Does each polypeptide have it's own function, or do they sometimes collaborate for new functions (emergent properties)? What are the most important uses of amino acids in the body? What is the largest known polypeptide?
In response to your second question, the most important uses of amino acids in the body are to make proteins necessary for bodily functions. There are some amino acids considered essential because the body cannot make them and needs to get them from outside sources. Much of the digestive system, protein synthesis, metabolism, and repairs in the body need amino acids for them to be carried out.
To answer your first question, yes polypeptides can have their own functions and if they bond together they form proteins which then have their own functions as well.
To help answer your third question, here is a website that goes into detail about the largest known protein/polypeptide, titin: https://pdb101.rcsb.org/motm/185#:~:text=Titin%20is%20the%20largest%20protein,more%20than%2034%2C000%20amino%20acids.
For your second question I found that amino acids are used in the body to break down food in the body and help the body to grow. Amino Acids also repair body tissue and are used as a source of energy in the body. Here is the link: https://medlineplus.gov/ency/article/002222.htm
1. What specifically can proteomes reveal about the cells and their activity? 2. What is the least common organic polypeptide? 3. How is the denaturing of proteins used inside of the body?
In response to your third question, the denaturation of proteins is not really used inside of the body. It is bad for cell survival and can potentially lead to Parkinson's disease or Alzheimer's. The abnormal folding of proteins in their bodies from denaturation of proteins is what leads to many of the conditions arising.
For your second question, because polypeptides have an (essentially) unlimited amount of possibilities for creation, there isn't necessarily a 'rarest' polypeptide as thousands (probably much more than that) could technically exist never will, so I suppose whatever those may be would be considered the rarest polypeptides (textbook)
TO answer your first question, studying proteomes tells us what it is that makes up entire organisms for a general overview and smaller parts of the organisms. Essentially, it tells us what chemicals are involved in different forms of life and how many of these chemicals there are. https://baker.edu.au/research/laboratories/molecular-proteomics/why-proteomics
1. How can polypeptides be so long (such as the titin one) and still fit within a cell? 2. Is there a limit to the number of amino acids in a polypeptide? 3. Can the terms enzyme and protein be used interchangeably, or do they have different meanings?
For your first question, the molecules titin is found in the sacromere of a striated muscle cell. The length of titan is 1um, and the sacromere is 2.5, so although it's quite big compered to the cell, it still fits comfortably. https://proteopedia.org/wiki/index.php/Titin_Structure_%26_Function#:~:text=Titin%2C%20a%20polypeptide%20chain%20protein,immunoglobulin%20(Ig)%20and%20fibronectin.
To answer your second question, there is no real limit to the amount of amino acids that can be in a polypeptide from what I have found. I do know the largest polypeptide is the titin molecule inside of muscle tissue which has a little over 35,000 amino acids making it the closest to a limiter to the amount of amino acids it can have.
To answer your third question, no they are interchangeable. Enzymes are functional proteins, whereas proteins are both functional and dysfunctional. https://www.differencebetween.com/difference-between-enzyme-and-vs-protein/#:~:text=Enzymes%20are%20functional%20proteins%2C%20whereas,be%20either%20functional%20or%20structural.&text=Unlike%20other%20proteins%2C%20enzymes%20are%20highly%20substrate%20specific%20molecules.&text=Proteins%20can%20be%20digested%20or%20broken%20down%20by%20enzymes%20(proteases).
To answer your third question, no enzyme and protein can not be used interchangeably. This is because enzymes are biological catalysts, while proteins can be involved in the formation of structures, transportation, catalysis, and regulation of biological processes
Here is an article that goes into more detail: https://pediaa.com/what-is-the-difference-between-enzyme-and-protein/#:~:text=The%20main%20difference%20between%20enzyme,and%20regulation%20of%20biological%20processes.
1. How is protein involved in muscle growth? 2. I have heard eating proteins helps keep you warm. Is this true, if so why? 3. What is the difference between right and left-handed amino acids?
In response to your second question, eating proteins does keep you warm because of a process that occurs whenever you eat food. The process is called diet-induced thermogenesis (DIT)and high protein foods increase DIT more than foods with a lot of starch or fat in them.
To answer your first question, Protein is needed because it is used to repair the cells and create new satellite cells which fill in the muscle and repair it. When you begin working out to increase muscle mass the muscles will tear and then when it heals it will be bigger. Citation https://pubmed.ncbi.nlm.nih.gov/11255140/
To answer your third question, the only difference between right and left handed molecules is the side in which most of the molecules fall. It is unknown why but for most amino acids, the contents of the molecule fall left of the central carbon. I wondered by you can't just look from the other side, but I assume there is a predetermined orientation that is considered the front of a molecule. Molecules have both right and left handed version, which for the same molecule would mean that all of the atoms are creating a mirror image of each other. This property is called chirality. Source: https://www.vanderbilt.edu/AnS/physics/astrocourses/ast201/aastruct.html
to answer your first question i found a website that talks about how your muscles use protein to help rebuild tissue. https://www.acefitness.org/education-and-resources/professional/expert-articles/6960/9-things-to-know-about-how-the-body-uses-protein-to-repair-muscle-tissue/#:~:text=The%20muscle%20damage%20initiates%20a,repair%20tissues%20damaged%20by%20exercise.
to answer your second question, I found a website that talks about how proteins can help keep you warm because they take longer to digest and it produces heat. https://timesofindia.indiatimes.com/life-style/health-fitness/diet/5-foods-that-can-keep-you-warm-in-winter/photostory/72279460.cms#:~:text=But%20there%20is%20a%20simple,keep%20you%20warm%20in%20winter.
To help answer your first question here is a website that I found: https://inbodyusa.com/blogs/inbodyblog/the-relationship-between-nutrition-and-muscle-growth/#:~:text=Protein%20is%20extremely%20important%20in,muscles%20slightly%20tear%20during%20exercise.
1. Is there a disease or disorder that prevents cells from synthesizing proteins 2. What is the most common polypeptide? 3. How many polypeptides can a ribosome synthesize at once?
In response to your second question, I don't believe there are any specific polypeptides that are the most common, but some of the more common ones would be insulin and growth hormones, which are used frequently in the human body.
Going off of my previous response, now on to your first question. I believe cancer is caused by cells not synthesizing right, leading to abnormal growths of cells (tumors). Diabetes, I believe, would also be caused by the cells not synthesizing proteins right, leading to a lack of insulin. However, I am not sure if there are any disorders or diseases that prevent the cells from doing their thing, I was only mainly able to find diseases caused by this lack of synthesized proteins. Sorry if this didn't directly answer your first question, this is just what I was able to find. Sources below!
1. It says Polypeptides are the main component of proteins. What other components are there? 2.How does the sequence of amino acids in a polypeptide affect it? 3. is there any way a gene sequence could be shorter than a polypeptide sequence?
In response to your first question, proteins also consist of amino acids, a carboxyl group, a hydrogen atom, and often something called a side chain. I attached a link about protein structure below, hope this helps!
For your second question, I found that the sequence of the amino acid ultimately determines the shape, function and size of a protein. Here is the link: https://courses.lumenlearning.com/boundless-biology/chapter/proteins/#:~:text=The%20sequence%20and%20the%20number,known%20as%20a%20peptide%20bond.
For your third question, I found that a genome sequence does not show many ORF's longer than 50 codons. Most genome sequences are longer than 50 codons. I also looked up an average amino acid has around 3 codons. For a polypeptide with 20 amino acids, there are roughly 64 codons. So, in conclusion, I suppose there really is no genome sequence that is shorter than a polypeptide sequence. I hope this helps https://www.ncbi.nlm.nih.gov/books/NBK21136/
1. Can polypeptides be created and imitated artificially? If so, what uses does this have? 2. How does protein misfolding work? More specifically, what does this process look like? 3. If the process of protein synthesis goes awry and an issue develops within a person's body and cells, are there any treatments that can be used to help fix this process?
In response to your second question, I found that proteins misfolding results when a protein follows the wrong folding pathway or an energy-minimizing funnel. Most of the time protein folding happens spontaneously. Here is the link I found: ature.com/scitable/topicpage/protein-misfolding-and-degenerative-diseases-14434929/#:~:text=As%20discussed%20already%2C%20misfolded%20proteins,and%20misfolding%20can%20happen%20spontaneously.&text=Proteins%20that%20have%20problems%20achieving,properly%2C%20using%20energy%20from%20ATP.
To answer your 3rd question, protein synthesis can go wrong and it will cause disease phenotypes. Polypeptide errors can result in cell death. There has not been much research into the field of protein synthesis error and there does not seem to be any treatments to help fix the process. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2764353/#:~:text=Errors%20in%20protein%20synthesis%20disrupt,shape%20gene%20and%20genome%20evolution.&text=At%20this%20error%20rate%2C%2015,and%20cell%20death%20(e.g.%20Ref.
1. How fast do condensation reactions occur between amino acids? 2. What is an example of the protein function of catalysis? 3. Have proteins ever been synthesized artificially? If they have been synthesized, how did scientists do it?
To answer your 2nd question, an example of a protein function of catalysis is working as an enzyme. Proteins that function for catalysis that will increase the rate of all chemical reactions within the cell. I got my information from https://www.ncbi.nlm.nih.gov/books/NBK9921/
To help answer your 1st question, the condensation reaction rates are dependable on the type of amino acid. I was unable o find a set rate that accumulates an overview of all amino acids but I was able to find an equation. The reaction rate (speed at which it take chemical reactions to occur) can be measured by using the equation: d[Z]/dt. T stands for time and [Z] is the concentration of the substance. Hope this helped for more information check this link out:
1) What are some of the 20 different amino acids found in polypeptides? 2) Is it required for the polypeptides to have all 20 of these amino acids? 3) Can someone help me better understand question 1a on page 90 for the DBQs?
To answer your second question it is not required for each polypeptide to use all 20 amino acids, as not all polypeptides are made up of 20 amino acids.
To answer your third question, I also had a hard time with this question, and I'm not completely sure if I am right, but hopefully this helps. I answered that the third hypothesis was the one supported with evidence because it is the only hypothesis that backs up the statement. So whereas the first 2 hypotheses simply state why they think there are only 20 amino acids used, the third hypothesis gives a reason why, which was explaining that it was difficult to create another amino acid. I hope this helps!
Question 2-no those 20 are the amino acids ribosomes synthesize (I am not sure if they are able to synthesize more and these 20 are just the most common). They are each options for polypeptides to be made of but it is not required all 20 are used at once. It can be as few as 3 to be considered a polypeptide. I believe your question is coming from the section that says if it is fewer than 20 amino acids it is usually referred to as an oligopeptide. These 20 do not have to all be different it is just talking about the amount of amino acids bonded in a single chain. There can be the same amino acids within a chain.
1. what is the most common polypeptide found in the human body? 2. is there any common reason to have a modified amino acid or doses it vary case by case? 3. what is the second most common function for genes.
To answer your first question, I found that the most familiar polypeptide in the body might be insulin. Many hormones like this are polypeptides :) In the textbook, it also mentioned hemoglobin (containing 4 polypeptides) and these proteins are everywhere in our blood. Source: https://www.thoughtco.com/what-is-a-peptide-definitionexamples4177787#:~:text=Examples%20of%20peptides%20include%20the,glucagon%20(a%20hyperglycemic%20factor).
For your 1st question, I was unable to find to find a clear number one answer on the "most" common polypeptide but one that is most familiar is Insulin. Insulin is a hormone in the body responsible for signalling cells to absorb glucose. If you would like more information on the polypeptide structure (including primary, secondary, tertiary, and quaternary) of Insulin here's an educational link: https://www.biotopics.co.uk/as/insulinproteinstructure.html For more a more detailed information on polypeptides and polymerization check his link out: https://www.sciencedirect.com/topics/chemistry/polypeptide
To answer your second question... I found a great video! https://www.youtube.com/watch?v=zIKcOQg-2YQ In the first 1:20, she explains 3 reasons why post-translational modifications occur. Then, when proteins are localized, she explains that they make modifications to serve more of their own individual purposes. The video also goes over different known changes that occur and what the effect is on the protein. Overall, modifying amino acids allows the proteins to react and adapt to the changes that may occur in the environment after translation. I hope that this helps!
To answer your second question, most amino acids (and in turn, proteins) are modified for a number of reasons, such as to mediate proper protein folding or to increase stability.
More information about the reasons for protein modification can be found here: https://www.thermofisher.com/us/en/home/life-science/protein-biology/protein-biology-learning-center/protein-biology-resource-library/pierce-protein-methods/overview-post-translational-modification.html#:~:text=For%20example%2C%20many%20proteins%20are,e.g.%2C%20nucleus%2C%20membrane).
To answer your 1st question, protein hormones do not have any enzymatic activity and target specific organs to help with biological actions. Scientist are still researching this topic but cyclic adenosine monophosphate has been hypothesized to play a role in on how protein hormones function. For example, the pancreas houses the hormone insulin which helps absorb glucose. Insulin is created through biosynthesis in the proinsulin in the pancreas. Hopefully this helped, if you would like more information check this link out: https://www.britannica.com/science/protein/Protein-hormones#ref593848
To help with your third question... Think of a proteome like a genome. A genome maps out all of the genes in an organism's body - the complete set of all its genes. A proteome maps out all of the proteins produced in an organism's body. Proteomes are typically more different from organism to organism because the proteins/amino acids vary in each. This means proteomes are unique in each individual. Here is an IB Bio video I watched if you would like to as well: https://www.youtube.com/watch?v=JnCg33-bIEk I hope this helped!
1. Is it possible for another amino acid to be created and used as much as the main 20 are? 2. What causes proteins to only complete certain functions? For example, what makes plasma proteins only complete certain functions, like blood clotting and not muscle contraction? 3. What are some examples of denaturation being completed?
To answer question 2, the function of proteins depend on their shape and, more importantly, their amino acid sequence. As mentioned in the textbook, fibrous proteins are used in muscle contraction, meaning that globular proteins cannot perform that action.
Question 3- I have no way of explaining these examples in a way that makes sense haha, but this website does an excellent job. It talks about different types of foods and examples of denaturation. https://biologydictionary.net/denature/
1. What is an example of how heat causes denaturation besides the one mentioned? 2. How do selenocysteine and pyrrolysine discredited the idea of amino acid diversity? 3. What would happen to the body, specifically the eyes if the Rhodopsin protein malfunctioned.
1) The question at the end of the chapter has stumped me: Why are proteomes larger than genomes? 2) Why exactly are three bases of genes necessary for each amino acid in the polypeptide? 3) Is there a specific term for when multiple polypeptides are linked together to form a protein? (and confirmation: the term polypeptide itself refers to the number *amino acids* bonded together in the chain?)
To answer your first question, proteomes are larger than genomes because a gene can be made up of multiple different proteins due to the gene sequences being spliced or the proteins being modified after translation.
To answer question 3, there is no term to distinguish proteins with differing polypeptide amounts. A protein with one polypeptide is a protein, just as one with 20 polypeptides.
Question 2- This is because codons come in sets of 3 and are what determine the coding of amino acids. I'm not sure if this makes sense or gives enough information, so here's a handy website that may help. https://www.ncbi.nlm.nih.gov/books/NBK22358/
1. What is the process used to create peptidoglycan in bacteria? 2. What type of organism has the most diverse proteome? 3. How does the sequence of amino acids determine the shape of the protein?
Question 3- Since amino acids are such a large and important part of proteins, the shape of the protein is significantly influenced by the sequence of amino acids. I am not sure how exactly to answer this myself, so instead I have a website link where I found a lot of nice information on this. https://www.nature.com/scitable/topicpage/protein-structure-14122136/
1) I don't exactly understand- What is denaturation and what causes it to happen? What is the result of denaturation? 2) Could amino acids be created artificially? If so, how? What would this benefit? 3) What are the main components of proteins? Which are the most important?
Question 1- denaturation is basically the changing of a protein's original shape. This change is permanent and it happens when weak R group bonds break apart. Globular proteins get their shape from the folding of the amino acids. This is when the R groups bond. When the bond breaks the shape is changed and cannot be reversed.
Question 3- Polypeptide(s) are the main part of a protein. There are 3 different types of protein structures but I don't think that's what you are referring to. I actually cannot find proteins being made of anything other than different sequences of amino acids and amounts of polypeptides. So there is no one being more important than another. Just lots of amino acids.
1) I don't understand what proteomes are. Could anyone give a simpler explanation or even just explain the comparison between them and genomes? 2)Are ribosomes what create the polypeptides and the peptide bonds? 3)This is a lot of questions around one thing I'll try to simplify. Yes, R group bonds are weak but what about general peptide bonds? Collagen is made of 3 wound polypeptides, the winding strengthens it but is it weaker without the R group bonding? Does it break easily still and is this what we refer to when our tendons tear (the bonds are breaking apart?)
Does each polypeptide have it's own function, or do they sometimes collaborate for new functions (emergent properties)?
ReplyDeleteWhat are the most important uses of amino acids in the body?
What is the largest known polypeptide?
To answer your third question, the largest known organic polypeptide is titin which is found in humans and is used for structuring muscle.
DeleteIn response to your second question, the most important uses of amino acids in the body are to make proteins necessary for bodily functions. There are some amino acids considered essential because the body cannot make them and needs to get them from outside sources. Much of the digestive system, protein synthesis, metabolism, and repairs in the body need amino acids for them to be carried out.
Deletehttps://www.healthline.com/nutrition/essential-amino-acids#:~:text=Amino%20acids%2C%20often%20referred%20to,synthesis%20of%20hormones%20and%20neurotransmitters.
To answer your first question, yes polypeptides can have their own functions and if they bond together they form proteins which then have their own functions as well.
Deleteto answer your last question, I found that Titan is the largest known polypeptide at a length of about 27,000 to about 35,000 amino acids.
DeleteTo help answer your third question, here is a website that goes into detail about the largest known protein/polypeptide, titin:
Deletehttps://pdb101.rcsb.org/motm/185#:~:text=Titin%20is%20the%20largest%20protein,more%20than%2034%2C000%20amino%20acids.
For your second question I found that amino acids are used in the body to break down food in the body and help the body to grow. Amino Acids also repair body tissue and are used as a source of energy in the body.
DeleteHere is the link: https://medlineplus.gov/ency/article/002222.htm
1. What specifically can proteomes reveal about the cells and their activity?
ReplyDelete2. What is the least common organic polypeptide?
3. How is the denaturing of proteins used inside of the body?
In response to your third question, the denaturation of proteins is not really used inside of the body. It is bad for cell survival and can potentially lead to Parkinson's disease or Alzheimer's. The abnormal folding of proteins in their bodies from denaturation of proteins is what leads to many of the conditions arising.
Deletehttps://biologydictionary.net/denature/#:~:text=The%20solid%20white%20portion%20that,make%20yogurt%20and%20fresh%20cheese.
For your second question, because polypeptides have an (essentially) unlimited amount of possibilities for creation, there isn't necessarily a 'rarest' polypeptide as thousands (probably much more than that) could technically exist never will, so I suppose whatever those may be would be considered the rarest polypeptides (textbook)
DeleteTO answer your first question, studying proteomes tells us what it is that makes up entire organisms for a general overview and smaller parts of the organisms. Essentially, it tells us what chemicals are involved in different forms of life and how many of these chemicals there are.
Deletehttps://baker.edu.au/research/laboratories/molecular-proteomics/why-proteomics
1. How can polypeptides be so long (such as the titin one) and still fit within a cell?
ReplyDelete2. Is there a limit to the number of amino acids in a polypeptide?
3. Can the terms enzyme and protein be used interchangeably, or do they have different meanings?
For your first question, the molecules titin is found in the sacromere of a striated muscle cell. The length of titan is 1um, and the sacromere is 2.5, so although it's quite big compered to the cell, it still fits comfortably. https://proteopedia.org/wiki/index.php/Titin_Structure_%26_Function#:~:text=Titin%2C%20a%20polypeptide%20chain%20protein,immunoglobulin%20(Ig)%20and%20fibronectin.
DeleteTo answer your second question, there is no real limit to the amount of amino acids that can be in a polypeptide from what I have found. I do know the largest polypeptide is the titin molecule inside of muscle tissue which has a little over 35,000 amino acids making it the closest to a limiter to the amount of amino acids it can have.
DeleteTo answer your third question, no they are interchangeable. Enzymes are functional proteins, whereas proteins are both functional and dysfunctional.
Deletehttps://www.differencebetween.com/difference-between-enzyme-and-vs-protein/#:~:text=Enzymes%20are%20functional%20proteins%2C%20whereas,be%20either%20functional%20or%20structural.&text=Unlike%20other%20proteins%2C%20enzymes%20are%20highly%20substrate%20specific%20molecules.&text=Proteins%20can%20be%20digested%20or%20broken%20down%20by%20enzymes%20(proteases).
To answer your third question, no enzyme and protein can not be used interchangeably. This is because enzymes are biological catalysts, while proteins can be involved in the formation of structures, transportation, catalysis, and regulation of biological processes
DeleteHere is an article that goes into more detail:
https://pediaa.com/what-is-the-difference-between-enzyme-and-protein/#:~:text=The%20main%20difference%20between%20enzyme,and%20regulation%20of%20biological%20processes.
1. How is protein involved in muscle growth?
ReplyDelete2. I have heard eating proteins helps keep you warm. Is this true, if so why?
3. What is the difference between right and left-handed amino acids?
In response to your second question, eating proteins does keep you warm because of a process that occurs whenever you eat food. The process is called diet-induced thermogenesis (DIT)and high protein foods increase DIT more than foods with a lot of starch or fat in them.
Deletehttps://firecareers.com/blog/body-heat-and-protein/#:~:text=High%20protein%20foods%2C%20for%20example,aid%20circulation%20and%20generate%20warmth.
To answer your first question, Protein is needed because it is used to repair the cells and create new satellite cells which fill in the muscle and repair it. When you begin working out to increase muscle mass the muscles will tear and then when it heals it will be bigger.
DeleteCitation
https://pubmed.ncbi.nlm.nih.gov/11255140/
To answer your third question, the only difference between right and left handed molecules is the side in which most of the molecules fall. It is unknown why but for most amino acids, the contents of the molecule fall left of the central carbon. I wondered by you can't just look from the other side, but I assume there is a predetermined orientation that is considered the front of a molecule. Molecules have both right and left handed version, which for the same molecule would mean that all of the atoms are creating a mirror image of each other. This property is called chirality. Source: https://www.vanderbilt.edu/AnS/physics/astrocourses/ast201/aastruct.html
Deleteto answer your first question i found a website that talks about how your muscles use protein to help rebuild tissue.
Deletehttps://www.acefitness.org/education-and-resources/professional/expert-articles/6960/9-things-to-know-about-how-the-body-uses-protein-to-repair-muscle-tissue/#:~:text=The%20muscle%20damage%20initiates%20a,repair%20tissues%20damaged%20by%20exercise.
to answer your second question, I found a website that talks about how proteins can help keep you warm because they take longer to digest and it produces heat.
Deletehttps://timesofindia.indiatimes.com/life-style/health-fitness/diet/5-foods-that-can-keep-you-warm-in-winter/photostory/72279460.cms#:~:text=But%20there%20is%20a%20simple,keep%20you%20warm%20in%20winter.
To help answer your first question here is a website that I found:
Deletehttps://inbodyusa.com/blogs/inbodyblog/the-relationship-between-nutrition-and-muscle-growth/#:~:text=Protein%20is%20extremely%20important%20in,muscles%20slightly%20tear%20during%20exercise.
1. Is there a disease or disorder that prevents cells from synthesizing proteins
ReplyDelete2. What is the most common polypeptide?
3. How many polypeptides can a ribosome synthesize at once?
In response to your second question, I don't believe there are any specific polypeptides that are the most common, but some of the more common ones would be insulin and growth hormones, which are used frequently in the human body.
DeleteSource:
https://laboratoryinfo.com/polypeptide/
DeleteGoing off of my previous response, now on to your first question. I believe cancer is caused by cells not synthesizing right, leading to abnormal growths of cells (tumors). Diabetes, I believe, would also be caused by the cells not synthesizing proteins right, leading to a lack of insulin. However, I am not sure if there are any disorders or diseases that prevent the cells from doing their thing, I was only mainly able to find diseases caused by this lack of synthesized proteins. Sorry if this didn't directly answer your first question, this is just what I was able to find. Sources below!
Sources:
https://sciencing.com/would-happen-cell-didnt-ribosomes-19003.html#:~:text=Ribosomes%20contain%20molecules%20called%20RNA,the%20process%20of%20creating%20proteins.&text=Without%20these%20proteins%2C%20the%20DNA,and%20problems%20such%20as%20cancer.
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4492843/
1. It says Polypeptides are the main component of proteins. What other components are there?
ReplyDelete2.How does the sequence of amino acids in a polypeptide affect it?
3. is there any way a gene sequence could be shorter than a polypeptide sequence?
In response to your first question, proteins also consist of amino acids, a carboxyl group, a hydrogen atom, and often something called a side chain. I attached a link about protein structure below, hope this helps!
Deletehttps://www.nature.com/scitable/topicpage/protein-structure-14122136/#:~:text=The%20building%20blocks%20of%20proteins,side%20chain%20(see%20below).
For your second question, I found that the sequence of the amino acid ultimately determines the shape, function and size of a protein.
DeleteHere is the link: https://courses.lumenlearning.com/boundless-biology/chapter/proteins/#:~:text=The%20sequence%20and%20the%20number,known%20as%20a%20peptide%20bond.
For your third question, I found that a genome sequence does not show many ORF's longer than 50 codons. Most genome sequences are longer than 50 codons. I also looked up an average amino acid has around 3 codons. For a polypeptide with 20 amino acids, there are roughly 64 codons. So, in conclusion, I suppose there really is no genome sequence that is shorter than a polypeptide sequence.
DeleteI hope this helps
https://www.ncbi.nlm.nih.gov/books/NBK21136/
1. Can polypeptides be created and imitated artificially? If so, what uses does this have?
ReplyDelete2. How does protein misfolding work? More specifically, what does this process look like?
3. If the process of protein synthesis goes awry and an issue develops within a person's body and cells, are there any treatments that can be used to help fix this process?
In response to your second question, I found that proteins misfolding results when a protein follows the wrong folding pathway or an energy-minimizing funnel. Most of the time protein folding happens spontaneously.
DeleteHere is the link I found: ature.com/scitable/topicpage/protein-misfolding-and-degenerative-diseases-14434929/#:~:text=As%20discussed%20already%2C%20misfolded%20proteins,and%20misfolding%20can%20happen%20spontaneously.&text=Proteins%20that%20have%20problems%20achieving,properly%2C%20using%20energy%20from%20ATP.
To answer your 3rd question, protein synthesis can go wrong and it will cause disease phenotypes. Polypeptide errors can result in cell death. There has not been much research into the field of protein synthesis error and there does not seem to be any treatments to help fix the process.
Deletehttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2764353/#:~:text=Errors%20in%20protein%20synthesis%20disrupt,shape%20gene%20and%20genome%20evolution.&text=At%20this%20error%20rate%2C%2015,and%20cell%20death%20(e.g.%20Ref.
For your 1st question I believe this should help
Deletehttps://phys.org/news/2019-06-artificial-peptide-bond-formation-clues.html
1. How fast do condensation reactions occur between amino acids?
ReplyDelete2. What is an example of the protein function of catalysis?
3. Have proteins ever been synthesized artificially? If they have been synthesized, how did scientists do it?
To answer your 2nd question, an example of a protein function of catalysis is working as an enzyme. Proteins that function for catalysis that will increase the rate of all chemical reactions within the cell.
DeleteI got my information from
https://www.ncbi.nlm.nih.gov/books/NBK9921/
To help answer your 1st question, the condensation reaction rates are dependable on the type of amino acid. I was unable o find a set rate that accumulates an overview of all amino acids but I was able to find an equation. The reaction rate (speed at which it take chemical reactions to occur) can be measured by using the equation: d[Z]/dt. T stands for time and [Z] is the concentration of the substance. Hope this helped for more information check this link out:
Deletehttps://www.britannica.com/science/reaction-rate
1) What are some of the 20 different amino acids found in polypeptides?
ReplyDelete2) Is it required for the polypeptides to have all 20 of these amino acids?
3) Can someone help me better understand question 1a on page 90 for the DBQs?
To answer your second question it is not required for each polypeptide to use all 20 amino acids, as not all polypeptides are made up of 20 amino acids.
DeleteTo answer your third question, I also had a hard time with this question, and I'm not completely sure if I am right, but hopefully this helps. I answered that the third hypothesis was the one supported with evidence because it is the only hypothesis that backs up the statement. So whereas the first 2 hypotheses simply state why they think there are only 20 amino acids used, the third hypothesis gives a reason why, which was explaining that it was difficult to create another amino acid. I hope this helps!
DeleteQuestion 2-no those 20 are the amino acids ribosomes synthesize (I am not sure if they are able to synthesize more and these 20 are just the most common). They are each options for polypeptides to be made of but it is not required all 20 are used at once. It can be as few as 3 to be considered a polypeptide. I believe your question is coming from the section that says if it is fewer than 20 amino acids it is usually referred to as an oligopeptide. These 20 do not have to all be different it is just talking about the amount of amino acids bonded in a single chain. There can be the same amino acids within a chain.
Delete1. what is the most common polypeptide found in the human body?
ReplyDelete2. is there any common reason to have a modified amino acid or doses it vary case by case?
3. what is the second most common function for genes.
To answer your first question, I found that the most familiar polypeptide in the body might be insulin. Many hormones like this are polypeptides :) In the textbook, it also mentioned hemoglobin (containing 4 polypeptides) and these proteins are everywhere in our blood.
DeleteSource: https://www.thoughtco.com/what-is-a-peptide-definitionexamples4177787#:~:text=Examples%20of%20peptides%20include%20the,glucagon%20(a%20hyperglycemic%20factor).
For your 1st question, I was unable to find to find a clear number one answer on the "most" common polypeptide but one that is most familiar is Insulin. Insulin is a hormone in the body responsible for signalling cells to absorb glucose. If you would like more information on the polypeptide structure (including primary, secondary, tertiary, and quaternary) of Insulin here's an educational link: https://www.biotopics.co.uk/as/insulinproteinstructure.html
DeleteFor more a more detailed information on polypeptides and polymerization check his link out: https://www.sciencedirect.com/topics/chemistry/polypeptide
To answer your second question... I found a great video! https://www.youtube.com/watch?v=zIKcOQg-2YQ
DeleteIn the first 1:20, she explains 3 reasons why post-translational modifications occur. Then, when proteins are localized, she explains that they make modifications to serve more of their own individual purposes. The video also goes over different known changes that occur and what the effect is on the protein. Overall, modifying amino acids allows the proteins to react and adapt to the changes that may occur in the environment after translation. I hope that this helps!
To answer your second question, most amino acids (and in turn, proteins) are modified for a number of reasons, such as to mediate proper protein folding or to increase stability.
DeleteMore information about the reasons for protein modification can be found here: https://www.thermofisher.com/us/en/home/life-science/protein-biology/protein-biology-learning-center/protein-biology-resource-library/pierce-protein-methods/overview-post-translational-modification.html#:~:text=For%20example%2C%20many%20proteins%20are,e.g.%2C%20nucleus%2C%20membrane).
I believe this should help with your second question
ReplyDeletehttps://www.nature.com/scitable/topicpage/protein-structure-14122136/#:~:text=Proteins%20are%20built%20as%20chains,well%2Dadapted%20for%20their%20functions.
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ReplyDeleteTo answer your 1st question, protein hormones do not have any enzymatic activity and target specific organs to help with biological actions. Scientist are still researching this topic but cyclic adenosine monophosphate has been hypothesized to play a role in on how protein hormones function. For example, the pancreas houses the hormone insulin which helps absorb glucose. Insulin is created through biosynthesis in the proinsulin in the pancreas. Hopefully this helped, if you would like more information check this link out: https://www.britannica.com/science/protein/Protein-hormones#ref593848
ReplyDeleteTo help with your third question... Think of a proteome like a genome. A genome maps out all of the genes in an organism's body - the complete set of all its genes. A proteome maps out all of the proteins produced in an organism's body. Proteomes are typically more different from organism to organism because the proteins/amino acids vary in each. This means proteomes are unique in each individual. Here is an IB Bio video I watched if you would like to as well: https://www.youtube.com/watch?v=JnCg33-bIEk
ReplyDeleteI hope this helped!
1. Is it possible for another amino acid to be created and used as much as the main 20 are?
ReplyDelete2. What causes proteins to only complete certain functions? For example, what makes plasma proteins only complete certain functions, like blood clotting and not muscle contraction?
3. What are some examples of denaturation being completed?
To answer question 2, the function of proteins depend on their shape and, more importantly, their amino acid sequence. As mentioned in the textbook, fibrous proteins are used in muscle contraction, meaning that globular proteins cannot perform that action.
DeleteQuestion 3- I have no way of explaining these examples in a way that makes sense haha, but this website does an excellent job. It talks about different types of foods and examples of denaturation. https://biologydictionary.net/denature/
Delete1. What is an example of how heat causes denaturation besides the one mentioned?
ReplyDelete2. How do selenocysteine and pyrrolysine discredited the idea of amino acid diversity?
3. What would happen to the body, specifically the eyes if the Rhodopsin protein malfunctioned.
To answer question 3, rhodopsin mutation can cause a multitude of retinal diseases, most of which involve the bearer of the disease to lose eyesight.
DeleteWikipedia delves into more depth on the subject. https://en.wikipedia.org/wiki/Rhodopsin#Retinal_disease
1) The question at the end of the chapter has stumped me: Why are proteomes larger than genomes?
ReplyDelete2) Why exactly are three bases of genes necessary for each amino acid in the polypeptide?
3) Is there a specific term for when multiple polypeptides are linked together to form a protein? (and confirmation: the term polypeptide itself refers to the number *amino acids* bonded together in the chain?)
To answer your first question, proteomes are larger than genomes because a gene can be made up of multiple different proteins due to the gene sequences being spliced or the proteins being modified after translation.
DeleteSource: https://ib.bioninja.com.au/standard-level/topic-2-molecular-biology/24-proteins/proteome.html
To answer question 3, there is no term to distinguish proteins with differing polypeptide amounts. A protein with one polypeptide is a protein, just as one with 20 polypeptides.
DeleteQuestion 2- This is because codons come in sets of 3 and are what determine the coding of amino acids. I'm not sure if this makes sense or gives enough information, so here's a handy website that may help. https://www.ncbi.nlm.nih.gov/books/NBK22358/
Delete1. What is the process used to create peptidoglycan in bacteria?
ReplyDelete2. What type of organism has the most diverse proteome?
3. How does the sequence of amino acids determine the shape of the protein?
Question 3- Since amino acids are such a large and important part of proteins, the shape of the protein is significantly influenced by the sequence of amino acids. I am not sure how exactly to answer this myself, so instead I have a website link where I found a lot of nice information on this. https://www.nature.com/scitable/topicpage/protein-structure-14122136/
Delete1) I don't exactly understand- What is denaturation and what causes it to happen? What is the result of denaturation?
ReplyDelete2) Could amino acids be created artificially? If so, how? What would this benefit?
3) What are the main components of proteins? Which are the most important?
Question 1- denaturation is basically the changing of a protein's original shape. This change is permanent and it happens when weak R group bonds break apart. Globular proteins get their shape from the folding of the amino acids. This is when the R groups bond. When the bond breaks the shape is changed and cannot be reversed.
DeleteQuestion 3- Polypeptide(s) are the main part of a protein. There are 3 different types of protein structures but I don't think that's what you are referring to. I actually cannot find proteins being made of anything other than different sequences of amino acids and amounts of polypeptides. So there is no one being more important than another. Just lots of amino acids.
Delete1) I don't understand what proteomes are. Could anyone give a simpler explanation or even just explain the comparison between them and genomes?
ReplyDelete2)Are ribosomes what create the polypeptides and the peptide bonds?
3)This is a lot of questions around one thing I'll try to simplify. Yes, R group bonds are weak but what about general peptide bonds? Collagen is made of 3 wound polypeptides, the winding strengthens it but is it weaker without the R group bonding? Does it break easily still and is this what we refer to when our tendons tear (the bonds are breaking apart?)