Explain why the cartoon pictures of proteins often look like ribbons coiled and laying flat. Your description should include the shape of the NMA molecule's amide bond as well as the fact that all peptides that make up a protein are linked by amide bonds.
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Explain why the cartoon pictures of proteins often look like ribbons coiled and laying flat. Your description should include the shape of the NMA molecule's amide bond as well as the fact that all peptides that make up a protein are linked by amide bonds.
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- How can a protein’s potential function be determined from a protein’s primary structure? I assumed this was not possible, I thought its function was determined from its 3-dimensional structure only. Thank you for explaining this.Hydrogen bonding is important at what level of protein structure (primary, secondary, tertiary, or quarternary)? Consider what would happen if there was no hydrogen bonding and just van der Waals in this protein structure. What would you anticipate to happen to its properties? Briefly explain with examples.Draw the chemical structure of an alanine pentapeptide. Indicate the location of each peptide bond. Label the phi () and psi () dihedral angles. Name and briefly define the four levels of protein structure.
- At what level of protein structure (primary, secondary, tertiary or quarternary) does Hydrogen bonding is relevant ? Consider if there is no Hydrogen bonding that exists, and only van der Waals exists in this protein structure, what do you expect to happen in its property? Explain with examples.One technique that is used when attempting to solve the crystal structure of a large protein is not to solve the structure of the whole protein itself. Instead, the protein is broken down into smaller components and the structure of the smaller components is what is solved. Of course, when performing this technique, it must be ensured that the process of breaking down the protein into smaller components does not drastically change the structure of the smaller components. With this in mind, where would be the best locations to cut a protein? At the beginning and end of secondary structures. At beginning and end of protein domains. O At the beginning and end of motifs. At the beginning and end of protein subunits.How do the following interactions help to stabilize the tertiary and quaternary structure of a protein? Give an example of a pair of amino acids that could give rise to each interaction.(a) Side-chain hydrogen bonding(b) Disulfide bonds
- All proteins have primary (1°), secondary (2°) and tertiary (3°) structure. In addition, some (but not all) proteins exhibit quaternary (4°) structure. Explain quaternary structure and why only some proteins exhibit that level of structure.In the illustration below, the blue squiggly line represents a protein. Notice that the amino acid that is colored red and the amino acid that is colored black are very close to each other in space, but they are far from each other in the primary structure of this protein. How can you explain why two amino acids that are so far from each other in the primary structure of a protein can be so close together in the tertiary structure of the same protein?Draw the protein folding pattern when the polypeptide is immersed in water and in oil. Justify your answers by using chemical explanations. In the structure, point all possible types of intramolecular forces of attraction possible for this polypeptide in the indicated solvent system and discuss each. Discuss your answer H3N*-ala-ile-trp-arg-gly-ala-his-tyr-trp-gly-gly-tyr-arg-ile-val-thr-ile-trp-cys- met-gly-ile-asp-cys-thr-glu-cys-trp-gly-cys-phe-arg-his-pro-val-phe-CO-
- You are supplied with an unknown protein that consists of more than 130 amino acids. Furthermore this protein consists of just 1 polypeptide chain. Explain (in detail) how you would determine the primary structure of this proteinCarbon’s versatile bonding behavior allows it to form a variety of structures and are the base of all macromolecules. The diagram shows the structure of an amino acid, which is the monomer unit for proteins. Identify and describe the polymer structures of a protein that constitutes its unique conformation.say you have been asked to determine the molecular structure of a soluble protein with roughly 500 amino acids per subunit. you think there may be a lysine and aspartic acid interaction so but you want to get molecular conformation. what structural technique would you utilize in order to picture this interaction and what resolution would be needed?