I did my PhD in the late 80’s. I studied structure-function of GPCR.
When I began, the amino acid sequences weren’t known. The nAchR was known, but it’s topography in the membrane was still debatable. When rhodopsin was sequenced, and then the b-adrenergic receptor was found to be homologous, molecular biological methods allowed the protein sequences to be known for many of them via cloning.
Now there’s the sequence of so many genomes.
As for your protein, a protein that gets cleaved up like that in storage is rare and almost nightmarish.
Anyone ever figure out why it was cut up so readily?
Anyone ever figure out why it was cut up so readily?
As I said, there is a very good biological reason the protein is unstable. Degradation is the main mechanism of down-activation of this protein once it has been activated; its function is necessary, but absolutely must be turned off once it has fulfilled its function. Its continued activity is lethal. This protein is the aryl hydrocarbon receptor, which was first identified for its role in mediating dioxin related toxicity.
As for how it degraded so rapidly despite every effort to prevent degradation--I just don't know. You would think that boiling in a beta-mercaptoethanol/SDS buffer would deactivate any protease that might be present, but no!