User:Floriane Briere/Notebook/CHEM-496/2011/10/25: Difference between revisions
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To do so, we are going to run a SDS-PAGE using a 12% discontinuous polyacrylamide gel. | To do so, we are going to run a SDS-PAGE using a 12% discontinuous polyacrylamide gel. | ||
# The SDS-PAGE technique permits to separate proteins according to their molecular weight. The SDS (Sodium Dodecyl Sulfate) is an anionique surfactant which is going to denature the proteins and add negative charges on it; so proteins are going to migrate through the gel according to their molecular weight/negative charge ratio. | |||
# The SDS-PAGE technique permits to separate proteins according to their | # The discontinuous polyacrylamide gel is composed of two parts: | ||
## The stacking gel: compare to the resolving gel, the stacking gel has a lower concentration of acrymalide and a lower pH. It allows to concentrate the proteins into a thight band. | |||
## The resolving gel: it permits to separate the proteins which are going to migrate through the gel according to their molecular weight. | |||
==Protocol== | ==Protocol== |
Revision as of 11:03, 25 October 2011
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ObjectiveToday's experiment consists on performing a gel electrophoresis on MPB-intein fusion which have been expressed and purified by groups 2 and 3. This experiment will help us to determine whether or not the expressions and purifications worked well. To do so, we are going to run a SDS-PAGE using a 12% discontinuous polyacrylamide gel.
Protocol
Data
NotesThis area is for any observations or conclusions that you would like to note.
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