Question 4 Prions(pronounced pree-ahns) are agents that cause a novel type of fatal brain disease. Bovine spongiform encephalopathy(BSE or mad cow disease), sheep scrapie and Creutzfeldt-Jakob disease(CJD)of humans are examples of prion diseases. Prions enter cells and convert normal proteins found within the cells into prions just like themselves. The normal cell proteins have all the same"parts"as the prions--specifically the same amino acid building blocks--but they fold differentI bonds,hydrogen bonds, or van der Waals forces)are involved in primary structure? onic a)What is the primary structure of a protein? What force or forces(covalent bonds, ic The primary structure of a protein is the linear sequence of the amino acids. Covalent bonds link the individual amino acids bonds,hydrogen bonds, or van der waals forces)are involved in secondary structure?C b)What is the secondary structure of a protein? What force or forces (covalent bonds, io The secondary structure of a protein is the region or regions within a protein that form a-helices or p- sheets. Hydrogen bonds dictate secondary structure c)What is the tertiary structure of a protein? What force or forces(covalent bonds, ionic bonds hydrogen bonds, or van der waals forces)are involved in tertiary structure? The tertiary structure of a protein is the three dimensional shape that a protein takes. All the forces discussed in class work together to stabilize the tertiary structure of a protein d)Do you expect both the normal and the infectious versions of a prion protein to have the same primary structure? Why or why not If the normal cell proteins have all the saine amino acid building block, then the normal and the infectious versions of a prion protein to have the same primary structure. e)Do you expect both the normal and the infectious versions of a prion protein to have the same tertiary structure Why or why not If the infectious version of a prion protein folds differently, then the normal and the infections versions of a prion protein have different tertiary structure 7012Fall20037.012 Fall 2003 4 Question 4 Prions (pronounced pree-ahns) are agents that cause a novel type of fatal brain disease. Bovine spongiform encephalopathy (BSE or mad cow disease), sheep scrapie and Creutzfeldt-Jakob disease (CJD) of humans are examples of prion diseases. Prions enter cells and convert normal proteins found within the cells into prions just like themselves. The normal cell proteins have all the same "parts" as the prions--specifically the same amino acid building blocks--but they fold differently. a) What is the primary structure of a protein? What force or forces (covalent bonds, ionic bonds, hydrogen bonds, or van der Waals forces) are involved in primary structure? The primary structure of a protein is the linear sequence of the amino acids. Covalent bonds link the individual amino acids b) What is the secondary structure of a protein? What force or forces (covalent bonds, ionic bonds, hydrogen bonds, or van der waals forces) are involved in secondary structure? The secondary structure of a protein is the region or regions within a protein that form α-helices or β- sheets. Hydrogen bonds dictate secondary structure. c) What is the tertiary structure of a protein? What force or forces (covalent bonds, ionic bonds, hydrogen bonds, or van der waals forces) are involved in tertiary structure? The tertiary structure of a protein is the three dimensional shape that a protein takes. All the forces discussed in class work together to stabilize the tertiary structure of a protein. d) Do you expect both the normal and the infectious versions of a prion protein to have the same primary structure? Why or why not. If the normal cell proteins have all the same amino acid building block, then the normal and the infectious versions of a prion protein to have the same primary structure. e) Do you expect both the normal and the infectious versions of a prion protein to have the same tertiary structure? Why or why not. If the infectious version of a prion protein folds differently, then the normal and the infectious versions of a prion protein have different tertiary structure