Non-denatured proteins can be separated according to charge and size.

In the first dimension, the proteins are separated by isoelectric focusing, which resolves proteins on the basis of charge.

In order for neuroproteomics to function correctly, proteins must be separated in terms of the proteome from which they came.

The cellular proteins were prepared, separated on 4% polyacrylamide gel and transferred onto nitrocellulose membrane.

The proteins of the sample are separated using gel electrophoresis.

Using an advanced form of chromatography, the protein is separated by passing the bacteria through a column containing agarose, a seaweed-based material.

Complete processing was also observed when the E. coli proteins were separated in non-denaturing and non-reducing gels.

These proteins are then separated from the bacteria and purified to be administered as a drug.

The two proteins of the domain are separated by a cleft and linked by two alpha-helices.

Though barely detectable, proteins of collagen 1, the main organic component of bone, were separated and examined.