I love the dudes accent so cool! This was a nice vid going over all the details and he also gave the structures of the molecules formed through glycolysis. What really made me like this s the handwritten part. So anyways what has been gained from this vid
1. There are a total of 10 steps in glycolsis.
2. The end products of glycolysis are 2NADH + 4ATP and 2pyruvate.
3.Steps 1-5 are the investment stages, 2Atp are invested here in steps 1 and 3 to form glucose-6-phosphate and fructose-1,6-bisphosphate.
4.Steps 6-10 are repeated due to the conversion of Dihydroxyacetone to Glyceraldehyde-3-phosphate by the enzyme Triose Phosphate Isomerase (based on it’s name it belongs to class of isomerases).
5. Two NADH are formed in step 6, due to the the enzyme Glyceraldehyde-3- phosphate dehydrogenase, it removes a hrdride ion and adds in onto the NAD+.
6. Steps 6-10 are the pay off stages, 4Atp are formed from steps 7 and 10. These ar referred to as substrate-level phosphorylation.
Twas a good vid, only improvements I would have liked to have seen was for the stating of the net gains which is 2ATP+ 2NADH and 2pyruvate. Also which steps are irreversible those are steps 1, 3 and 10. But all in all enjoyable vid!
So found a cool Protein vids here, a nice lady pleasant voice. So lets start ok this is a two part series, in the first vid she dealt with Protein structure the different levels of structure such as Primary, Secondary, Tertiary and Quaternary. Primary structure is the linear sequence of aa and only have peptide bonds in the polypeptide chain. Secondary structure has both peptide bonding between the individual aa and also hydrogen bonding within the polypeptide chain that gives rise to alpha-helix and beta-pleated sheets. However she didn’t goes as much into detail as BiochemJm did in his vids, which was unfortunate but can be expected from a 12 minute vid. Tertiary structure is the 3D shape of the enitre polypeptide chain and has hydrogen bonding, ionic bonding between positive and negatively charged R-groups, Van der Waals and Disulphide bridges what I thought was very important but left out was hydrophobic interactions which is particulary what gives the active site its shape. Quaternary structure she pointed out possess more than one polypeptide chain and has the same bonding found in tertiary structure.
A cool fact she added in was the Chaperonins, these are proteins themselves but help in the folding of the polypeptide chain. In addition Denaturation, how it is the unfolding of the protein and how it occurs at high temperatures or highly acidic or basic environments.
The second vid was a bit more exploration to why protein is important and a little tad mention of Lock and Key hypothesis and enzyme specificity . She delved into Quaternary structure and giving of example such as haemoglobin and how substitution of a single aa can cause Sickle cell Anemia. Finally she gave functions of proteins such as Structural- keratin in hair and nails, Transport- hemoglobin for oxygen transport, Receptors- receiving and sending signals, Movement, Defense- antibodies that attack foreign materials in your body and Enzymes.
A good two for roughly 20 mins she covered good basic stuff although lacking some important things but added some interesting stuff.