Which of the following describes the lining of the channel within maltoporin?

a. A series of aromatic side chains arrange in a helical pattern matching the relative curvature of the protein backbone, thus provided little restriction to transport.
b. Hydroxyl groups on glucose hydrogen bond with polar and charged side chains lining the channel, thus resulting in a series of interactions mimicking a screw-like pathway.
c. There is a pathway of phospholipids that line the inside of the channel and facilitate transport.
d. Constriction in the channel removes waters of hydration, thus making the substrate more hydrophobic and "greasy."

Option A.

Explanation:

Maltoporin is a membrane protein. It forms trimetric structure that facilitate the translocation of maltodextrins across outer membrane of E.coli bacteria. It is responsible for the guided diffusion in E.coli. it recognised bacteriophage sequence. It formed water filled pores across the outer membranes of gram negative bacteria. The lining of channel with maltoporin has a series of aromatic side chains stranded in a helical pattern matching the relative curvature of the protein backbone, thus providing little restriction to transport.

c-reactive protein (crp) is an acute phase protein belonging to pentraxin family of proteins, whose levels increases 1000-fold or more in concentration in blood during the occurrence of an injury, inflammation or tissue death.