Sandbox Reserved 334: Difference between revisions
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=Mechanism= | =Mechanism= | ||
==Dimer Formation== | ==Dimer Formation== | ||
Proteolysis of RNase S can activate oligomerization by destabilizing the native state<ref name = "RNase1" />. This occurs via the three dimensional domain-swapping mechanism<ref name = "RNase1" />. In this mechanism two monomers trade structural motifs called swap domains which adopt essentially identical conformations in the monomeric and oligomeric forms<ref name = "RNase1" />. RNase S oligomerizes by swapping C termini, which are not cut by subtilisin<ref name = "RNase1" />. | Proteolysis of RNase S can activate oligomerization by destabilizing the native state<ref name= "RNase1" />. This occurs via the three dimensional domain-swapping mechanism<ref name= "RNase1" />. In this mechanism two monomers trade structural motifs called swap domains which adopt essentially identical conformations in the monomeric and oligomeric forms<ref name= "RNase1" />. RNase S oligomerizes by swapping C termini, which are not cut by subtilisin<ref name= "RNase1" />. | ||
==Dissociation of RNase S Dimers== | ==Dissociation of RNase S Dimers== | ||
=references= | =references= | ||
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