Aquaporins are membrane proteins that span the entire membrane. An aquaporin protein must be able to interact with polar regions that are both extracellular and intracellular as well as polar water molecules moving through it’s core. Additionally, it must be able to interact with the nonpolar phospholipid tails. How is it possible that this protein (a collection of amino acids) can meet all of these requirements?

- Proteins are macromolecules that are large enough to cross the membrane of biological cells regardless of different regional polarities and they may act as pores through which molecules diffuse.

- Proteins have well-defined domains with amino acid residues whose R-groups contain both polar and nonpolar portions and thereby they interact with surrounding molecules according to their requirements.

Explanation:

Porins are a type of protein that cross the cell membrane and thus act as pores through which molecules can diffuse. Aquaporins are porins that form pores across the cell membrane and allow the transport of water molecules between cells. These proteins consist of six transmembrane α-helices embedded in the cell membrane. Aquaporins have five loop regions that enter and exit the cell membrane, and two of these regions are hydrophobic.

adefioyelaoye adefioyelaoye · Answer 2 · 2021-11-16T12:42:21+01:00

Aquaporins are regarded as membrane proteins which span the entire

membrane and are able to perform the listed functions as a result of the

following:

Proteins are structures composed of amino acids which are able to change

in structure and shape thereby aiding different types of interactions

Proteins are able to cross the membrane of biological cells because they

also act as pores through which materials pass through regardless of the

polarity of the molecules.

They also have polar and nonpolar amino acid properties which help to favor polarity of any type.

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