RNase A Oligomers: Difference between revisions

==Dimers==

Ribonuclease A has both a <scene name='Sandbox_Reserved_200/Major_dimer/11'>major</scene> and <scene name='Sandbox_Reserved_200/Minor_dimer/4'>minor</scene> dimer which are very similar to one another. Though they are similar, they are formed by different types of 3D domain swapping.  3D domain swapping occurs when identical domains are interchanged.  The major dimer is formed by 3D domain swapping the β-strand of the C-terminus.<ref name="liu98"/> The minor dimer, on the other hand, is formed by 3D domain swapping of the α-helix on the N-terminus <ref name="liu98"/>.  Domain swapping is extremely specific and can only occur at the <scene name='Sandbox_Reserved_200/Major_dimer/10'>C-terminus</scene> or the <scene name='Sandbox_Reserved_200/Major_dimer/9'>N-terminus</scene>.

==Trimers==

RNase A trimers are formed in the same way as the dimers, except there are now three monomeric subunits.  There is both a major and minor trimer.  The structure of the major trimer is not known, but the two trimers can be separated by both chromatography and gel electrophoresis. <ref name="liu01"/>  The major trimer is more common than the minor trimer.

The <scene name='Sandbox_Reserved_200/Minor_trimer/12'>minor trimer</scene> forms a cyclic propeller like shape.  It is 3D domain swapped at the C-terminus of the beta strand.<ref name="liu01"/>  No domain swapping a the N-terminus has been seen.  When the minor trimer dissociates, it forms a dimer and a monomer.  The minor and major dimer are both formed, but the major dimer is much more common.<ref name="liu01"/>     

* [http://www.proteopedia.org/wiki/index.php/RNaseS_RNaseB RNase S and RNase B]

* [http://www.proteopedia.org/wiki/index.php/RNaseA_Nobel_Prizes RNase A Nobel Prizes]

==References==