Two new structured intermediates in the oxidative folding of RNase A.

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 Lett

journal_title

FEBS letters

authors

Welker E,Narayan M,Volles MJ,Scheraga HA

doi

10.1016/s0014-5793(99)01391-5

keywords:

subject

Has Abstract

pub_date

1999-11-05 00:00:00

pages

477-9

issue

3

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(99)01391-5

journal_volume

460

pub_type

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