For each amino acid listed, tell whether its influence on tertiary structure is largely through hydrophobic interactions, hydrogen bonding, formation of salt bridges, covalent bonding, or some combination of these effects.
a. Tyrosine

Question

For each amino acid listed, tell whether its influence on tertiary structure is largely through hydrophobic interactions, hydrogen bonding, formation of salt bridges, covalent bonding, or some combination of these effects.
a. Tyrosine

a. Tyrosine

Accepted Answer

All right. Hi everyone. So this question is asking us which of the following is primarily responsible for the influence of glutamine on the tertiary structures of proteins. Option A says hydrophobic interactions. Option B says hydrogen bonding. Option C says ionic interactions and option D says covalent bonding. Now recall first and foremost that the tertiary structure of any given protein refers to its overall three dimensional shape. And the three dimensional shape of a given protein is dictated by the interactions created or formed between the side chains of the amino acids that make up that protein glutamine. Of course, being one of them. So our four answer choices here describe a different interaction possible between amino acid side chains. So before we get into what glutamine looks like, let's go ahead and talk about these definitions starting off with a hydrophobic interaction. For option A recall that a hydrophobic interaction is one that takes place between amino acids that have nonpolar side chains. Hence the term hydrophobic. Now, the reason for this interaction is because of the London dispersion forces that are the primary intermolecular force observed in nonpolar compounds or specifically nonpolar side chains in the context of an amino acid side chain. Now, for option B, on the other hand, we have hydrogen bonding or each bonding, each bonding is a very specific type of interaction that involves amino acid side chains that include a hydrogen bound to a highly electron element, including oxygen, nitrogen and fluorine. Now, in the context of amino acids, the amino acids that contain, for example, o groups or NH two groups in their side chains are the ones that participate in age bonding. So long as these groups are neutral, because if they're not neutral, then those side chains participate in ionic interactions. Instead, ionic interactions. For option C are interactions that take place between amino acid side chains that have a charge one positive and one negative last but not least we have covalent bonding. Now, in this case, a covalent bond that's possible between amino acid side chains is the disulfide bridge and recall that a disulfide bridge is a bond formed between two residues of cysteine. Because cysteine, if you recall contains a file or an sh group at the very end of its side chain. So when these two files interact with each other, they create a new bond between both sulfur atoms. Hence the term disulfide. So now we can go ahead and talk about the structure of glutamine. Recall that glutamine as well as the other amino acids contain the same general structure to them in the center of the structure is one alpha carbon connecting to a hydrogen. The side chain abbreviated as an R group, as well as an amino group and a carboxylic acid group. Now to be more specific, the side chain of glutamine, in particular is a three carbon amide. So first, we have a three carbon chain branching off of the alpha carbon. But at the very end of the side chain is an amide functional group where we have a car bal or a carbon double bonded to oxygen, as well as an NH two group or an amino group connecting directly to the car bono carbon. So that's glutamine or GLN for short. Now, in this case, the side chain of glutamine is neutral. So ionic interactions are not going to take place in this case. And we can see that the side chain of glutamine contains electron elements, particularly nitrogen and oxygen. This is to say that the side chain of glutamine is polar. So hydrophobic interactions would not play a role either. Now, what the cino glutamine does have is at least one hydrogen atom connecting to the highly electron nitrogen. And earlier on in this video, we said that amino acids whose side chains contain NH two groups or oh groups can participate in h bonding. So as we can see, glutamine does fit our description and also we can eliminate option d in the multiple choice too because glutamine is not cystine. So th sulfide bridges which are covalent bonds are not possible either. So therefore, our answer is going to be option B in the multiple choice because H bonding is primarily responsible for the influence of glutamine on the tertiary structure of a protein. And with that being said, thank you so very much for watching. And I hope we found this helpful.

For each amino acid listed, tell whether its influence on tertiary structure is largely through hydrophobic interactions, hydrogen bonding, formation of salt bridges, covalent bonding, or some combination of these effects.
a. Tyrosine

Verified video answer for a similar problem:

Key Concepts

Tertiary Structure of Proteins

Hydrophobic Interactions

Hydrogen Bonding

For each amino acid listed, tell whether its influence on tertiary structure is largely through hydrophobic interactions, hydrogen bonding, formation of salt bridges, covalent bonding, or some combination of these effects.a. Tyrosine

Verified video answer for a similar problem:

Key Concepts

Tertiary Structure of Proteins

Hydrophobic Interactions

Hydrogen Bonding

For each amino acid listed, tell whether its influence on tertiary structure is largely through hydrophobic interactions, hydrogen bonding, formation of salt bridges, covalent bonding, or some combination of these effects.
a. Tyrosine