There are many well-known mutant forms of hemoglobin. These forms are usually named after the region where they are first identified. Hemoglobin "Philly" is a form of hemoglobin that is destabilized by having an F substitute for a Y in the -subunits. The Y normally participates in the hydrogen-bonded network that helps to knit together the 1-1 interface. Would we say that this mutation destabilizes 1o, 2o, 3o, or 4o structure? Pick one (the best answer) and explain why F causes this problem

The answer is given below.

Explanation:

Such a mutation would have an effect upon that Four design. It has been said, such substitution is a component of the linking of the alpha 1 as well as beta 1 groups, and those of the unit linking of each si 4 design, quite assured.

The design will be affected to a large extent since Y seems to be a polar amino acid, and it should not be substituted by an enlarged hydrophobic side chain.e Those units mentioned in such statement would not be able to bind or bind to one another properly, due to which lack in protein.

i think its the first one

many other transport proteins, often called pumps, move materials against a concentration gradient. active transport drives molecules across a membrane from a region of lower concentration to a region of higher concentration. this process, shown in figure 5.1, uses transport proteins powered by chemi- cal energy.