期刊
FEBS LETTERS
卷 574, 期 1-3, 页码 156-160出版社
WILEY
DOI: 10.1016/j.febslet.2004.08.022
关键词
EGF repeat; solid phase peptide synthesis; oxidative folding; disulfide topology; NOTCH signaling
Human Jagged-1 is predicted to contain 16 epidermal growth factor-like (EGF) repeats. The oxidative folding of EGF-2, despite the several conditions tested, systematically led to complex mixtures. A longer peptide spanning the C-terminal part of EGF-1 and the complete EGF-2 repeat, on the contrary, could be readily refolded. This peptide, which corresponds to the entire exon 6 of the Jagged-1 gene, thus represents an autonomously folding unit. We show that it is structured in solution, as suggested by circular dichroism and NMR spectroscopy, and displays an EGF-like disulfide bond topology, as determined by disulfide mapping. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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