I've watched all over your biochemistry videos and they are pretty much on point with my lecture content. THANK YOU SO MUCH!!!!!!! YOU ARE A LIFE SAVER!!!!!!!!!!
I really love the to the point explanations. As a point of minor correction, I think the video title means Aspartyl, and not Aspratyl. Though nobody seems to mind, as everybody who watches your videos know what it means :)
How do calculate the specific activity of an enzyme? Im going through a past paper with a graph showing the absorbance of two enzymes (1 is trypsin the other is unknown) the absorbance is measured 280nm at intervals of 10 minutes.a casein solution was incubated with equal volumes of either the unknown protease(10mg/ml) or trypsin (50mg/ml) in 2 separate reactions.after set periods of time equal amounts were withdrawn from the two reaction mixtures and separately added to 5% TCA, filtered and their absorbance measured at 280nm. Based on this information please could you tell me what formula i would need to solve this please?
Because it's easier to pull hydrogen from sulphur as compared to oxygen atom in case of serine .... Sulphur is below oxygen in periodic table and as we know that a larger anion can stabilize charge much better therefore it's easier to pull proton from sulphur ... And we do not require aspartate (which acts as proton withdrawing group from histidine thereby increasing the polarizing power of histidine to pull the proton of other residue)
I was in 4th grade when this video was made, now it's helping me for my first biochemistry exam in medical school
Thats pretty mind boggling! Glad its helping you all this time later :)
I've watched all over your biochemistry videos and they are pretty much on point with my lecture content. THANK YOU SO MUCH!!!!!!! YOU ARE A LIFE SAVER!!!!!!!!!!
7 years later and this guy is still saving biochem studens! This content is more comprehensive than my professor has ever made it.
I really love the to the point explanations. As a point of minor correction, I think the video title means Aspartyl, and not Aspratyl. Though nobody seems to mind, as everybody who watches your videos know what it means :)
You are the god of biochemistry, be safe and continue :)
this is a great video
thank you this is very helpful !
YOU ARE THE BEST!
Thank you this is so helpful :)
Jade H You're welcome Jade :)
are cysteine proteases less selective and cleave a broader range of proteins?
I'm really interested,
How do calculate the specific activity of an enzyme? Im going through a past paper with a graph showing the absorbance of two enzymes (1 is trypsin the other is unknown) the absorbance is measured 280nm at intervals of 10 minutes.a casein solution was incubated with equal volumes of either the unknown protease(10mg/ml) or trypsin (50mg/ml) in 2 separate reactions.after set periods of time equal amounts were withdrawn from the two reaction mixtures and separately added to 5% TCA, filtered and their absorbance measured at 280nm.
Based on this information please could you tell me what formula i would need to solve this please?
I LOVE YOU!!! :) THANK YOU SO MUCH!
these videos are my only hope in passing lmaooooo
Anyone which specific amino acid does cysteine protease cleave?
Awesome
Why cysteine proteases don't have a stabilizer of the hystidine like the serine proteases do have?
you mean the oxyanion hole , ri8?
Because it's easier to pull hydrogen from sulphur as compared to oxygen atom in case of serine .... Sulphur is below oxygen in periodic table and as we know that a larger anion can stabilize charge much better therefore it's easier to pull proton from sulphur ... And we do not require aspartate (which acts as proton withdrawing group from histidine thereby increasing the polarizing power of histidine to pull the proton of other residue)
How many subjects he can teach 😂