Salting Out 

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.

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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.

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U are indeed a great teacher and great biochemist

Videos are invaluable! Our professor described the process of salting-out as "not entirely understood" hahahah. wonderful explanation.

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Great video ,translates well to other languages and covers all the basics

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connoisseur. .it is so enlightening to go through your lectures! Thank you heaps :)

Amazing lecture, i was so confused about this effect. Thank you.

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Great lecture and a good starting point on the topic!

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Genius, thank you a lot for this explanation

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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-

Amazing lectures as usual by Ak lectures

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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Pretty informative, great performance by the way!

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In my book it is given that hydrophobic patches interact with water molecule please explain how is it so

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This helped me so much 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.

Thank you so much!

Thanks from Chile ! c:

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?

Thank you so much! This video was very helpfull

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??

thanks again from Chile!

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.

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GREAT EXPLANATION

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For salting in (adding salt to protein) doesn't the protein solubility increase, not decrease?

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How to know which salt concentration is needed for protein? Like based on what fibrinogen requires 0.8 M salt?

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.

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?

awesome

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thank you!

Helped alot! Thanks!

what characteristics of the proteins determine the level of salt it takes to form a precipitate

Is there any mathematical way to determine at what salt concentration a particular protein salts out?

I think crystallize is not the right word here, as the clusters of proteins are amorphous.

thanks from NOLA!

It was good and informative

Señor, Porfavor agregue subtitulos en Español, considero muy importante su material.

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Sir,how do we know how much concentration of salt is required for which protein?

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does this mean fibrinogen is more hydrophobic than albumin? thank you !

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Wow

In salting out hydrophobic interaction will decrease or increase?

What is the best method to isolate protein from beans/seeds?

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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

Thank you very much!

Amazing lectures as usual by Ak lectures