Hi in this topic we're gonna be talking about protein regulation. So proteins need to be regulated because they don't always need to be active. So sometimes or sometimes they need to change their activity based on the needs of the sound. And so in this video we're gonna talk about um protein regulations that are caused from Covalin modifications to the protein itself. So modifications so the proteins can affect their activity. So let's go through a few different types of protein modifications that exist. So the first one is going to be false correlation and that's the reversible edition of a phosphate group somewhere on the protein. And so this caught this brings with it two different negative charges and that can result in confirmation all changes. Um And so the enzymes responsible for you know adding or removing this phosphate are called kindness is when they add it and phosphate. Asus when they remove it. Um So phosphor relation is that is a really big one that we're going to talk a lot more about in future topics. A second one is called like oscillation and that's gonna be the reversible edition of carbohydrates meaning that carbohydrates can be added or they can be removed. And there's two main types of this that's gonna be the end linked um If it's attached to a nitrogen and it's going to be called o linked if attached to an oxygen which makes complete sense. Um So glad consolation is a big protein modifying process. Now, modifications can also occur by the covalin addition of lipids. So for instance glycol lipids are lipids that are linked to um Olivo sacha rides which which are sugars and then can be added to proteins. So you can have lipids, you can add sugars, you can add proteins and you can add everything to a protein essentially and all of them have different effects. So um you don't necessarily need to know these types of names but you may see them in your textbook and things are like ventilation, um Morris titillation and they're all names kind of on their lipid type but all of these lipids and sugars and things can be added to proteins to affect their function. Um Now there's two other types of protein modifications that I want to just hit out really quickly. One is called Ubiquity Nation. Ubiquity Nation. Ubiquity Nation labels the protein with another protein called the ubiquity. And that protein is really sort of marks the protein to be degraded. And then you also have cleavage and that is just sort of cutting off a section of the protein and usually out of everything that I've talked about, cleavage is really the only irreversible one. So once you chop the protein up, not easily put back together. And so um so cleavage is really important for a variety of functions of the protein including getting them to certain organelles or sort of sequestering them in one area. So if we look at, let me back up here we can look at different types of protein modifications. We have phosphor elation which is gonna be the addition of the phosphate wave like oscillation which is the addition of um sugars or Allah go sacha rides to the protein. We have like a lipid binding. So we have sugars here attached to lipids which sort of anchor the protein inside of some type of bi layer. We have ubiquity ubiquity nation which attaches ubiquity for degradation. And then we also have cleavage in which you can see all these proteins are a little bigger. But then there's a section here on this one that's been cut out and so that's going to be cleavage of the protein. So these are the types of protein modifications. So now let's move on.
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GTP and Calcium Binding
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so another type of protein regulation that I really want to talk about is the GTP and calcium binding and so binding. So let's first talk about GTP so binding and hydraulic sis of GTP acts as a major source of protein regulation and how it does this is because proteins can bind to G. T. P. In a special sort of domain or binding site GTP binding domain and then um GTP is usually hydrolyzed to form G. D. P. And in this process it can result in confirmation all changes of itself um that usually in activates its GTP form and then when it does this it can control you know its own self so the protein itself or it can control the functions of other proteins that it might be bound to. And so an example of this is going to a big example of this is gonna be the Wrasse protein and that's a major GTP binding regulator. And actually wrasse is sort of mis regulated or mutated in a ton of cancer. So it's really important for protein regulation to have this GTP GDP um transition taken care of and so um I'm going to give an example of this in a second if it's not entirely clear. But first I want to talk about the second form and that's binding of cal calcium can regulate a variety of proteins. So calcium concentration has generally kept very low in the side of saul and so if for some reason something triggers a change in that concentration. So there is now a high concentration of calcium. The side of saul it can activate or inactivate a bunch of proteins that bind calcium and respond to calcium signals. So calcium is a big protein regulator. But let's get back here to the GTP protein. So you can see here that there's an inactive form of this protein with uh some type of G protein bound GDP and then it becomes activated when it then has G. T. P. And so um proteins can go back and forth between these two states um inactivating or activating itself. Or it can inactivate or activate say other proteins that it might be bound to. For instance if this is a third protein it can inactivate this protein or it can activate this protein depending on how the particular g. Protein works. So that's GTP hydraulic sis and calcium binding. So now let's move on.
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Protein Machines
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Hi in this video we're gonna be talking about protein machines. So protein machines are protein complexes that contain 10 or more proteins. And these machines generally have interchangeable or dynamic and dynamic parts, meaning that the parts are constantly coming in, they're moving around, they're changing being replaced. So these protein machines are actively moving protein machines. And so in order for these protein machines to have a function, each part has to be specific or positioned in a very specific way so that the protein can exert its function. So control of these machines or how these machines are regulated. Remember this is a protein regulation topic um depends on control of each individual part. So if there's one protein missing that protein machine isn't gonna work. So each protein of these 10 or more proteins have to be positioned correctly and regulated independently so that they all can come together and work as a single machine. So if you were to look at what this looks like, this is an example of one. Um you don't need to know anything about this right now. Um or what all these proteins are. Just get an overall view here that there's a bunch of proteins involved in this protein machine and each one of them have to be independently regulated um to arrive here at the right time for the right function. And so protein machines are super important and a big part of protein regulation so that they can exert their function. So now let's move on
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Problem
Which of the following is not a protein modification that allows for protein regulation?
A
Ubiquitination
B
Phosphorylation
C
Glycosylation
D
Noncovalent interactions in the binding site
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Problem
Hydrolysis of GTP to GDP causes what to occur to a GTP-Binding protein
A
It marks it for degradation
B
It cleaves it
C
It activates it
D
It inactivates it
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Problem
To regulate large protein complexes there is a single, powerful regulator of the entire complex.