During SDS-PAGE, glycoproteins migrate as relatively diffuse bands, whereas nonglycosylated proteins typically migrate as narrow, well-defined bands. Explain the reason for this difference in electrophoretic behavior.

Describe the function of the Bicoid protein. Explain how its ability to exert its effects in a concentration-dependent manner is a critical feature of its function.

Propose an experimental strategy to characterize the sequence and linkages of different glycan subtypes that comprise the glycome. For example, how might protein-associated N- and O-glycans be structurally characterized?

Is this statement true or false? exlain why

What is the pelleting time for eukaryotic ribosome subunits, 40S and 60S, in a rotor with k = 180? Assume that the medium viscosity and density are similar to water at %3D 20°C.

If you were to remove the ER retrieval signal fromprotein disulfide isomerase (PDI), which is normally a sol-uble resident of the ER lumen, where would you expect themodified PDI to be located?

Why are proteins unfolded in order to enter the mitohondria during post-translational transport? Which transport proteins do they enter through? Is it a receptor? Does it take energy to bring the unfolded protein in? What kind of proteins are brought into the mitochondria and why? Also, why are the proteins folded back up once it enters the mitochindria? Please help me understand this a little bit better...Thank you

Explain the presence of the protein identified by peptide keratin, type I cytoskeletal ?

The trans-Golgi network is the site of multiple sorting processes as proteins and lipids exit the Golgi complex. Compare and contrast the sorting of proteins to lysosomes with the packaging of proteins into regulated secretory vesicles such as those containing insulin. Compare and contrast the sorting of proteins to the basolateral versus apical cell surfaces in MDCK cells and in hepatocytes.

Describe the importance of ubiquitin-dependent degradation of soluble proteins.