When you add salt to a H2O solution, you initially INCREASE the solubility of the protein as you salt in. This is due to a reduction in charge to charge interactions. As you continue to increase the salt concentration, the protein is then salted out as the salt and water compete. The entire process is a curve. Thanks for all the videos, they are excellent.
great video, very educational, but i wish i hadn't been distracted by my half-blind eyes screaming the whole time tbh i'm kinda impressed what kinda lighting did he use-
this is basically explained on the basis of a protein which possess hydrophilic aa on its outer surface.. that is globular proteins that is found in our blood..
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From the figure, why only the hydrogen from water molecule interact with the hydrophilic part of protein? Can the oxygen interact on the hydrophilic part as well?
please if you can explain to me, why the mobile phases containing a concentration of ammonium sulfate promote the binding of many proteins to HIC columns??
QUESTION : will more hydrophobic amino acids precipitate first or will more hydrophilic amino acids precipitate first? I have been trying to figure this out for a while and honestly the reasoning in my head for either one kinda makes sense.
Actually, most of proteins are more soluble in small concentrations of salt than in pure water (salting in). Moreover, the conventional dialysis would not separte these proteins. We should centrifuge fibrin and take out the supernatant with albumins. Then we can put fibrin into dialysis to remove salt. Nevertheless, good explanation, as always.
If you were to add 2.4M to the solution, would it be impossible via salting out to distinguish between the two precipitates? I would imagine that if you attain the fibrogen salt concentration first at .8 M, then repeat the process with 2.4 M, you could subtract some net precipitate value from the fibrogen concentration value to attain the serum albumin value. Does this make any remote sense or am I speaking nonsense?
Thanks so much. How do we separate proteins that is already dissolve in a salt. For example beta-glucosidase in citrate......... How do i get this enzyme out of this salt.
When you add salt to a H2O solution, you initially INCREASE the solubility of the protein as you salt in. This is due to a reduction in charge to charge interactions. As you continue to increase the salt concentration, the protein is then salted out as the salt and water compete. The entire process is a curve. Thanks for all the videos, they are excellent.
not all heroes wear cape
Όντως
some heros wear a very snug white tshirt
People like you deserve the heaven. Thanks for these videos. Greetings from Colombia.
Your videos are incredible! Thank you!
U are indeed a great teacher and great biochemist
Thank you sir. 6 years of pharmacy doctorate and 2 years of second master. And i have done that with the help of this channel thank you
omg. love it. you explained perfectly! thank you!
i become a genius after watching your videos. you have helped me thru 5 semesters of upper level/detailed science courses so far !!
the video is amazing, but i wish if u explained the salting in mechanism as well cuz i looked online and i still cant find a good explanation for it.
you are so good in explanation.thanks so much
Videos are invaluable! Our professor described the process of salting-out as "not entirely understood" hahahah. wonderful explanation.
I have watched your videos since 2nd school until now in university. You sir have saved me a lot of times. Thank you so much
Great video ,translates well to other languages and covers all the basics
great lecture series....please keep them coming
J Williams will do! :-)
Great video, really helpful. Thank you
Genius, thank you a lot for this explanation
connoisseur. .it is so enlightening to go through your lectures! Thank you heaps :)
Your explenations our outstanding! Thank you so much you are super helpful
you are a wonderful teacher!
Great explanation! You are awesome! Keep it up! Greetings from Mexico
YOU ARE THE MAN! Mucho gracias
Muchas gracias!!! Me ayudaste demasiado! Grandiosa forma de explicar :D Saludos desde Colombia!!! :)
Amazing lecture, i was so confused about this effect. Thank you.
so much thanks from Vietnam
Great lecture and a good starting point on the topic!
These videos are so clear, thank you so much!
Great job
thank you for contributing and sharing your knowledge to us. : ) Helped me a lot in studying by BCs in Biochemistry
Thank you so much for that explanation! I was slowly giving up before seeing your video.
Thanks for the help! You're great at explaining!
Great Lecture! Big Thanks from Borneo.
Amazing lectures as usual by Ak lectures
Thank you, you do such a great job with explaining!
Thank you so much!
Thank you very much!
Thank you so much from México :)
Thanks from Germany!
tomorrows experiment at Biochem Lab!!!. thanks to him im not gonna look like a total dumb. Thank you so much for your help!!!
This helped me so much thank you
i loved this video
Pretty informative, great performance by the way!
GREAT EXPLANATION
awesome.. it's damn fluent and smooth..
Thanks from Chile ! c:
Bastian Nier Chile ! :-) thats awesome. and you're welcome.
thank you!
Awesome explanation....Keep uploading such videos
thanks again from Chile!
U r great sir
Thanks a lot! very clear and well explained! good stuff! cheers
great video, very educational, but i wish i hadn't been distracted by my half-blind eyes screaming the whole time
tbh i'm kinda impressed what kinda lighting did he use-
Thank you so much! This video was very helpfull
thanks
Damn. Killed it. Boss.
this is basically explained on the basis of a protein which possess hydrophilic aa on its outer surface.. that is globular proteins that is found in our blood..
Thank You For This!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!
You are e gem
Helped alot! Thanks!
awesome
A small thank you would be less for you Sir❤
You are fantastic
thanks from brazil
In my book it is given that hydrophobic patches interact with water molecule please explain how is it so
INTERESSTING
thanks from NOLA!
Thank you soooo much!
It was good and informative
I adore you
From the figure, why only the hydrogen from water molecule interact with the hydrophilic part of protein? Can the oxygen interact on the hydrophilic part as well?
please if you can explain to me, why the mobile phases containing a concentration of ammonium sulfate promote the binding of many proteins to HIC columns??
omg thank you thank youu
QUESTION : will more hydrophobic amino acids precipitate first or will more hydrophilic amino acids precipitate first? I have been trying to figure this out for a while and honestly the reasoning in my head for either one kinda makes sense.
thank u soooooooooooooooooo much!!!
the video is amazing, thank you!!
Actually, most of proteins are more soluble in small concentrations of salt than in pure water (salting in). Moreover, the conventional dialysis would not separte these proteins. We should centrifuge fibrin and take out the supernatant with albumins. Then we can put fibrin into dialysis to remove salt. Nevertheless, good explanation, as always.
I think crystallize is not the right word here, as the clusters of proteins are amorphous.
For salting in (adding salt to protein) doesn't the protein solubility increase, not decrease?
great thaaaaaanks alot
Señor, Porfavor agregue subtitulos en Español, considero muy importante su material.
diego fernando agudelo galeano that would actually require some sort of funding! perhaps some time in the future!
Wow
If you were to add 2.4M to the solution, would it be impossible via salting out to distinguish between the two precipitates? I would imagine that if you attain the fibrogen salt concentration first at .8 M, then repeat the process with 2.4 M, you could subtract some net precipitate value from the fibrogen concentration value to attain the serum albumin value. Does this make any remote sense or am I speaking nonsense?
Is there any mathematical way to determine at what salt concentration a particular protein salts out?
what characteristics of the proteins determine the level of salt it takes to form a precipitate
Thanks so much. How do we separate proteins that is already dissolve in a salt. For example beta-glucosidase in citrate......... How do i get this enzyme out of this salt.
How to know which salt concentration is needed for protein? Like based on what fibrinogen requires 0.8 M salt?
does this mean fibrinogen is more hydrophobic than albumin?
thank you !
Sir,how do we know how much concentration of salt is required for which protein?
In salting out hydrophobic interaction will decrease or increase?
What is the best method to isolate protein from beans/seeds?
Boiled?
Proof that god is real ⬆
6:18
🥰
Por favor en español !! Con subtítulos :(
I would appreciate it if you stopped moving around. Thanks.
Amazing lectures as usual by Ak lectures
Amazing lectures as usual by Ak lectures