This 30-nm fiber is further folded, results in 1000-fold compaction in euchromatin in interphase chromatin and in mitotic chromosomes to achieve an overall 10,000- fold compaction in euchromatin.

#Id: 2492

#Unit 13. Methods in Biology

In conventional discontinuous gel electrophoresis two type of GEL system is used on top with comb there is a stacking gel with pH 6.8 and below resolving with gel pH 8.8 phenomenon known as isotachophoresis.

#Id: 2493

#Unit 13. Methods in Biology

The band-sharpening effect relies on the fact that negatively charged glycinate ions (in the electrophoresis buffer) have a lower electrophoretic mobility than do the protein–SDS complexes, which, in turn, have lower mobility than the chloride ions (Cl − ) of the loading buffer and the stacking gel buffer. 

#Id: 2494

#Unit 13. Methods in Biology

More recently Different from conventional gels, the matrix of single gel system introduced  which contains  three amino acids (serine, glycine and asparagine).

#Id: 2495

#Unit 13. Methods in Biology

The relationship between acrylamide gel concentration and protein fractionation range

#Id: 2496

#Unit 13. Methods in Biology

.In the Native (Buffer) Gels electrophoresis SDS is absent, and the proteins are not denatured prior to loading. Since all the proteins in the sample being analyzed carry their native charge at the pH of the gel (normally pH 8.7), proteins separate according to their different electrophoretic mobilities and the sieving effects of the gel.

#Id: 2497

#Unit 13. Methods in Biology

In the Native (Buffer) Gels electrophoresis it not possible to predict the behavior of a given protein in a buffer gel, but, because of the range of different charges and sizes of proteins in a given protein mixture, good resolution is achieved.