Abstract:
:The effects of protein disulfide isomerase (PDI) on the four structured des species that accumulate in the rate-determining steps of ribonuclease A folding were investigated at pH 8.0 and 15 degrees C. The results indicate that PDI catalyzes the conversion of the kinetically trapped intermediates, des-[26-84] and des-[58-110], by reshuffling them into the on-pathway intermediate, des-[40-95], and the formation of native protein, by acting as both a chaperone and an oxidase on this on-pathway intermediate. These results provide the first strong evidence for the mechanism of PDI in the rate-determining steps of the oxidative folding pathways of ribonuclease A. Our approach, using PDI and blocked PDI, combined with the fast-blocking 2-aminoethyl methanethiosulfonate method, may be generally applicable to the clarification of the effect of PDI on folding intermediates.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Shin HC,Song MC,Scheraga HAdoi
10.1016/s0014-5793(02)02825-9keywords:
subject
Has Abstractpub_date
2002-06-19 00:00:00pages
77-80issue
1-3eissn
0014-5793issn
1873-3468pii
S0014579302028259journal_volume
521pub_type
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