Sandbox Reserved 197: Difference between revisions

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==='''Disulfide Bonds'''===

Another important feature of the folding of RNase A is the presence of four disulfide bonds. These bonds contribute to the thermal stability and the rate of folding of RNase A. The residues involved in these linkages include <scene name='Sandbox_Reserved_197/Cys26-cys84/2'>Cys26-Cys84</scene>, <scene name='Sandbox_Reserved_197/Cys58-cys110/2'>Cys58-Cys110</scene>, <scene name='Sandbox_Reserved_197/40-95_disulfide_native_form/4'>Cys40-Cys95</scene>, and <scene name='Sandbox_Reserved_197/Cys65-cys72/3'>Cys65-Cys72</scene>. Cys26-Cys84 and Cys58-Cys110 create an interaction between an ~~alpha~~-helix and a ~~beta~~ sheet. This connection is the main contributor to the thermodynamic stability. RNase A actually has a rate-determining three-disulfide intermediate. An analog of this, <scene name='Sandbox_Reserved_197/C40-95a_variant/4'>C[40,95]A</scene>, shows RNase A, missing the disulfide bond that would normally occur here, Cys40-Cys95. As you can see in the variant, there are only 3 disulfide bonds present, shown in red.

Another important feature of the folding of RNase A is the presence of four disulfide bonds. These bonds contribute to the thermal stability and the rate of folding of RNase A. The residues involved in these linkages include <scene name='Sandbox_Reserved_197/Cys26-cys84/2'>Cys26-Cys84</scene>, <scene name='Sandbox_Reserved_197/Cys58-cys110/2'>Cys58-Cys110</scene>, <scene name='Sandbox_Reserved_197/40-95_disulfide_native_form/4'>Cys40-Cys95</scene>, and <scene name='Sandbox_Reserved_197/Cys65-cys72/3'>Cys65-Cys72</scene>. Cys26-Cys84 and Cys58-Cys110 create an interaction between an α-helix and a β-sheet. This connection is the main contributor to the thermodynamic stability. RNase A actually has a rate-determining three-disulfide intermediate. An analog of this, <scene name='Sandbox_Reserved_197/C40-95a_variant/4'>C[40,95]A</scene>, shows RNase A, missing the disulfide bond that would normally occur here, Cys40-Cys95. As you can see in the variant, there are only 3 disulfide bonds present, shown in red.

=='''References'''==

Sandbox Reserved 197: Difference between revisions

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@@ Line 17: / Line 17: @@
 ==='''Disulfide Bonds'''===
-Another important feature of the folding of RNase A is the presence of four disulfide bonds.  These bonds contribute to the thermal stability and the rate of folding of RNase A.  The residues involved in these linkages include <scene name='Sandbox_Reserved_197/Cys26-cys84/2'>Cys26-Cys84</scene>, <scene name='Sandbox_Reserved_197/Cys58-cys110/2'>Cys58-Cys110</scene>, <scene name='Sandbox_Reserved_197/40-95_disulfide_native_form/4'>Cys40-Cys95</scene>, and <scene name='Sandbox_Reserved_197/Cys65-cys72/3'>Cys65-Cys72</scene>.  Cys26-Cys84 and Cys58-Cys110 create an interaction between an alpha-helix and a beta sheet.  This connection is the main contributor to the thermodynamic stability.  RNase A actually has a rate-determining three-disulfide intermediate.  An analog of this, <scene name='Sandbox_Reserved_197/C40-95a_variant/4'>C[40,95]A</scene>, shows RNase A, missing the disulfide bond that would normally occur here, Cys40-Cys95.  As you can see in the variant, there are only 3 disulfide bonds present, shown in red.
+Another important feature of the folding of RNase A is the presence of four disulfide bonds.  These bonds contribute to the thermal stability and the rate of folding of RNase A.  The residues involved in these linkages include <scene name='Sandbox_Reserved_197/Cys26-cys84/2'>Cys26-Cys84</scene>, <scene name='Sandbox_Reserved_197/Cys58-cys110/2'>Cys58-Cys110</scene>, <scene name='Sandbox_Reserved_197/40-95_disulfide_native_form/4'>Cys40-Cys95</scene>, and <scene name='Sandbox_Reserved_197/Cys65-cys72/3'>Cys65-Cys72</scene>.  Cys26-Cys84 and Cys58-Cys110 create an interaction between an α-helix and a β-sheet.  This connection is the main contributor to the thermodynamic stability.  RNase A actually has a rate-determining three-disulfide intermediate.  An analog of this, <scene name='Sandbox_Reserved_197/C40-95a_variant/4'>C[40,95]A</scene>, shows RNase A, missing the disulfide bond that would normally occur here, Cys40-Cys95.  As you can see in the variant, there are only 3 disulfide bonds present, shown in red.
 =='''References'''==