chaperonin

can anybody explain me how the GroEs connects to the GroEl allowing a protein that doesn't have it's natural shape to slowly go to it's tertiary structure? ^^

I'll try to explain.

The GroES and the GroEl act like a cage for the protien to have enough time to be shape properly. The GroES and the GroEl binds together so that the protien doesn't escape. Its like the way a jar lid and a jar connects.

I hoped this helped because I know little about this stuff.

it was a joke

these are the things that I study, this is like the basics of the formation of protein forming

but you explanation was a rather good general definition..


but for the real stuff:


the inner ring of the chaperonin consists of hydrophobic groups which enables the protein to curve in it's natural way without the interference of hydrophilic groups from proteins that are close to the one thats forming

hypnobe wrote:

it was a joke

these are the things that I study, this is like the basics of the formation of protein forming

but you explanation was a rather good general definition..


but for the real stuff:


the inner ring of the chaperonin consists of hydrophobic groups which enables the protein to curve in it's natural way without the interference of hydrophilic groups from proteins that are close to the one thats forming

Oh so thats it!

Because I don't know stuff like that.

When do you learn about this stuff? It seems complicated. What is it?