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Biochemistry

Learn the toughest concepts covered in Biochemistry with step-by-step video tutorials and practice problems by world-class tutors

4. Protein Structure

Alpha Helix Hydrogen Bonding

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Alpha Helix Hydrogen Bonding

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in this video, we're going to talk about Alfa Helix hydrogen bonding. So, as you guys already know, Alfa Ulysses are stabilized by interchange, hydrogen bonds and recall. What we mean by interchange is that these hydrogen bonds form within the same single poly peptide chain. And there are not multiple poly peptide chains involved with stabilizing in Alfa Helix. And so these hydrogen bonds form between the amino and the Carbonnel groups in the peptide backbone. And so what this means is that the are groups of amino acids are not involved with the hydrogen bonding that stabilizes and Alfa Helix. And so this bullet point here applies not only toe Alfa Ulysses, but also to other secondary structures as well, such as beta sheets, which we'll talk about later in our course. Now these next two bullet points here are dedicated to telling us how Alfa he looks, hydrogen bonding works and the way that it works is that a carbonnel group of an amino acid residue in an Alfa helix well hydrogen bond to the amino group that is four residues away towards the C terminal end of the peptide. And so another way to say that same thing is that the Carbonnel Group of Residue X will hydrogen bond to the amino group of Residue X plus four away towards the C terminal. And and this also applies for the amino groups where the amino group of an amino acid residue in an alfa helix will hydrogen bond to the Carbonnel Group of a residue X minus four away towards the end terminal end of the peptide. And so, essentially, What we're saying here is that the Carbonnel group of an amino acid residue in an Alfa helix well hydrogen bond to the amino group of a residue X plus four away towards the C terminal, and and the amino group of an amino acid residue, which we know has a nitrogen atom in it. Well, hydrogen bond to the residue that is X minus four away towards the end terminal end. And so the end in the amino group can remind you of the negative sign in the X minus four here to distinguish, uh, the X Plus four in the car bottle group from the X minus four with the Amino Group. And so because Alfa Helix hydrogen bonding works in this fashion, that we described up above. Therefore, that means that the both the first and the last four amino acid residues oven Alfa Helix will not fully participate in Alfa Helix hydrogen bonding. And we'll be able to understand how that works a little bit better down below in our example of Alfa Helix hydrogen bonding. So notice in this example, what we have is a hex of peptide or a peptide with six amino acid residues, and we know that it has six residues because it has a total of six different are groups throughout our peptide, and so essentially, what you'll notice is the left side. Over here is the amino group with the ferry. Amino, uh, is the amino terminal with the free amino group, and the right side is the C terminal with a free car box elite group. And so, essentially, what you'll notice is that the way that the hydrogen bonding works is that the Carbonnel group of an amino acid residue will hydrogen bond to the amino group of a residue X plus four away. So this pink line that's being highlighted in green here is essentially showing the hydrogen bond that forms and so Essentially, what you'll also note is that the amino group will vice versa hydrogen bond to the Carbonnel group of a residue X minus four away. And so notice. Here we have another hydrogen bond that's forming in this Alfa helix. But we also know that the first and the last four amino acid residues do not fully participate in Alfa Helix hydrogen bomb it. And so the first four residues would be these first four residues. And then the last four residues would, of course, be these last four residues. And so what that means is that none of the residues in this Alfa helix are participating fully in Alfa Helix hydrogen bonding. And so it turns out that the total number of hydrogen bonds in an Alfa helix is equal to the number of amino acid residues that are participating in the Alfa Helix minus this magical number four here. And so, um, we can put this four here and so essentially because we have a total of six amino acid residues, if we subtract four, that tells us that we have a total of two hydrogen bonds participating in that half a helix, and both of those hydrogen bonds are highlighted in pink shown here and so moving forward, we'll be able to get some practice utilizing these concepts in this video. And so I'll see you guys in our next example video.
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Alpha Helix Hydrogen Bonding Example

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all right. So this example problem asks. Which residue does the Carbonnel Group of the 21st residue and a 30 residue Alfa Helix hydrogen bond to and so down below? I've drawn an Alfa helix, and we know that this Alfa helix has a total of 30 amino acid residues in it. And so we're specifically being asked about the 21st residue. So let's imagine that the 21st residue is somewhere at this position here on our Alfa Helix and noticed that were specifically being asked about the car bottle group of this 21st residue. And so recall from our previous lesson videos that the Carbonnel group of an amino acid residue in an Alfa he looks will hydrogen bond to the residue that is X plus four away towards the C terminal end. And so because we're not being asked about the amino group, we're not going to use the X minus four here for this problem, so we could go ahead and cross this portion off. And so because our X here is referring to the 21st residue, we could essentially bring that over here so we could take our 21st residue And then, of course, we can add four to it. So plus four. And that gives us 25. So this is our answer. And essentially, what we're saying is that the Carbonnel Group of the 21st residue well, hydrogen bond to the amino group of the 25th of residue and so option A here is the correct answer. We go ahead and indicated as being correct. And so that concludes this example problem, and I'll see you guys in our practice videos.
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Problem

The oxygen-storage protein myoglobin has 8 α-helices in its single polypeptide chain. Its 67th residue is near the center of a 19 residue α-helix. Which residue does the amino group of myoglobin’s 67th residue hydrogen bond to?

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Alpha Helix Hydrogen Bonding

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So now that we know how Alfa Helix hydrogen bonding works, let's talk about Alfa Helix Net die poles and so Alfa Ulysses have an overall net die poll. And this is due to the fact that the direction of all of the polar peptide bonds are forced to face the same direction because of all of the interchange hydrogen bonds and so we'll be able to see how that works down below. But essentially what's happening is that there's a net electron density being shifted towards the C terminus end the car box will terminus and so negative charges going towards the C terminus. And and what that means is that the end terminus of the Alfa Helix is going to result with a net positive charge. Whereas the C terminus, on the other hand, is gonna end up having a net negative charge. So let's take a look at our example down below of the Alfa, he looks net dipole and so what we've got is our right handed Alfa Helix here, and the peptide bonds notice are all highlighted in pink and so you can see that for all of these peptide bonds that are shown here all of them are facing in the same direction. So in the direction that I'm talking about is that the Carbonnel Group of all of the peptide bonds is facing towards the C Terminus end. And so the Carbonnel Group, remember, has a net negative charge on it. So you've got net negative charge pointing towards the C terminus end. So essentially, what we've got is a net dipole going in this direction and so negative charges, Um, essentially pointing towards us and plus for all of these hydrogen bonding hydrogen bonds that air forming here. So all of these yellow hydrogen bonds, essentially electron density of the Carbonnel group is being donated to up forwards to the amino group up above. So you have this shift and electron density towards the car boxful terminus. So over here, towards the car boxful terminus, we have a negative charge. And then that means that the amino terminus, on the other hand, is gonna be left with a net positive charge. And again, this has to do with the hydrogen bonding orienting the carbonnel groups for all the peptide bonds and the same exact orientation and over a net effect of all of these peptide bonds that creates the overall net dipole that we see with Alfa jealousies and really this net dipole is a really unique feature off Alfa He'll ISI. So it's important to keep that in mind because we don't really see this die poll with other secondary structures like beta sheets, for instance. So that's something important to keep in mind, and so we'll be able to get some practice utilizing these concepts in our practice videos, so I'll see you guys in those videos.
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Problem

True or False: Negatively charged residues near the α-helix N-terminal are stabilizing due to its net dipole.

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Problem

Triose phosphate isomerase (TPI) is a crucial enzyme involved in the glycolysis pathway and contains 14 α-helices. Considering the net dipole of the α-helix, which of the following would be most destabilizing to TPI’s structure?

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Problem

The hemagglutinin protein in influenza virus contains a remarkably long α-helix with 53 residues.

A. How long is the α-helix? _____________

B. How many turns does this α-helix have? _____________

C. How many hydrogen bonds are present in this α-helix? ______________

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Problem

Which of the following statements about α-helices is false?

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