Seriously Sir👍its just awsum way of explaining da things...takes no tym to feed in mind. Beautifully way of presenting through diagram by making it colourfull & neat. Eye catching👌handwriting n diagram. Am going to suggest frndz to for dis channel. Thank you🙏
Oh god ..i dont have words to thank u sir... May Allah subhanwatala bless u and give u the mightest rewards for putting so much efforts and then providing the content for free..
Dear Dr. Hussain, Another superb video! Thank you. Have scientists tried to predict how a polypeptide will fold? Does the technology exist for a scientist to build de novo a functioning protein or enzyme?
The real question is really how does the polypeptides know it’s path to final shape in less than milliseconds let alone knowing what does the cell need to make such protein
@@avicennawater My guess is if you connected the same peptides in the same order they would fold the same way every time. It is because of the acid and base charges at each end of the individual amino acids, and the R groups. I think quantum mechanics and thermodynamics attempts to explain the mechanism of atomic interactions such as folding. It happens super fast. If you believe in evolution those proteins would not be here, nor you or I, if they did not fold into a functioning protein. Polypeptides evolved thru trial and error. The ones that folded into useful proteins were selected to stay. The duds were not promoted. Also chaperone proteins evolved (the same way) to help some proteins fold correctly. Not all proteins need the help of chaperones. Usually, if a protein folds incorrectly it is ubiquitinated and sent to the garbage heap (the proteasomes).
Are hydrophobic effects necessary for stability of a protein or is it just H-bonding? Particularly asking because I came across such question and I answered H-bond. Wondering if I was right.
Nice lecture! Are there any exceptions in the boy where 2ndary structure proteins are functional? (2ndary is when the bonds like disulfide and others form no?)
Hi Ramela , first of all thanks for appreciation........Now talking about proteins,,,,, I think Apolipoprotein E found to play crucial role in Alzheimer's disease has got functional secondary structure in the form of linear Alpha helices. ( still i am not 100% sure ). Thanks again
How do amino acids or cell in the process of forming fold to get to the ultimate final shape that cell needed to perform certain function ? I am alluding to the protein folding problem
There will always be intra interactions..... Like intramolecular hydrogen bonds between beta sheets..... If you say interchain , that means two different molecule ( chains) form hydrogen bonds but in Beta sheets we always have same molecule and we will always form intramolecular hydrogen bonds.
