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Is DNA smaller or bigger than a protein?
Let's put it this way, we know that electrophoresis is a test for the sizes of the fragments of DNA molecules while SDS-page is a test of the size of protein molecules. If you use electrophoresis to test the differences of protein, there will not be any bands as all the protein will travel to the end of SDS-page. Therefore, we can conclude that the pores of electrophoresis is much more larger than SDS-page. Since electrophoresis has larger pores than SDS-page, it also shows that overall DNA is larger than protein in size.
What is the function of glycine in sds page?
glycine molecular weight high so mobility also high so using in SDS PAGE
Who discovered SDS PAGE electrophoresis?
Laemmli U. K.
What is role of glycine in SDS-PAGE?
Glycine increases the mobility of the gel.
What is the purpose of sds?
SDS, sodium dodecyl sulfate, is a detergent, which means it's a molecule with both a hydrophobic (hates water) and hydrophilic (likes water) end. For protocols such as SDS-Page, it's a mild detergent that breaks the folded structure of proteins without breaking their amino chains. It's negatively charged and highly reactive, so it imparts a fairly consistent shield of negative charge to the entire linearized protein. When you then attempt to separate proteins using an applied field of positive charge, SDS provides the means for all proteins to migrate uniformly based on their size -- the purpose of SDS-page. Without SDS, it's difficult to sort out the migration patterns because different proteins have different folding states and different charges.
What is the advantage of adding SDS to gel electrophoresis?
SDS PAGE electrophoresis is an important method in the separation of proteins. it can be use to identify and isolate proteins aswell as determine if a protein solution is pure or contaminated
What are the drawbacks of sds page?
The major drawback is that treatment with SDS denatures the protein, meaning you are not looking at it in its natural state.
Difference between native page and sds page?
In SDS-PAGE complexes are separated to their subunits, proteins are denatured and covered by SDS molecules at a ratio of approximately 1 SDS molecule per 2 amino acids. Thus any charge that the protein might have is masked by he huge negative charge by the SDS molecules and migration and thus separation of proteins depends mainly on their size. That's why SDS page is commonly used for determing approximate molecular weight of proteins, for following the progress of protein purification, etc. In native PAGE proteins retain their natural fold and can remain in complex. So the migration depends on the charge of the protein, the size, shape and if it is in complex with other molecules or if it oligomerizes. For a example a protein that forms tetramers will give one band in an SDS-PAGE that corresponds to the monomer (provided that denaturation is complete) while on a native PAGE it can give more than one band, depending on the amount of each species (monomer, dimer, trimer, tetramer) From native PAGE usually in combination with other techniques you can see the oligomerization state of your protein or study complexation reactions like protein-DNA (band-shift assays).
What method could you use to further separate two bands from the same protein fraction after SDS-PAGE?
Electrophoresis is the method that could be used to further separate two bands from the same protein fraction after SDS-PAGE.
Is DNA smaller or bigger than a protein?
Let's put it this way, we know that electrophoresis is a test for the sizes of the fragments of DNA molecules while SDS-page is a test of the size of protein molecules. If you use electrophoresis to test the differences of protein, there will not be any bands as all the protein will travel to the end of SDS-page. Therefore, we can conclude that the pores of electrophoresis is much more larger than SDS-page. Since electrophoresis has larger pores than SDS-page, it also shows that overall DNA is larger than protein in size.
What is the need for using edta in sds page?
break the S-S bonds in a protein
What causes a protein to migrate on SDS-page in such a way that it appears to be a protein that is much bigger?
SDS-PAGE normally binds to proteins at a ratio of 1.4 grams of SDS for every gram of protein. Hydrophobic proteins, however, have an particularly difficult time binding to SDS because SDS is polar. Hence they may not be well coated in negative charge and may end up traveling down the gel much more slowly than other proteins. This gives them the appearance of much greater molecular weight.
What is sds-page used for?
SDS - PAGE is apparently used to seperate proteins. The proteins are by nature different sizes. SDS works as a stabilizer by separating proteins according to similar forms.
Why is denaturing sds-page used for running sds-page electrophoresis of egg-white lysozyme and not non-denaturing page?
may be because of toomany disulfide linkages
What is the function of glycine in sds page?
glycine molecular weight high so mobility also high so using in SDS PAGE
Why p53 is run as 53 kda on sds page?
Due to many proline residues it migrates slower on sds page and appears heavier than it is.
Role of tritonx100 in protein isolation?
TritonX-100 was used for Remove the SDS-From the crude protein, during homogenization the cell lysis buffer as contain SDS otherwise no need.
