Two new structured intermediates in the oxidative folding of RNase A

E. Welker, Mahesh Narayan, Michael J. Volles, Harold A. Scheraga

Research output: Contribution to journalArticle

42 Citations (Scopus)

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°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.

Original languageEnglish
Pages (from-to)477-479
Number of pages3
JournalFEBS Letters
Volume460
Issue number3
DOIs
Publication statusPublished - Nov 5 1999

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Pancreatic Ribonuclease
Disulfides
Temperature

Keywords

  • Disulfide bond
  • Dithiothreitol
  • Folding
  • Intermediate
  • Oxidative refolding
  • Ribonuclease A

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Two new structured intermediates in the oxidative folding of RNase A. / Welker, E.; Narayan, Mahesh; Volles, Michael J.; Scheraga, Harold A.

In: FEBS Letters, Vol. 460, No. 3, 05.11.1999, p. 477-479.

Research output: Contribution to journalArticle

Welker, E. ; Narayan, Mahesh ; Volles, Michael J. ; Scheraga, Harold A. / Two new structured intermediates in the oxidative folding of RNase A. In: FEBS Letters. 1999 ; Vol. 460, No. 3. pp. 477-479.
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