Diffusional barrier crossing in a two-state protein folding reaction.
There has been some debate as to whether protein folding involves diffusive chain motions and thus depends on solvent viscosity. The interpretation of folding kinetics in viscous solvents has remained difficult and controversial, in that viscogenic agents affect folding rates not only by increasing solvent viscosity but also by increasing protein stability. By carefully choosing experimental conditions, we can now eliminate the effect on stability and show that the folding dynamics of the cold shock protein CspB are viscosity dependent. Thus Kramers' theory of reaction rates rather than transition state theory should be used to describe this folding reaction.
Jacob
M
M
Laboratorium für Biochemie, Universität Bayreuth, D-95440 Bayreuth, Germany.
Geeves
M
M
Holtermann
G
G
Schmid
F X
FX
D001412:Bacillus subtilis / Q000737:chemistry; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D002352:Carrier Proteins / Q000737:chemistry* / Q000378:metabolism*; D004058:Diffusion; D019855:Ethylene Glycol; D006360:Heat-Shock Proteins; D006358:Hot Temperature; D007700:Kinetics; D008956:Models, Chemical; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D020673:Protein Renaturation; D012997:Solvents; D013816:Thermodynamics; D014783:Viscosity
D001426:Bacterial Proteins; D002352:Carrier Proteins; D006360:Heat-Shock Proteins; D012997:Solvents; C077188:cold-shock protein CspB, Bacteria; D019855:Ethylene Glycol