Hi Shahid. Personally, I have never heard of detergent off or on rates.

Unless you are dealing with a monomer detergent molecule interacting with a monomer protein in non-aqueous solvent, the whole on-off detergent rates is daft.

Detergents mostly assemble in  micelles in aqueous solvents. These structures may be unilamellar or multilamellar. Their assembly is dictated  by their CMC (critical micellar concentration). Totally different from imaginary on-off detergent binding to proteins.

Hi Steingrimur,

Thanks for the reply. I am familiar with CMC and deterrent micelles but in the article bellow they say DDM and LMNG have different off rates and therefore they have different affects on GPCR conformational changes. DDM with higher off rates facilities switching between these conformational state more efficiently than LMNG. I want to know how?

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3476297/

After reading this paper now I understood this better. I think detergents binds to the protein more or less like a ligand and when micelles are formed monomer detergent species can exchange with free detergents in the solution (the one not being part of micelle). The fact that DDM has faster exchange rates may also mean that it is more flexible and therefore GPCR conformational switches are facilitated. On the other hand LMNG with very very low CMC and slow off rates is more like lipid and therefore more stabilising as reported in many papers. Thanks