The key is to have a directed way to get the bee venom to the cancer cells.

the 3 dimentional structure of a protein is key to its function, so to understand what a particular protein does or how disease occurs, we want to look at it. We have multiple different methods to do this, and each has their advantages. Our main goal when looking at a protein is to see it in its original form, as would be found in the cell, otherwise known as the native structure. The issue with some techniques, such as x ray crystallography, is that the conditions required to cause a protein to crystalize lie outside the normal function range the protein works in, so the shape we see is more of an approximation. 3D NMR is a technique that is capable of seeing a molecule based on how atom react to an external magnetic field. With 3D NMR we are looking at this reactivity using 3 atoms: hydrogen, carbon, and nitrogen. From the gathered data, we can form a 3d computer model that is more closly resembling the native structure. The additional advantage of 3D NMR is that we can see the areas of the protein that are static and other parts that are more dynamic. Cryo EM or cyrogenic electron microscopy requires us to freeze the proteins on a platoform, and then send a beam of electrons to see the proteins. The resulting image is a blurred representation of the protein, but acts as a quick and easy starting point for research. When combined together, we get a good idea of what the structure looks like.

Xray crystallography produces the most detailed images we can get, up to the resolution of 1 angstrom, which lets us see hydrogen bonding, but getting the protein and having it synthesized in a manner that allows it to be imaged is just one of the few headaches researchers have to go through before they can get an image. When I was a researcher the lab next to us worked with cryo EM. It was cool.

im a biochemist, so yes i know what a protein is. Im trying to explain the importance of maintaining the 3d structure of a protein to its function. Both proteins have the same sequence, but there is a slight difference in what the software rendered. Now, based on the sequence, a cell would reliably recreate the same protein. However, in the context of having 2 slightly different structures from the same amino acid strand, yes, you can have widely varying functions that result depending on the original purpose of the peptide strand.

It can. A single point mutation of one amino acid is enough to cause a deviation in normal function, as is the case of some diseases.

Protein structures have both static and dynamic sections inside of them, but computer models are not not well suited to predict them. You'd need to confirm you findings with an imaging experiment, like 3d NMR, that is capable of capturing those dynamic, shifting structures.

Just combine this with a 3D NMR and cryo EM model and you're good to go.

For research purposes, this is perfect. It's the best approximation to the native protein structure we can get. Before this, we had xray crystallography, but the problem with that was it cause the protein to change shape.

Very. Proteins must maintain their shape as much as possible if they are function. When a protein interacts with another compound or structure, the positioning of the amino acid side chains is crucial. The side chain positioning acts lkle a key in a lock, and exert their influence based on their angle, distance, and positioning relative to what they interact with.

I thought this was already well known? I don't understand what's new about it?