Great video, the only thing I’d specify if I’m not wrong is that quaternary structure doesn’t have disulfide bonds holding together the sub-units because the quaternary structure proteins have to change their conformational status in case they bind a substrate, disulfide bonds would create a rigid structure that is not super incline to conformational changes.
Are there any physical forces that can cause protein denaturization, either by breaking the bonds themselves or damaging the Solvation Shield? For example vigorous shaking of a protein, striking it with various electromatic waves, applying external positive or negative charges etc.
michaelslarc But I have also heard the reason we cook them is for easier chewing purposes because of the type of teeth and strength of the jaw humans aren't meant to eat raw meat (African ancestors likely ate a diet consisting mostly of fruit). I don't think it's likely we would have been intelligent enough to figure out that we were cooking food because it made it easier to digest, simply to chew. We had to change to survive, makes complete sense. Though I'm not on the side of vegetarianism here, which is what it may sound like. What I am trying to figure out is... If we get a fever to denature a virus, we are the rendering it useless or making it not do what it is designed to do? Then when a protein is denatured to the extent of inactive is it really doing everything it is supposed to do? I wonder this off of the idea that we have a LOT of depressed people in the US, so many on drugs (legal or not) or alcohol to control these issues. Tryptophan regulates serotonin which regulates mood, and is said to be one amino acid highly effected by heat. So when we are cooking that turkey at 300+ degrees how much is actually left for our body to use? Taurine is another example, and is now being put into energy drinks. How denatured are these amino acids when cooked and are the useful to us like they once were? Maybe once upon a time eating cooked meat was what kept us going out of necessity, but is it now contributing to our failing health? I'm not sure, but I can't find anything to help me answer these questions.
Hello, according to my biochem class the denatured/cooked proteins are easier to breakdown into amino acids, due to the unfolded structure, which are then absorbed readily. We break down proteins into its amino acid components and then use the amino acids to make our own bodily proteins. As for burnt proteins I have no idea.
Thank you! I have doubt: is it possible for a protein to be active in its primary structure ( the native state to be just the primary structure)? if so, can you give me an example? Thank you :)
I feel like the Ph category is inaccurate. After all cant you have acid or base catalyzed hydrolysis of the peptide bonds, and therefore disrupting the primary structure?
Are there any physical forces that can cause protein denaturization, either by breaking the bonds themselves or damaging the Solvation Shield? For example vigorous shaking of a protein, striking it with various electromatic waves, applying external positive or negative charges etc.
That's a very good question, and I hope someone can answer this in detail! I've seen a thread online that says mechanical forces can denature proteins. I am not sure how that works, and what level of protein structure mechanical forces can break down to. Whisking egg white itself with a hand mixer make the egg white fluffy, but after a day or so letting the fluffy egg white sit in the fridge, it returns to its original state (well, it looks like it is?) So, I guess it doesn't affect the folding, but only causes a temporarily disturbance in the matrix? Also, EM waves such as X-ray and short wavelength UV break chemical bonds, so would it break down the primary structure of protein? I am confused because the 3D structures can be determined by shooting X-rays to crystallized protein... ?? Please help!
