Theoretically this makes a lot of sense... however, realistically you won't know exactly where your protein has been cleaved prior to running it on a diagonal PAGE. Wouldn't you have to purify and sequence the protein fragments following the diagonal PAGE to determine the approximate location of the disulfide bond?
I was under the impression that with SDS-PAGE the proteins are trapped in the gel, making it useful for reference and characterization, but not for physical separation and further purification?
+Paul Turcott It seems like gel filtration chromatography would be a better option for this? By the way, I love these videos man. I'm using them to brush up on basics before I go back to grad school ;)
Thanks sir...this video has very effective explanation!!
You're Awesome! Thank you!
Theoretically this makes a lot of sense... however, realistically you won't know exactly where your protein has been cleaved prior to running it on a diagonal PAGE. Wouldn't you have to purify and sequence the protein fragments following the diagonal PAGE to determine the approximate location of the disulfide bond?
Thank you soooooooooo much
good one
Thank you
I was under the impression that with SDS-PAGE the proteins are trapped in the gel, making it useful for reference and characterization, but not for physical separation and further purification?
+Paul Turcott It seems like gel filtration chromatography would be a better option for this? By the way, I love these videos man. I'm using them to brush up on basics before I go back to grad school ;)
AWESOME
THANKSSSS AWTSS GEGE
nojs