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..
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.
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?
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.
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.
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??
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?
Thank You For This!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!
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.
People like you deserve the heaven. Thanks for these videos. Greetings from Colombia.
not all heroes wear cape
Όντως
some heros wear a very snug white tshirt
i become a genius after watching your videos. you have helped me thru 5 semesters of upper level/detailed science courses so far !!
Your videos are incredible! Thank you!
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
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
Videos are invaluable! Our professor described the process of salting-out as "not entirely understood" hahahah. wonderful explanation.
connoisseur. .it is so enlightening to go through your lectures! Thank you heaps :)
omg. love it. you explained perfectly! thank you!
U are indeed a great teacher and great biochemist
you are so good in explanation.thanks so much
Great video ,translates well to other languages and covers all the basics
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.
thank you for contributing and sharing your knowledge to us. : ) Helped me a lot in studying by BCs in Biochemistry
Great explanation! You are awesome! Keep it up! Greetings from Mexico
Muchas gracias!!! Me ayudaste demasiado! Grandiosa forma de explicar :D Saludos desde Colombia!!! :)
Your explenations our outstanding! Thank you so much you are super helpful
Amazing lecture, i was so confused about this effect. Thank you.
Thank you so much for that explanation! I was slowly giving up before seeing your video.
Great Lecture! Big Thanks from Borneo.
Genius, thank you a lot for this explanation
you are a wonderful teacher!
These videos are so clear, thank you so much!
Great lecture and a good starting point on the topic!
Thanks for the help! You're great at explaining!
Great video, really helpful. Thank you
YOU ARE THE MAN! Mucho gracias
Thank you, you do such a great job with explaining!
great lecture series....please keep them coming
J Williams will do! :-)
Amazing lectures as usual by Ak lectures
tomorrows experiment at Biochem Lab!!!. thanks to him im not gonna look like a total dumb. Thank you so much for your help!!!
so much thanks from Vietnam
Thanks from Germany!
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-
Awesome explanation....Keep uploading such videos
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..
This helped me so much thank you
Pretty informative, great performance by the way!
Great job
Thank you so much from México :)
A small thank you would be less for you Sir❤
You are fantastic
GREAT EXPLANATION
Damn. Killed it. Boss.
thanks again from Chile!
In my book it is given that hydrophobic patches interact with water molecule please explain how is it so
Thank you so much! This video was very helpfull
awesome.. it's damn fluent and smooth..
Thanks a lot! very clear and well explained! good stuff! cheers
U r great sir
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.
i loved this video
Thanks from Chile ! c:
Bastian Nier Chile ! :-) thats awesome. and you're welcome.
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?
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 very much!
thanks from brazil
Is there any mathematical way to determine at what salt concentration a particular protein salts out?
Helped alot! Thanks!
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.
For salting in (adding salt to protein) doesn't the protein solubility increase, not decrease?
what characteristics of the proteins determine the level of salt it takes to form a precipitate
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??
How to know which salt concentration is needed for protein? Like based on what fibrinogen requires 0.8 M salt?
It was good and informative
thanks from NOLA!
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?
thank you!
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?
thanks
In salting out hydrophobic interaction will decrease or increase?
Thank you soooo much!
What is the best method to isolate protein from beans/seeds?
Boiled?
I think crystallize is not the right word here, as the clusters of proteins are amorphous.
awesome
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thank u soooooooooooooooooo much!!!
the video is amazing, thank you!!
omg thank you thank youu
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!
You are e gem
INTERESSTING
great thaaaaaanks alot
I adore you
6:18
Wow
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 so much!
Amazing lectures as usual by Ak lectures