Use the table and ramachandran plot List all of the regions

Use the table and ramachandran plot. List all of the regions in lysozyme that are likely to be part of an alpha helix.

(Consider a range of +/- 15° degrees relative to the ideal alpha helix phi/psi angles listed in the table under the Ramachandran plot in the “Rama_plot” supplemental file.)

Please explain and thank you for your help!

I updated the pictures, hopefully you can now see them better.

180 90 90 180 1800 90 90 180 (deg) Figure 8-7 The Ramachandran diagram. It shows the sterically allowed and ls angles for poly-L-alanine and was calculated using the van der Waals distances in Table 8-1. Regions of \"normally allowed\" and angles are shaded in blue, whereas green-shaded regions correspond to conformations having \"outer limit\" van der Waals distances. The conformation angles, dand l, of several secondary structures are indicated below: (deg) (deg) Secondary Structure Right-handed a helix (a) 47

Solution

25th amino acid residue Leusine to 35th number residue Glutamate will make  alpha helix.

Threonine 41 and glutamate 42 can also a part of alpha helix.

Threonine 47, isoleusine 47, Arginine 61, proline 71 and glycine 71 can also make alpha helix.