Abstract:
:Two new three-disulfide intermediates have been found to be populated in the oxidative folding pathway of bovine pancreatic ribonuclease A at a low temperature (15 degrees C). These intermediates, des-[26-84] and des-[58-110], possess all but one of the four native disulfide bonds and have a stable tertiary structure, similar to the two previously observed intermediates, des-[65-72] and des-[40-95]. While the latter two des species each lack one surface-exposed disulfide bond, the newly discovered intermediates each lack one buried disulfide bond. The possible involvement of these species in the rate-determining steps during the oxidative folding of RNase A is discussed and a specific role for such species during oxidative folding is suggested.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Welker E,Narayan M,Volles MJ,Scheraga HAdoi
10.1016/s0014-5793(99)01391-5keywords:
subject
Has Abstractpub_date
1999-11-05 00:00:00pages
477-9issue
3eissn
0014-5793issn
1873-3468pii
S0014-5793(99)01391-5journal_volume
460pub_type
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