F helix F hellx HN- O2 HN- O2 (a) The effect of O, binding according to the Perutz model: The F helix is drawn toward the heme. F helix F helx HN- O2 HN- (b) Now lacking a covalent connection to the heme, the F helix is not disturbed by O, binding, and there is significantly reduced cooperativity. A FIGURE 7.26 The effect of replacing the proximal histidine in hemoglobin with a glycine residue and adding a noncovalently bonded imidazole.
F helix F hellx HN- O2 HN- O2 (a) The effect of O, binding according to the Perutz model: The F helix is drawn toward the heme. F helix F helx HN- O2 HN- (b) Now lacking a covalent connection to the heme, the F helix is not disturbed by O, binding, and there is significantly reduced cooperativity. A FIGURE 7.26 The effect of replacing the proximal histidine in hemoglobin with a glycine residue and adding a noncovalently bonded imidazole.
Chapter26: Biomolecules: Amino Acids, Peptides, And Proteins
Section26.SE: Something Extra
Problem 50AP: The -helical parts of myoglobin and other proteins stop whenever a proline residue is encountered in...
Related questions
Question
In the experiments of Barrick et al. (as shown), it was observed that
replacement of histidine by a noncovalently bonded imidazole not only
reduced cooperativity but also increased the oxygen affinity of the hemoglobin. Suggest an explanation.
Expert Solution
This question has been solved!
Explore an expertly crafted, step-by-step solution for a thorough understanding of key concepts.
This is a popular solution!
Trending now
This is a popular solution!
Step by step
Solved in 2 steps
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, chemistry and related others by exploring similar questions and additional content below.Recommended textbooks for you