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