Protein folding- what is the Role of chaperones and chaperonins in protein folding. The Formation of intermediate structures in the process of protein folding , explain the theory of intermediate structure. Example of Protein folding energy diagram.
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A: We are answering first question. For other question pls repost.
Q: Protein folding with PDI and Peptidyl-prolyl isomerase
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- Formation of the tertiary structure of a protein - what are the main physical forces affecting the assembly of the tertiary structure of proteins. The chemical compounds formed during the assembly of the tertiary structure of a protein.Describe how a polypeptide can fold to become a functioning protein. Be sure to address the four levels of protein (folding or organization known as hierarchy of structure). In addition, describe three different jobs proteins can perform if the protein has the correct shape.The final 3-dimensional structure of a globular protein is defined by several types of structural units. Rank the following structural units in function of their complexity, starting from the bigger and more complex and ending with the smaller and less complex structural unit: Alpha helices, domains, peptide bonds, oligomers, reverse turns
- A) List each of the five major functional classes of proteins. B) Discuss the function for each class, give an example of a protein for each class and mention how the function of the protein example fits the function of the class (40 words or less for each class with its exampleWhat life uses proteins for? (functions of proteins) Describe protein structures. Describe the alpha helix and the beta sheet structure of proteins. Which structure is the most important in the function of a protein? Describe what can affect the protein structure. Why the structure of a protein is important?How multiple domains in a single protein increases the versatility of each molecule ?
- Give at least 10 functions of protein and describe each function. Cite an example for each function if there are any.Linus Pauling’s a-helix structure (found in hemoglobin, myoglobin, actin, myosin, and keratin) is one of the most common examples of which level of protein organization? the quaternary structure the tertiary structure the secondary structure the primary structure all of the aboveAffinity and specificity of protein-protein interactions are mainly mediated by many weak chemical bonds such as: Group of answer choices van der Waals forces hydrogen bonds hydrophobic interactions all of the above
- Protein folding with PDI and Peptidyl-prolyl isomeraseProtein denaturation usually refers to the disruption of which of the following types of molecular interactions? Select all that apply. A.)Van der Waals attraction B.)Covalent bonds C.)Hydrogen bonds D.)Hydrophobic interactionsExplain the role of hydrophobic exclusion during protein folding (tertiary structure); what type of aminoacids would you find towards the center of the protein? Charged? Polar? Non-polar