Describe the 4 levels of structure found in proteins. How does the sequence of amino acids determine protein function? How does molecular shape influence protein function?
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A: Please follow step 2 & 3 for detailed explanation.
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Q: In Protein structure: a). Write the name of the four levels of protein structure,
A: Answer of the question is below,
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Q: . Draw an annotated diagram to illustrate the four levels of protein structure
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Q: explain the four levels of protein structure
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- what are the four levels of protein structure? what stabilizes each level of folding? what environmental factors affect protein folding?Describe the four levels of protein structure and what kind of forces create each level of structure?d) Describe what is meant by the primary structure of a protein? e) At the secondary level of structure, protein molecules will fold in either of two ways. • What are these two secondary forms of folding called? • What do these two forms look like structurally? • How is their structural arrangement stabilised? f) Describe the tertiary structure of a protein. g) Describe the biological function of the peptide hormone insulin. h) Haemoglobin is an example of a quaternary protein. Briefly describe the structure of this protein and state its biological function. Part 2 Monosaccharides and disaccharides are two of the sub-classes of Carbohydrates. Structure B shown below is a specific example of a monosaccharide. H HO Structure B CH₂OH H OH H OH H OH a) Name Structure B and describe its function within cells. b) State the name of a disaccharide that contains this molecule (Structure B) and describe its structure. c) A branched polysaccharide made up of many monomers of Structure B bonded…
- d) Describe what is meant by the primary structure of a protein? e) At the secondary level of structure, protein molecules will fold in either of two ways. • What are these two secondary forms of folding called? • What do these two forms look like structurally? • How is their structural arrangement stabilised? f) Describe the tertiary structure of a protein. g) Describe the biological function of the peptide hormone insulin. h) Haemoglobin is an example of a quaternary protein. Briefly describe the structure of this protein and state its biological function.Discuss the different structures (primary, secondary, tertiary, and Quaternary structures) of protein. What are the five factors that promote protein folding and stability. (Hint: One factor is the Hydrogen bond). Extra Hint: Another factor is the Hydrophobic effect.Protein folding is critical for function because the properties of a protein arise from its overall shape and the distribution within that shape of the various amino acid side-chains. Which of the following statements about protein three-dimensional structure are correct? 1) the folding pattern of a protein is ultimately determined by its amino acid sequence. 2) proteins tend to fold in such a way that the hydrophobic amino acids are buried in the interior, while hydrophilic amino acids are exposed at the surface. 3) the chemical interactions within a protein molecule that support its overall folded structure are mostly covalent C-C (carbon to carbon) bonds between amino acid side-chains. 4) the overall folding pattern/shape of a protein molecule is termed its primary structure. 5) during evolution, the three-dimensional structure of a protein is often more strongly conserved than its amino acid sequence. More than one answer might be right
- A mutation leads to a change in amino acid from valine, an amino acid with a nonpolar side chain, to aspartic acid, an amino acid with a polar, negatively-charged side chain. Do you think that the following levels of protein structure change? If so, how and why? If not, why not? Please frame your answer in terms of chemical bonds and interactions. (primary structure, secondary structure, tertiary structure, quartenary structure)Which protein structure is due to interactions between amino acid side-chains? tertiary, quaternary, secondary, or primary?What are the four levels of protein structure and what type of bond is primarily responsible for each level?
- Describe as completely as possible, the four levels of protein What type of bonds hold a protein together at the primary level? What type of bonds maintain the protein at the secondary and tertiary level? Give an example of secondary, tertiary, and quarternary level proteins. At which level is the protein functional? What happens (at a molecular level) when a protein is denatured?In a subunit of a protein, arginine and aspartic acid have an ionic interaction between their side chains. Part a) If arginine is changed to glutamic acid, would the ionic interaction's stability increase, decrease, or not change and what effect would it have on the protein structure? Explain why. Part b) If arginine is changed to lysine, would the ionic interaction's stability increase, decrease, or not change and what effect would it have on the protein structure? Explain why. Part c) If arginine is changed to isoleucine, would the ionic interaction's stability increase, decrease, or not change and what effect would it have on the protein structure? Explain why.Why is the 3-Dimensional structure important for protein function? What factors or agents can denature protein structure? Give examples (more than one factor) Why denaturation affect the function of proteins? Explain the structure - function relationship.