I am currently taking a biochemistry course. And I am just learning that there is way more to amino acids than I previously thought. I took cellular and molecular biology and we talked about how there were polar and nonpolar, hydrophobic and hydrophilic amino acids, etc. But I never knew how many different properties could go into changing amino acid structure and how that would ultimately change a protein's structure and function. When amino acids are in an acidic environment both alpha groups (amino and carboxyl) are deprotonated. When they are at a physiological pH of approximately 7 then only the amino group is protonated while the carboxyl group is still deprotonated. Then when amino acids are in a very basic environment both the amino and carboxyl groups are protonated. This will affect how these amino acids interact with one another and how they come together to form a structure. When these structures or chains of amino acids come together and fold up and join other folded up chains they function as proteins. But whether or not the protein is in a basic or an acidic environment affects how it’s monomers, the amino acids, are behaving. This is part of the reason why it is so crucial for your body to maintain a constant pH as to not interrupt or disturb the function of many different proteins.
Recent comments