BMD - Proteomics

MALDI-TOF measures the _____ of a protein sample.

• molecular weight

• charge

• pI

• mass to charge ratio

The method of transferring the protein bands from SDS-PAGE gel onto a nitrocellulose membrane and probing with specific antibodies is called as

• isoelectric focusing

• mass spectrometry

• Western blot

• two-dimensional gel electrophoresis (2-DE)

 

In SDS-PAGE, the stain that is used for protein visualization after electrophoresis is ____.

• Ponceu Red

• methylene blue

• Coomassie brilliant blue

• bromophenol blue

 

The role of SDS in SDS-PAGE is to ______.

• add density to the protein sample

• coat the proteins with positive charge

• coat the proteins with negative charge

• make the pI value of the proteins to zero.

In SDS-PAGE, proteins are separated according to their _____.

• size and pH

• charge only

• size only

• size and charge

 

Which one of the following steps is NOT part of the Western blotting workflow?

 

• Transfer of separated proteins to a membrane.

•  

  Digesting the protein mixtures into smaller peptides.

• Specific detection of a target protein by appropriate antibodies.

• Separation of protein mixtures by size using gel electrophoresis.

Before mass spectrometry, the in-gel digestion of the protein samples are performed using

• lysozyme.

• endonucleases.

• trypsin.

• proteinase K.

The function of TEMED is SDS-PAGE is to

• cross-link with acrylamide to form the gel.

• coat the proteins with negative charge.

• break the disulfide bonds of the proteins.

• catalyze the polymerization of the acrylamide.

IEF focusing separates proteins based on their

• molecular weight.

• size.

• pI value.

• charge.

In SDS-PAGE the gel is made by the polymerization of acrylamide and

• APS.

• bis-acrylamide.

• agarose.

• TEMED.