00:01
Hello everyone, in this question we have been asked that arginine is the most basic of the 20 amino acid because of its size chain that is under dash most cell condition.
00:14
Basically arginine has the nh2 present in its functional group.
00:19
So if this here gets deprotonated then this will become nh2 and if it stays in the protonated state then this will have the plus charge here.
00:31
So if this becomes deprotonated, so if it becomes deprotonated then it will be nh here and so there will be zero charge and in the protonated state there will be plus charge.
00:44
So this here is the positively charged amino acid and this is hydrophilic in nature.
00:53
So this is basic because of the positive charge present on it.
00:57
So in this option the positive charge is not present.
01:00
So here we will choose option a that is very highly charged side chain is present in this amino acid.
01:09
Then in the next question it says that amino acids which are not incorporated into polypeptides are sometimes converted into.
01:18
There are many protein amino acids which are the neurotransmitters like there is gamma amino butyric acid that is known as the gaba which is the major inhibitory neurotransmitter and some of the amino acid directly act as the neurotransmitter.
01:39
There is glutamic acid, aspartic acid and glycine also.
01:42
These here can be the antibiotics and they can also form the blood flow controllers like the arginine changes from nitric oxide which is a powerful neurotransmitter that helps blood vessels relax and also improves the circulation.
02:04
So here our right answer will be option e all of the above.
02:08
Then in the next question it says that proteins can be modified by adding dash to protein residue.
02:15
So there can be modification on the side chain or n -terminus of a protein thereby changing the fundamental chemical composition.
02:27
The protein modification allow a level of chemical diversity far greater than can be achieved using canonical amino acid alone.
02:36
So here option a says if we add sugar and phosphate group so that is basically added to the nitrogenous base.
02:44
Then option b says hydroxyl and formyl group.
02:47
So that here will change the property of the amino acid that will completely change the protein structure but this is added to the solution.
02:59
Then option c says adding cysteine.
03:02
So basically native cysteine residues can be targeted or cysteine can be introduced at a desired site in a protein by means of reliable genetic engineering techniques like in the insulin the introduction of the disulfide hydrogen bond is there.
03:19
So these are considered to be order promoted due to the ability to form the inter or intramolecular disulfide bond.
03:27
So here our right answer will be option c cysteine.
03:30
Then in the next question it says that a sequence of the amino acid.
03:35
Then in the next question it says a protein that contain more of the isoleucine, phenylalanine, leucine, asparagine, lysine and arginine.
03:48
Sorry this is leucine.
03:49
So this is most likely to be.
03:51
So here we can see this is hydrophobic.
03:55
This is also hydrophobic...