In regards to the protein structure, explain what is meant by “tertiary structure.” What are the main forces that stabilize tertiary structures in proteins? Provide examples.
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In regards to the protein structure, explain what is meant by “tertiary structure.” What
are the main forces that stabilize tertiary structures in proteins? Provide examples.
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- 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.Describe the forces that are involved in the tertiary structure of a protein and give an example of each force listed.is Tertiary protein structure come from secondary structure？How are they related？（do we need to build up a secondary structure before make it become tertiary？）
- 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.Glycine provides structural flexibility in proteins. What is the consequence of this on protein structure?Discuss and identify the four levels of protein structure (primary, secondary, tertiary,and quaternary). Explain how the structure of a protein affects its properties and howdenaturation changes the structure.
- Identify the following statements as descriptive of the secondary, tertiary, or quaternary structure of a protein. What types of interactions stabilize each type of structure?(a) The polypeptide chain has a number of bends and twists, resulting in a compact structure.(b) The polypeptide backbone forms a right-handed coil.(c) The four polypeptide chains are arranged in a spherical shape.b) It's said that secondary structures form because of intra- and intermolecular hydrogen bonding involving the peptide bond. Describe what is going on to further stabilize secondary structure through these interactions.List the attractive interactions involved in secondary, tertiary, and quaternary protein structure.
- Which kinds of interactions can be seen in the tertiary structure of proteins?Structures of proteins comprising domains separated by flexible linker regions can be quite difficult to solve by x-ray crystallographic methods. Why might this be the case? What are possible experimental approaches to circumvent this barrier?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.