Here is a paper that discusses membrane protein physics. It is not something that is easily digestible for anyone without specialized knowledge. I use it to hopefully elucidate some things.
I'm not just talking out of my ass
I'm not trying to talk over anyone, on the contrary I am trying to make it more digestible to the average reader
there are a few details I can point out that will support the claims I am making from this literature.
Point 1) The membrane holds a membrane protein very tightly
After release into the membrane’s bilayer fabric, a MP resides stably in a thermodynamic free
energy minimum (evidence reviewed in Refs. 2 and 3).
A thermodynamic free energy minimum means that it can't escape. It is in a valley. It can't by itself climb the hills out. In the case of these TM proteins that valley is very deep when in an aqueous environment (our bodies).
Point 2) The membrane determines the structure of the protein
This means
that the prediction of MP structure from the amino acid sequence is
fundamentally a problem of physical chemistry
Structure is determined by the membrane. Ergo, without the membrane the structure changes. In the case of a TM protein this structural change will be dramatic as it tries to minimize exposure to the aqueous environment outside of the membrane.
Point 3) The structure of the protein must be in a very specific configuration in order to interact with the ACE-2 protein (the target of the S protein on another cell).
This study sheds light on the mechanisms underlying conformational stability and functional motions of the S-protein, which are relevant for vaccine and antiviral drug developments.
It is difficult to find a paper that says why the conformation of the SARS S protein must be so specific in a way that is easily digestible. I hope the above quote will at least suggest that this is an important consideration, even though it provides way too little detail into how essential it really is.
As analogy: If I had a car, and I took it all apart and put it all back together in a completely different configuration, the car probably wouldn't be much good for transportation.
When a TM protein is in an aqueous environment (after miraculously escaping a membrane) it must change to find a new valley of thermodynamic minimum. That means all the hydrophobic parts that were perfectly happy to be on the outside in the membrane must now find a way to hide themselves from the water they find themselves in. So all the parts of the molecule that can hide the hydrophobic parts, will hide them. And they will also hide themselves, going from the outside to the inside.
It becomes a completely different thing. It almost certainly no longer has the capacity to interact with ACE-2, or likely do anything at all except be degraded.
Here is a paper that discusses membrane protein physics. It is not something that is easily digestible for anyone without specialized knowledge. I use it to hopefully elucidate some things.
Point 1) The membrane holds a membrane protein very tightly
A thermodynamic free energy minimum means that it can't escape. It is in a valley. It can't by itself climb the hills out. In the case of these TM proteins that valley is very deep when in an aqueous environment (our bodies).
Point 2) The membrane determines the structure of the protein
Structure is determined by the membrane. Ergo, without the membrane the structure changes. In the case of a TM protein this structural change will be dramatic as it tries to minimize exposure to the aqueous environment outside of the membrane.
From a different paper:
Point 3) The structure of the protein must be in a very specific configuration in order to interact with the ACE-2 protein (the target of the S protein on another cell).
It is difficult to find a paper that says why the conformation of the SARS S protein must be so specific in a way that is easily digestible. I hope the above quote will at least suggest that this is an important consideration, even though it provides way too little detail into how essential it really is.
As analogy: If I had a car, and I took it all apart and put it all back together in a completely different configuration, the car probably wouldn't be much good for transportation.
When a TM protein is in an aqueous environment (after miraculously escaping a membrane) it must change to find a new valley of thermodynamic minimum. That means all the hydrophobic parts that were perfectly happy to be on the outside in the membrane must now find a way to hide themselves from the water they find themselves in. So all the parts of the molecule that can hide the hydrophobic parts, will hide them. And they will also hide themselves, going from the outside to the inside.
It becomes a completely different thing. It almost certainly no longer has the capacity to interact with ACE-2, or likely do anything at all except be degraded.
I hope that helps.
Ok. We are on the right track. Now send that to Dr Warren and the experts who disagree and come to a consensus.
You mean I should send it to the very likely Cabal guy? Really?
I'd rather be wrong and alive than right and dead.
Thanks.