A limiting speed for protein folding at low solvent viscosity.
Because protein folding dynamics are heavily overdamped, Kramers theory predicts the rate of folding to scale inversely with the reaction friction, which is usually interpreted to mean the solvent viscosity. This does not mean, however, that the speed of folding can increase without limit as solvent viscosity decreases. We show that, in a sufficiently fast-folding protein, the folding speed approaches a finite limit at low solvent viscosity, indicating a reaction controlled by internal friction.
Qiu
Linlin
L
Physics Department, University of Florida, P.O. Box 118440, Gainesville Florida 32611-8440, USA. sjhagen@ufl.edu
Hagen
Stephen J
SJ
D005947:Glucose / Q000737:chemistry; D007700:Kinetics; D010455:Peptides / Q000737:chemistry*; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000737:chemistry*; D012997:Solvents / Q000737:chemistry; D013816:Thermodynamics; D014783:Viscosity
D010455:Peptides; D011994:Recombinant Proteins; D012997:Solvents; C476389:TC5b protein, synthetic; D005947:Glucose