Structures of proteins in unfolded states have important implications
for the protein folding problem and for the translocation of polypepti
de chains. Acid-denatured, cold-denatured, and 6 M guanidine hydrochlo
ride (GuHCl) denatured yeast phosphoglycerate kinase (PGK) are ensembl
es of flexible unfolded molecules with rapidly interconverting structu
res of the individual polypeptide chains. They differ, however, in the
ir physical properties, such as in coil size and in stiffness over a s
hort distance along the chain. These properties of polypeptide chains
can be described well by persistence statistics. A solution containing
0.7 M GuHCl at 4.5 degrees C is nearly a theta-solvent for PGK. By co
ntrast, 6 M GuHCl is a good solvent for PGK. Acid-denatured PGK at low
ionic strength has the most expanded and stiffest chains. The conform
ation of heat-denatured PGK should be more compact than that of random
walk chains at the theta-point, as can be inferred from measurements
on other proteins. Investigations of heat-denatured PGK by scattering
methods are unfeasible due to aggregation of the protein. The persiste
nce length as a measure of chain stiffness varies between a 1.74 nm fo
r cold-denatured PGK and a = 3.0 nm for acid-denatured PGK. The distri
bution functions of the gyration radii were calculated from the X-ray
scattering data for all unfolded states and compared with the radius o
f gyration of the natively folded molecule.