Sandbox Reserved 197: Difference between revisions

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The <scene name='Sandbox_Reserved_197/Tyr92-pro93/5'>Tyr92-Pro93</scene> peptide group of RNase A in its native state is found in the ''cis'' conformation. Despite a mutation from proline to alanine, <scene name='Sandbox_Reserved_197/P93a/7'>P93A</scene>, a ''cis'' conformation still forms; this is an unfavorable conformation for an alanine residue. Upon unfolding, Tyr92-Ala93 undergoes isomerization to form its more favorable ''trans'' conformation demonstrating that the ''cis'' conformation is favored by protein interactions other than the proline residue. Although the overall structure of RNase A is not affected by this mutation, the rate of folding greatly decreases upon insertion of the P93A mutation.

<scene name='Sandbox_Reserved_197/Cis-proline114/1'>''cis'' proline</scene>

<scene name='Sandbox_Reserved_197/Cis-proline114/1'>''cis'' proline</scene> resides in a ''cis'' conformation in its folded structure, but exists in the ''trans'' conformation in its unfolded state; therefore, steric restraints imposed by the rest of the protein must be responsible for this ''cis'' conformation. Insertion of <scene name='Sandbox_Reserved_197/P114g/1'>P114G</scene> causes the chain to adopt a ''trans'' conformation and causes a 9.3A movement of the loop where it is located. The kinetic rate and overall native conformation are not significantly effected by this mutation; however, locally, a rearrangement of the hydrogen-bonding network occurs. Results of this mutation confirm that steric hinderance of the protein causes formation of the ''cis'' conformation by a proline and is further energetically stabilized by hydrogen bonding, Van der Waals, and electrostatic interactions within the protein.

Sandbox Reserved 197: Difference between revisions

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@@ Line 16: / Line 16: @@
 The <scene name='Sandbox_Reserved_197/Tyr92-pro93/5'>Tyr92-Pro93</scene> peptide group of RNase A in its native state is found in the ''cis'' conformation. Despite a mutation from proline to alanine, <scene name='Sandbox_Reserved_197/P93a/7'>P93A</scene>, a ''cis'' conformation still forms; this is an unfavorable conformation for an alanine residue.   Upon unfolding, Tyr92-Ala93 undergoes isomerization to form its more favorable ''trans'' conformation demonstrating that the ''cis'' conformation is favored by protein interactions other than the proline residue. Although the overall structure of RNase A is not affected by this mutation, the rate of folding greatly decreases upon insertion of the P93A mutation.
-<scene name='Sandbox_Reserved_197/Cis-proline114/1'>''cis'' proline</scene>
+<scene name='Sandbox_Reserved_197/Cis-proline114/1'>''cis'' proline</scene> resides in a ''cis'' conformation in its folded structure, but exists in the ''trans'' conformation in its unfolded state; therefore, steric restraints imposed by the rest of the protein must be responsible for this ''cis'' conformation. Insertion of <scene name='Sandbox_Reserved_197/P114g/1'>P114G</scene> causes the chain to adopt a ''trans'' conformation and causes a 9.3A movement of the loop where it is located. The kinetic rate and overall native conformation are not significantly effected by this mutation; however, locally, a rearrangement of the hydrogen-bonding network occurs. Results of this mutation confirm that steric hinderance of the protein causes formation of the ''cis'' conformation by a proline and is further energetically stabilized by hydrogen bonding, Van der Waals, and electrostatic interactions within the protein.
-<scene name='Sandbox_Reserved_197/P114g/1'>P114G</scene>
 <Structure load='7RSA' size='500' frame='true' align='left' caption='Insert caption here' scene='Sandbox_Reserved_197/Rnase_a_wild_type/4' />