAS zoology
Thank you so much for appreciating my efforts
Shoutout to this channel, you deserve more recognition sir, very well explained....
Thank you so much for appreciating my efforts
Your videos really help me during my exam.... Thanx
Finally i understand the protein folding😊 thanku very much sir😊😊
+ABHIJEET TRIPATHI glad you liked my lectures
A wonderful video summary on protein folding. I just read an article that the amount of ATP in the cell is much higher than actually needed for all the processes in the cell. It has been shown, that ATP contributes to protein solubility. I am really impressed by your work. I always watch your lectures to revise all the things I learned in my study course Biosciences. Thx again.
Is there a possibility to make a video about the updated view on ubiquitin system and deubiquitinating enzymes? I recently did my Bachelors in it and I have to say, this system is really really interesting.
excellent video, i will take an exam of protein biochemistry.
Explaination in most lucid language, ty sir
You're welcome. Glad to hear that you're getting benefit from my lectures
Thnx for explaining pro folding ib this way sir i also need to clear the concept of amyloid, ubiquitin mediated protein degradation and N end rule pathway..plz explain this further to clear the protein folding well.
Thanks so much 👍
You're welcome
Such a great vid, absolute clarity.
your vedios r really helpful..sir plz make vedios on how to prepare for ICMR..topics and everything..thank you😊
+Angel Swati will do that soon. Thank you
Great video 👍
Thank you
Outstanding 👍
Thank you so much for appreciating my efforts
Thanks for upload this video sir it is very useful for us 🤩🤩😇😇💫💫
You're welcome
@@shomusbiologyofficial i didnt expect this fast reply from you sir thank you sir and most welcome sir.
hi shomus...greate video! one question: what do u do in your life as a biologist? thx bye from italian biologist:)
+fla1994 hmm.. So many things.. Wil post that later
Thank you sir
You're welcome
Whenever I get confused, i come to see your videos. Don't take me wrong your videos are great, highly comprehensive but there is a problem. I think they need improvement in organization section. They are organized for sure, but there are better ways to Improve them
+WOW Okay. I will keep that in mind
WOW hi
thank you my dear teacher to upload such conceptual teacher
+Sami Ullah glad it helped.
thnks specially from my side for ur countribution u done a gr8 job
+arvind kumar thank you for appreciating my efforts
Here from 2021 and AlphaFold is open sourced recently!
very nice very helpfull
You're welcome
Sir ye topic protin folding problem ko bhi complete krta hai ky ?
hello sir.. great vedio... sir can u plzz uplod the vedio in which u ecxplane how to solve the qustion of gene deletion....
hello sir ..your videos are really good and understandable. Please provide some tips and tricks regarding part A of Csir net exam
+khan Yasmeen will do that. Thanks
that is great , how we can investigation of protein folding using infrared spectroscopy
Sirrr..... plz make a video on UPR or ER stress plzzzzz as soon as possible
hi sir ....your videos hv been a great support fr me..it is like before. starting with any topic i do watch ur videos to clear my basics nd i must say u. r doing a gr8 job .
sir I m in last year bsc biochemistry. can u please guide. what can I do. after. graduation..i hv intrest in research but I also want to be self independent as soon as possible. is it good if I go fr msc or should I prepare for ssc n other exams ?
+iki Mahajan stay tuned as many videos on biology career about to come
Such a good lecture... Thanks... Student 2019 😅 ... Sir how old are u now ? U look young...
Glad to hear that you're getting benefit from my lectures
please Provide a video regarding to the ^ PROTEIN FOLDING PROBLEMS ^.
Sir...is protein folding , molecular chaperones , amyloid protein sequencing and assays are there in biochemistry syllabus for biotechnology gate exam 2021...
I was watching your videos to understand thoroughly... please tell me
Yes
as soon as possible sir
please aplod n linked glycosylation of protein
You can increase sound sir
Sir, may i ask something. How do you know what kind of protein is produced (hydrophobic on the outside or hydrophobic on the core) only based on the amino acid sequence given? For example MLQSMVSLLQSLVSSIIQ, is it hydrophobic on the outside? or it has hydrophobic core?
Shomu, can you explain what the nature of the hydrophobic interaction is? I know what types of molecules tend to be hydrophobic but what is the fundamental force that means that non-polar molecules associate with each other in water? Is it purely that they can not form hydrogen bonds, and that therefore they are excluded from the water structure? In that case it's not really an interaction is it. I know it's not a nuclear force. And it's not an electrostatic force. It's not a London Dispersion force. Is it possible to explain what it is, rather than what it isn't? Thank you to you or anyone else who can answer this question.
I think I understand this a bit better now... When water molecules surround small pockets of non-polar molecules they form a highly ordered structure, and the more dispersed the non-polar molecules are the lower the entropy of the water. The effect is that hydrophobic molecules tend to aggregate together because there is an energy cost if they disperse which you could consider as equivalent to a bond dissociation energy. Anyone disagree? Let me know. Thanks.
Great efforts and teaching but I'll suggest you should use more pen and board instead of just explaining verbally because we tend to forget things after some time
Sure. Thanks
Sir can i get reference of this sir
sir 1 request,,,, protein,, sec protein,,, and quaternary prot,,,,please pawer point presentation banun sanga,,,,aani marathit explain kra,,,please sir
I am also intrigued by certain issues.
1. Must every amino acid present in a protein participate in bonding during the Protein folding process?
2. What is the process of breaking up protein to small clusters to aid computation?
great
+Swati Sharma thanks
U r voice is low sir
Plasmid replication
Hi sir ap acha pfhate ho
But aap board pr Bhoot kam likhte ho
Please board pr bhi note krte hue chlo
You can take notes from my voice
Soooooooooooooooooooooooooooooooooooooooooo many ads.... 5-10 seconds, fine. But 2 x 20 seconds?
I don't put them.
Volume is soooo low... Rest 👌
Thank you.
Hindi nhi aati kya tujhe yr
Nahi
😂😂
@@neetutiwari1463 maje le rhe ho नाबालिक bche ke ye achi bat nhi h