Water forms hydrogen bonds with proteins. How might these hydrogen bonds alter the ability of a protein to undergo conformational changes in water versus in the gas phase?

Question

Eugene Diaz

Chemistry

21 December, 03:06

Water forms hydrogen bonds with proteins. How might these hydrogen bonds alter the ability of a protein to undergo conformational changes in water versus in the gas phase?

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Layne Braun · Answer 1

Answer and Explanation:

Water is the most important solvent for biomolecules such as proteins because its form very strong and unique hydrogen bonds.

The secondary, tertiary and also quaternary structures of proteins depends on its solvatation (in which the protein is surrounded by water molecules). That means that is very important the interaction between water molecules and aminoacids in the primary sequence of the protein. In water, the protein is stabilized by the effect of the hydrogen bonds. As the conformation of the protein is essential to mantain the protein functionality (e. g. in enzymes, which are proteins that catalize reactions) and to interact to other proteins, its proper hydratation is very important.

Conversely, if the protein is in the gas phase, there are not interactions with water, and there is not stabilization of its conformation. The protein cannot retain its essential structure and functionality.