The ribbons and helices you see in those pictures are abstract representations of the underlying positions of specific arrangements of carbon atoms along the backbone.
There are tools such as DSSP https://en.wikipedia.org/wiki/DSSP_(hydrogen_bond_estimation... which will take out the 3d structure determined by crystallography and spit out hte ribbons and helices- for example, for helices, you can see a specific arrangement of carbons along the protein's backbone in 3d space (each carbon interacts with a carbon 4 amino acids down the chain).
Protein motion at room temperature varies depending on the protein- some proteins are rocks that stay pretty much in the same single conformation forever once they fold, while others do thrash around wildly and others undergo complex, whole-structure rearrangements that almost seem magical if you try to think about them using normal physics/mechanical rules.
Having a magical machine that could output the full manifold of a protein during the folding process at subatomic resolution would be really nice! but there would be a lot of data to process.
There are tools such as DSSP https://en.wikipedia.org/wiki/DSSP_(hydrogen_bond_estimation... which will take out the 3d structure determined by crystallography and spit out hte ribbons and helices- for example, for helices, you can see a specific arrangement of carbons along the protein's backbone in 3d space (each carbon interacts with a carbon 4 amino acids down the chain).
Protein motion at room temperature varies depending on the protein- some proteins are rocks that stay pretty much in the same single conformation forever once they fold, while others do thrash around wildly and others undergo complex, whole-structure rearrangements that almost seem magical if you try to think about them using normal physics/mechanical rules.
Having a magical machine that could output the full manifold of a protein during the folding process at subatomic resolution would be really nice! but there would be a lot of data to process.