Calculate structure: Difference between revisions

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'''Myohemerytherin''' (<scene name='Globular_Proteins/Anti_helix_erythrin2/1'>Restore initial scene</scene>)

* There are two T segments (<scene name='Calculate_structure/Turn_84/2'>T : A:86_A:86</scene> (run ''calculate hbonds structure'' in the console to show the hbonds) and <scene name='Calculate_structure/Turn_110/2'>T : A:110_A:110</scene>~~) that contain one residue~~, ~~and~~ the other three residue ~~in both of the turns~~ are involved in a helix which has priority over a turn. Both of these turns are class I β-turn.

* There are two T segments that contain one residue. The first two residues of the β-turn marked by <scene name='Calculate_structure/Turn_84/2'>T : A:86_A:86</scene> (run ''calculate hbonds structure'' in the console to show the hbonds)are part of a helix and residue 87 is not part of any other structure. A situation described below is similar but both residues that are not part of another structure are included in the T segment. The first residue (# 110) of the turn marked by <scene name='Calculate_structure/Turn_110/2'>T : A:110_A:110</scene> is not involved in another structure, but the other three residue are involved in a helix which has priority over a turn. Both of these turns are class I β-turn.

* There are two T segments that contain two residues. The first two residues of the β-turn marked by<scene name='Calculate_structure/Turn_63/3'>T : A:65_A:66</scene> are #'s 63 and 64, these two are part of a helix as well as the β-turn, and therefore only #'s 65 and 66 are part of the T segment. The middle two residues (68 and 69) of the β-turn marked by <scene name='Calculate_structure/Turn_67/6'>T : A:68_A:69</scene> are not part of a helix, but residue #70 is. Notice that part of residues 67 and 68 are colored white rather than blue. Both turns are class I.

* The ~~last T identifies a three residue segment indicating a~~ <scene name='Calculate_structure/Turn_114/2'>~~4-turn~~</scene>. ''Calculate hbonds structure'' shows hbonds between 114 and 117 (3-turn and type II β-turn) and between 114 and 118 (4-turn). A β-turn is nested in a 4-turn. Residue 114 is part of the 3<sub>10</sub>-helix, and part of residue 118 is colored white.

* The <scene name='Calculate_structure/Turn_114/2'>last T</scene> identifies a three residue segment, and ''Calculate hbonds structure'' shows hbonds between 114 and 117 (3-turn and type II β-turn) and between 114 and 118 (4-turn). A β-turn is nested in a 4-turn. Residue 114 is part of the 3<sub>10</sub>-helix, and part of residue 118 is colored white.

* Can you locate the two β-turns that are not coloredwith blue traces and not contain a hbond between the first and the last residues of the turn. Remember that you can confirm the presence of this type of β-turn by showing the presence of a Pro at position three. (Hover the cursor over the trace to display the name and number of the residues.) There are two class VIb β-turns in myohemerytherin.

* Can you locate the two turns that are not coloredwith blue traces and not contain a hbond between the first and the last residues of the turn. Remember that you can confirm the presence of this type of β-turn by showing the presence of a Pro at position three. (Hover the cursor over the trace to display the name and number of the residues.) There are two class VIb β-turns in myohemerytherin.

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 '''Myohemerytherin'''  (<scene name='Globular_Proteins/Anti_helix_erythrin2/1'>Restore initial scene</scene>)
-* There are two T segments (<scene name='Calculate_structure/Turn_84/2'>T : A:86_A:86</scene> (run ''calculate hbonds structure'' in the console to show the hbonds) and <scene name='Calculate_structure/Turn_110/2'>T : A:110_A:110</scene>) that contain one residue, and the other three residue in both of the turns are involved in a helix which has priority over a turn. Both of these turns are class I β-turn.
+* There are two T segments that contain one residue. The first two residues of the β-turn marked by <scene name='Calculate_structure/Turn_84/2'>T : A:86_A:86</scene> (run ''calculate hbonds structure'' in the console to show the hbonds)are part of a helix and residue 87 is not part of any other structure. A situation described below is similar but both residues that are not part of another structure are included in the T segment. The first residue (# 110) of the turn marked by <scene name='Calculate_structure/Turn_110/2'>T : A:110_A:110</scene> is not involved in another structure, but the other three residue are involved in a helix which has priority over a turn. Both of these turns are class I β-turn.
 * There are two T segments that contain two residues. The first two residues of the β-turn marked by<scene name='Calculate_structure/Turn_63/3'>T : A:65_A:66</scene> are #'s 63 and 64, these two are part of a helix as well as the β-turn, and therefore only #'s 65 and 66 are part of the T segment. The middle two residues (68 and 69) of the β-turn marked by <scene name='Calculate_structure/Turn_67/6'>T : A:68_A:69</scene> are not part of a helix, but residue #70 is. Notice that part of residues 67 and 68 are colored white rather than blue. Both turns are class I.
-* The last T identifies a three residue segment indicating a <scene name='Calculate_structure/Turn_114/2'>4-turn</scene>. ''Calculate hbonds structure'' shows hbonds between 114 and 117 (3-turn and type II β-turn) and between 114 and 118 (4-turn). A β-turn is nested in a 4-turn. Residue 114 is part of the 3<sub>10</sub>-helix, and part of residue 118 is colored white.
+* The <scene name='Calculate_structure/Turn_114/2'>last T</scene> identifies a three residue segment, and ''Calculate hbonds structure'' shows hbonds between 114 and 117 (3-turn and type II β-turn) and between 114 and 118 (4-turn). A β-turn is nested in a 4-turn. Residue 114 is part of the 3<sub>10</sub>-helix, and part of residue 118 is colored white.
-* Can you locate the two β-turns that are not coloredwith blue traces and not contain a hbond between the first and the last residues of the turn. Remember that you can confirm the presence of this type of β-turn by showing the presence of a Pro at position three. (Hover the cursor over the trace to display the name and number of the residues.) There are two class VIb β-turns in myohemerytherin.
+* Can you locate the two turns that are not coloredwith blue traces and not contain a hbond between the first and the last residues of the turn. Remember that you can confirm the presence of this type of β-turn by showing the presence of a Pro at position three. (Hover the cursor over the trace to display the name and number of the residues.) There are two class VIb β-turns in myohemerytherin.