Remarkably slow folding of a small protein.
Equilibrium denaturation of the 72 amino acid alpha/beta-protein MerP, by acid, guanidine hydrochloride, or temperature, is fully reversible and follows a two-state model in which only the native and unfolded states are populated. A cis-trans equilibrium around a proline peptide bond causes a heterogeneity of the unfolded state and gives rise to a slow- and a fast folding population. With a rate constant of 1.2 s(-1) for the major fast folding population, which has none of the common intrinsically slow steps, MerP is the slowest folding protein of this small size yet reported.
Aronsson
G
G
Department of Biochemistry, Umeå University, Sweden. aron@chem.umu.se
Brorsson
A C
AC
Sahlman
L
L
Jonsson
B H
BH
D001426:Bacterial Proteins / Q000737:chemistry*; D002352:Carrier Proteins / Q000737:chemistry*; D002942:Circular Dichroism; D019791:Guanidine; D006146:Guanidines; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008958:Models, Molecular; D011392:Proline / Q000737:chemistry; D011489:Protein Denaturation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011506:Proteins; D013050:Spectrometry, Fluorescence; D013696:Temperature
D001426:Bacterial Proteins; D002352:Carrier Proteins; D006146:Guanidines; C086060:MerP protein, Bacteria; D011506:Proteins; D011392:Proline; D019791:Guanidine