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 which is very unlikely 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 other interactions within the protein. 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'>Asn113-Pro114</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 9.3Å 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/Cis-proline114/1'>Asn113-Pro114</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. This is further demonstrated with the insertion of a <scene name='Sandbox_Reserved_197/P114g/1'>P114G</scene> point mutation which causes the chain to adopt a ''trans'' conformation and causes a 9.3 Å 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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 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 which is very unlikely 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 other interactions within the protein. 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'>Asn113-Pro114</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 9.3Å 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/Cis-proline114/1'>Asn113-Pro114</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. This is further demonstrated with the insertion of a <scene name='Sandbox_Reserved_197/P114g/1'>P114G</scene> point mutation which causes the chain to adopt a ''trans'' conformation and causes a 9.3 Å 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.
 <Structure load='7RSA' size='500' frame='true' align='left' caption='Insert caption here' scene='Sandbox_Reserved_197/Rnase_a_wild_type/4' />