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Figure 5.
Fig. 5. Folding kinetics of EETI-II wild type, EETI-  ^NEDE, and
EETI- ^TNNK. A-C,
HPLC analysis of the acid trapped folding intermediates of
EETI-II wild type (A), EETI- ^NEDE (B),
and EETI- ^TNNK (C).
Proteins were allowed to refold from the fully reduced form in
the presence of 100 mM NH[4]HCO[3] pH 9.1. Acid-trapped
intermediates, taken at the indicated time points were analyzed
by reversed-phase HPLC. R indicates the reduced form of the
respective variant, I the predominant folding intermediate, and
N the native form. D-F, concentration of fully reduced peptide (
 ),
dihydro-2,19-EETI-II folding intermediate (  circle ),
and native peptide (  ),
expressed as percentage of total peptide, after various times of
incubation of reduced peptide. The relative concentrations were
determined from the HPLC peak areas.
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