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).
may be because of toomany disulfide linkages
glycine molecular weight high so mobility also high so using in SDS PAGE
Due to many proline residues it migrates slower on sds page and appears heavier than it is.
The major drawback is that treatment with SDS denatures the protein, meaning you are not looking at it in its natural state.
It is the gel of choice for SDS PAGE
The short answer to your question is "yes". I found myself researching the same question a few days ago and found that the real difference is between SDS/SDS Plus and SDS Max. I don't recall the exact dimension now, so I won't try to quote it, but the Max is a larger size. The answer I found was enough to tell me I used SDS (SDS Plus), and those were the bits I needed to buy. Once I knew that, I didn't need to remember the size of SDS Max...they were too big for my drill. Last point, SDS Plus is sometimes shortened to SDS+.
Laemmli U. K.
This refers to the type of detergent used to lyse cell membranes when extracting DNA from cells. SDS=Sodium dodecyl sulfate, CTAB=Cetyl trimethylammonium bromide
The SDS drill is considered to be the superior option for efficiency and ease of use, it does not require a chuck key. The hammer drill requires a chuck key for fitting different drill bits, which is considered the main difference of the drills.
SDS-PAGE method
Glycine increases the mobility of the gel.
Electrophoresis is the method that could be used to further separate two bands from the same protein fraction after SDS-PAGE.