Protein separation techniques

$1$ When separating proteins on SDS$-$

$2$ points PAGE, all proteins are positively charged because they are treated with Sodium dodecyl sulphate

True

False

Clear selection

$2$ Assuming that a protein had a

$4$ points

molecular weight of $100$ KDa when performing an SDS page. In presence of Beta Mercaptoethanol $($reducing agent$),$ the molecular weight shown on the SDS is reduced to $50$ KDa $.$ What can you deduce concerning the structure of the protein.

it has a tertiary structure

it's made of one subunit of $50$ KDa

it's made of $2$ subunits of same molecular weight

the protein got fragmented

$3$ When separating proteins on SDSPAGE large molecular weight protein migrate faster than the small MW protein

False

True

$4$

We want to separate the following

$4$ points protein using gel filtration chromatography, the order of elution of these protein will be:

$\backslash$table$[[$Protein$,\backslash$table$[[$Molecular size$],[($KDa$)]]],[$Myoglobin$,17\mathrm{.}0],[$Enolase$,93\mathrm{.}7],[$BSA$,66\mathrm{.}4],[$Ovalbumin$,42\mathrm{.}8]]$

BSA eluate first, followed by enolase, then Myoglobin then ovalbumin eluate last

Enolase eluate first, followed by BSA, then Ovalbumin and Myoglobin eluate last

Myoglobin eluate first,followed by Ovalbumin, then BSA, and Enolase eluate last

Ovalbumin eluate first, followed by myoglobin, then BSA, and Enolase eluate last

The course is biochemistry