Sandbox Reserved 200: Difference between revisions

Ribonuclease A has both a <scene name='Sandbox_Reserved_200/Major_dimer/11'>major</scene> and <scene name='Sandbox_Reserved_200/Minor_dimer/2'>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 its α-helix of 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>.

The two domains of the dimer are linked via the hinge loop.<ref name="liul"/>. In the major dimer, the hinge loop is composed of residues 112-115. In the minor dimer, the hinge loop is composed of residues 16-22.<ref name="liul"/>  The most important component of the hinge loops is Ala19.  <scene name='Sandbox_Reserved_200/Minor_dimer_hinge/1'>Ala19</scene> is the reason that the hinge loops are so flexible . This flexibility allows the dimers to adopt different orientations, for example the major and minor structures.<ref name="liu98"/>