I know Im asking randomly but does anyone know of a trick to log back into an instagram account? I was dumb lost my login password. I would appreciate any assistance you can offer me!
no such words could EVER show how thankful i am for you... my medical studies are in french and i don't get a word of what our prof say... but here you are explaining better than any prof could ever do!!! such a HERO
#Chromatography is the collective term for a set of laboratory techniques for the separation of mixtures. The separation is based on differential partitioning between the mobile and stationary phases. Commonly used chromatography techniques include: gel filtration, ion exchange chromatography, hydrophobic interaction chromatography and affinity chromatography. Creative BioMart contains all different types of chromatography at all scales of matrix include: cross-linked agarose, cross-linked cellulose, dextran, methacrylic and polystyrene.
this is a great video and I found it to be a helpful review for my studies. However as a friendly correction you stated that this technique is only useful "if you know what specific protein that molecule binds to" However, I believe you can use Affinity chromotography for undetermined binding. If you use s tag such as FLAG that is is very hydrophilic it can be used to bind / tag the protein to the column even if that have no known binding partner. Then you can look at similar family of proteins with known/potential binding partners and run those partners through the column to see what your proteins of interest binds to. This technique has been used in many publications such as " Optimal Translational Termination Requires C4 Lysyl Hydroxylation of Erf1" Feng Et AL. Again just a friendly correction. Thank you .
A great teacher ...really impressed by your way of teaching . Got to know about your lectures by random searching.Your dedication is reflecting in ur lectures ...
But if that second solution of glucose replaces the first one, wouldn't the protein come out bound with the second solution, thus making it still not clear?
I think the second solution should not be glucose, but some other molecule that has more affinity to the glucose attached to the bead, so that it will competitively bind to it making our protein/enzyme of interest free so that it moves down.
Really you are amazing lecture i used to follow your lectures,but in this one i have a notes which is whats make free sugar solution pull glucose oxidase from its attracted state ?
may I ask: 1. what can we do to ensure the enzyme will not digest, only binds with the immobilized substrate during running the column? 2. after step E, what methods can be used to extract the enzyme of interest i.e. separate them from the glucose solution and transfer them to a suitable buffer solution since there still exists a binding force?
avedesco You telling me green-blue colorblind tells me absolutely nothing. If you want me to correct something I might have said in this lecture, add an annotation to your comment so I can go straight to that point and make the appropriate corrections.
The homie AK getting me through all of undergrad, and I already know he'll be with me all throughout med school haha. Thank you bruda!
Definitely will! Creating a ton of new content geared for medical school :)
Awesome!!!! :D
I know Im asking randomly but does anyone know of a trick to log back into an instagram account?
I was dumb lost my login password. I would appreciate any assistance you can offer me!
@Kenneth Kyle instablaster :)
@@kennethkyle1766 If you can't reset it through your email, or you don't have access to your email, I suggest contacting insta support
I love you man, my prof can't teach, first exam tomorrow and im dying
no such words could EVER show how thankful i am for you... my medical studies are in french and i don't get a word of what our prof say... but here you are explaining better than any prof could ever do!!! such a HERO
Amazing. Getting me thru undergrad and now job interviews in the biotech industry. Thank you!
totally help me to understand more about the differences between ion chromatography and affinity chromatography. thank you very much!
I‘m a German student and I can’t believe how easy it was to understand you. Thank you, you helped me a lot
You are simply excellent!!!!!!! the way you cover the points and also the use of diagrams is really helpful!!! thanks alot!
you are the best! I cannot tell you how much your lectures have helped me through my biochemistry degree
It is INSANE how well you lecture WOW THANK YOU SO MUCH
Wow. This seems so simple! I feel like I can explain it to anyone!
GREAT! you're a really good teacher, keep it up ;D
Stijn Vanmegen Thanks, appreciate that :)
Tomorrow i have final exam on enzymology,then i am here to understand this course and it is very helpful🥺❤️
The greatest in biochemistry THANKS
I love how hou you explain the topics
All your videos make all the topics so easy to understand... Thanks! :)
Last exam of the year tomorrow and this helps heaps!
Your lectures are so clear ! thanks
Why will the washout glucose solution outcompete the glucose on the beads?
#Chromatography is the collective term for a set of laboratory techniques for the separation of mixtures. The separation is based on differential partitioning between the mobile and stationary phases. Commonly used chromatography techniques include: gel filtration, ion exchange chromatography, hydrophobic interaction chromatography and affinity chromatography. Creative BioMart contains all different types of chromatography at all scales of matrix include: cross-linked agarose, cross-linked cellulose, dextran, methacrylic and polystyrene.
Pardon, it is great for me to have the image after you ( I mean your lecture). Thanks, Sir.
If you watch the entire video at 1.75x speed this dude is aggressively teaching you
You are a life saver!
This man is like oxygen for a student like me studying in a subject like biochemistry and molecular biology.....
😰😰😰
thank you so much for ALL THESE WONDERFUL VIDEOS, they help me a lot to study biochemistry!
thank you so much.... you are a perfect teacher.
great video !! really comprehnesive ! thanks a lot for making it so easy !
Thank you for your hard work 👍
Awesome informational video. Thanks!!
Thank you very much, your lectures are very helpful :D
Thank-you for doing this! People like you are awesome.
Thank you very much for this useful videos😃
Thank you thank you so much! You're a lifesaver!!
dam, you are the best teacher in the World
I'm your biggest fan man! Thank you
this is a great video and I found it to be a helpful review for my studies. However as a friendly correction you stated that this technique is only useful "if you know what specific protein that molecule binds to" However, I believe you can use Affinity chromotography for undetermined binding. If you use s tag such as FLAG that is is very hydrophilic it can be used to bind / tag the protein to the column even if that have no known binding partner. Then you can look at similar family of proteins with known/potential binding partners and run those partners through the column to see what your proteins of interest binds to. This technique has been used in many publications such as " Optimal Translational Termination Requires C4 Lysyl Hydroxylation of Erf1" Feng Et AL. Again just a friendly correction. Thank you .
you are a biochemistry God!
A great teacher ...really impressed by your way of teaching . Got to know about your lectures by random searching.Your dedication is reflecting in ur lectures ...
Very nice Explanation 👍
Very helpful 👌👌
Thanks for teaching easley!🌟
your videos have helped me a lot, thanks!
Thank you....
Thank you ♥️♥️
you’re the best
Great lecture Ever...
thanku Sir
thank you keep going that was very very helpfull
that was awesome , Thanks
But if that second solution of glucose replaces the first one, wouldn't the protein come out bound with the second solution, thus making it still not clear?
I don't even know what the hell I was trying to ask 2 years ago.
lol your were just saying that the enzyme was still bound to glucose and therefore it doesn't make since that we would call it isolated.
I think the second solution should not be glucose, but some other molecule that has more affinity to the glucose attached to the bead, so that it will competitively bind to it making our protein/enzyme of interest free so that it moves down.
What's the answer? Is it bound?
Axe10011 Actually it makes sense.
use displace instead of outcompete for reversible reactions.
Thank you so much!
man thank god i found u thanks a lot :) you are the one
finally I understand it, many thank you so much
How do we separate the protein from the glucose solution once collected?
Best ever lecture..👌
Really you are amazing lecture i used to follow your lectures,but in this one i have a notes which is whats make free sugar solution pull glucose oxidase from its attracted state ?
omg i love u so much ! thank you!
so saweet u
你好中国女人
you are my savior :3
hi, how do we know when it's time to collect the respective eluate?
as in real life, the solution would be all same in colours.
Thanks
Thanks Sir.
may I ask:
1. what can we do to ensure the enzyme will not digest, only binds with the immobilized substrate during running the column?
2. after step E, what methods can be used to extract the enzyme of interest i.e. separate them from the glucose solution and transfer them to a suitable buffer solution since there still exists a binding force?
Amen. Thank you!
thank you
You the MVP
do you give private lecture??
Hi AK,
can imidazole essentially do the same thing as pouring glucose to elute the protein of interest?
thank you ^_^
Will you make lectures for informatics?
@AK Lectures... What if our protein didn't have color, how would we be able to separate then?
Mahmud Bhuiyan through SDS PAGE electrophoresis.
nice
hi, what does crude mixture of proteins mean?
Crude mixture, which has unknown sample whether proteins or other compounds
can you explain Gas chromatography please
***** i already did a lecture on that.
very informative lecture ,,, thanks very much to represent such a grear lectures
Blue-green colorblind?
Good lecture though.
avedesco You telling me green-blue colorblind tells me absolutely nothing. If you want me to correct something I might have said in this lecture, add an annotation to your comment so I can go straight to that point and make the appropriate corrections.
avedesco so well
Dude the hair... Let it go.
You shut your mouth.