Certain intrinsically disordered proteins protect tardigrades from desiccation. What property of intrinsically disordered proteins will most likely allow them protect tardigrades from desiccation?

a. Intrinsically disordered proteins can form disulfide bonds with numerous proteins.
b. Intrinsically disordered proteins use ATP hydrolysis to refold proteins.
c. Intrinsically disordered proteins can interact with multiple proteins.
d. Intrinsically disordered proteins have large patches of hydrophobic amino acids exposed to solution.

The correct answer is option c.

Explanation:

IDP or intrinsically disordered protein refers to a protein, which is devoid of an ordered or fixed 3-D composition. These proteins can be partially structured or completely unstructured and are also one of the prime kinds of protein like a membrane, fibrous and globular proteins.  

The IDPs safeguards tardigrades from desiccation as they possess the tendency to associate with multiple proteins. With the association, these proteins give rise to a non-crystalline amorphous composition that functions to protect tardigrades from desiccation. In case, in the absence of non-crystalline composition, desiccation of tardigrades results.  

hydroxyl -oh

alcohols, always polar, can form hydrogen bonds with h2o molecules

carboxyl -cooh  

cargoxylic acids, has acidic properties which is a source of hydrogen ions, found in cells in ionized for with a charge of oh-1

carbonyl > co

ketone if within skeleton, aldehyde if group is at the end of skeleton, k & a may be structural isomers, it determines 2 sugars (ketose & aldose)

amino -nh2

amines, acts as a base, it can pick up h+ ions from surrounding solution, ionized with charge of 1+

methyl ch2

addition to rna/dna affects and gene expression

phosphate -opo3 ²⁻

organic phosphates, contributes to negative charge to, molecule that it is a part of, and potential to react with h20

sulfhydryl -sh

thiols, cross-linking stabilize the protein, and it is structure