1. Most eukaryotic signaling proteins have modular structures composed of severa

Question

1. Most eukaryotic signaling proteins have modular structures composed of several domains that each carry out a distinct subfunction. What evolutionary constraints or advantages may have led to this type of organization?

2. A particular modular protein interaction domain is often found in many different signaling proteins in a given organism. Hypothesize how a modular protein interaction domain family may have expanded over the course of evolution. What issues may arise as such a domain family expands in size?

Explanation / Answer

Ans 1)The signalling proteins in eukaryotes have several domains and each of the sub-domains have sub-functions. The organisation of the proteins was done so that that structure of the protein is compact. The constraint is of space that leads to folding of the larger proteins into multiple domains due to the formation of the primary, second, tertiary and quaternary structures. The domains are responsible for different functions making it an advantage. While folding and creating different domains, there might have been certain mutations in terms of nucleotide change and sequence.

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