Figure 7 shows one additional type of bond that can stabilize the tertiary structure of aprotein. This bond is called a disulfide bond (or disulfide bridge), and it involves thesulfhydryl (-SH) R groups from one particular type of amino acid. A disulfide bond canform only under certain conditions (oxidative conditions). We'll talk about oxidation andreduction next week. For now, just note that this type of bond does exist in someproteins.Answer the below questions on tertiary structure in your own document.8. Figure 6 shows examples of bonds that might stabilize the tertiary structure of aprotein (labeled A, B, and C). Do these interactions involve only the amino acid Rgroups, only the polypeptide backbone atoms, or both?9. In the table below, indicate what type of bond/ interaction is represented inthe examples shown in Figure 6, panels A, B, and C and whether eachinteraction involves group or backbone atoms.ExampleType of Bonding InteractionR group or backbone?AВ10. For each of the three interactions shown in Figure 6, indicate how changes inthe following conditions might affect those interactions: pH, temperature, saltconcentration. Explain your answer.11. Which amino acid can form disulfide bonds? To help you answer, refer to aminoacid chart and Figure 7.12. What is different about the disulfide bond compared to the other types of bondsthat stabilize tertiary structure? Based on your existing knowledge of bonding, isthis bond weaker or stronger than the other types of bonds that stabilize tertiarystructure?13. Make a prediction of which tertiary interactions you might be more likely to find inthe proteins of prokaryotic species that live in the extreme environment of hotsprings compared to similar species that live in more moderate environments.Explain your answer. QUATERNARY STRUCTUREOne final level of structure exists for some, but not all, proteins. This is calledquaternary structure. Proteins that have quaternary structure are formed from two ormore polypeptides that assemble into one active structure. The different polypeptides ina protein with quaternary structure are often called subunits. These subunits may beidentical or different. One example of a protein with quaternary structure is hemoglobin,the protein that transports oxygen in our blood. The structure of hemoglobin is shown inFigure 8.B-Fe2+- HemeaFigure 8. Quaternary structure of hemoglobin with labeled subunits. Note: eachsubunit contains one non-protein heme group complexed to an oxidized iron atom(Fe2+). These “prosthetic groups" are required for carrying oxygen in the blood.Modified from this link under Creative Commons license.Answer the below questions on quaternary structure in your own document.1. Based on your interpretation of Figure 9, how many subunits does hemoglobincontain? Are they all the same or different?2. Which types of interactions do you think stabilize the quaternary structure ofproteins that have this level of structure? (Hint: this is not any different from theinteractions you identified in tertiary structure, except for the fact that multiplepolypeptides are involved).

Question

Figure 7 shows one additional type of bond that can stabilize the tertiary structure of aprotein. This bond is called a disulfide bond (or disulfide bridge), and it involves thesulfhydryl (-SH) R groups from one particular type of amino acid. A disulfide bond canform only under certain conditions (oxidative conditions). We'll talk about oxidation andreduction next week. For now, just note that this type of bond does exist in someproteins.Answer the below questions on tertiary structure in your own document.8. Figure 6 shows examples of bonds that might stabilize the tertiary structure of aprotein (labeled A, B, and C). Do these interactions involve only the amino acid Rgroups, only the polypeptide backbone atoms, or both?9. In the table below, indicate what type of bond/ interaction is represented inthe examples shown in Figure 6, panels A, B, and C and whether eachinteraction involves group or backbone atoms.ExampleType of Bonding InteractionR group or backbone?AВ10. For each of the three interactions shown in Figure 6, indicate how changes inthe following conditions might affect those interactions: pH, temperature, saltconcentration. Explain your answer.11. Which amino acid can form disulfide bonds? To help you answer, refer to aminoacid chart and Figure 7.12. What is different about the disulfide bond compared to the other types of bondsthat stabilize tertiary structure? Based on your existing knowledge of bonding, isthis bond weaker or stronger than the other types of bonds that stabilize tertiarystructure?13. Make a prediction of which tertiary interactions you might be more likely to find inthe proteins of prokaryotic species that live in the extreme environment of hotsprings compared to similar species that live in more moderate environments.Explain your answer. QUATERNARY STRUCTUREOne final level of structure exists for some, but not all, proteins. This is calledquaternary structure. Proteins that have quaternary structure are formed from two ormore polypeptides that assemble into one active structure. The different polypeptides ina protein with quaternary structure are often called subunits. These subunits may beidentical or different. One example of a protein with quaternary structure is hemoglobin,the protein that transports oxygen in our blood. The structure of hemoglobin is shown inFigure 8.B-Fe2+- HemeaFigure 8. Quaternary structure of hemoglobin with labeled subunits. Note: eachsubunit contains one non-protein heme group complexed to an oxidized iron atom(Fe2+). These “prosthetic groups&#34; are required for carrying oxygen in the blood.Modified from this link under Creative Commons license.Answer the below questions on quaternary structure in your own document.1. Based on your interpretation of Figure 9, how many subunits does hemoglobincontain? Are they all the same or different?2. Which types of interactions do you think stabilize the quaternary structure ofproteins that have this level of structure? (Hint: this is not any different from theinteractions you identified in tertiary structure, except for the fact that multiplepolypeptides are involved).

Accepted Answer

Note: In the first image, the questions are based on figure 6 & 7. But the figures 6 & 7 are…