Exon 6 of human Jagged‐1 encodes an autonomously folding unit
Copyright policy )Exon 6 of human Jagged‐1 encodes an autonomously folding unit
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.
Protein Folding, Magnetic Resonance Spectroscopy, Sequence Homology, Amino Acid, Circular Dichroism, Calcium-Binding Proteins, Molecular Sequence Data, EGF repeat, Membrane Proteins, Oxidative folding, Exons, Solid phase peptide synthesis, Disulfide topology, Humans, Intercellular Signaling Peptides and Proteins, Serrate-Jagged Proteins, Spectrophotometry, Ultraviolet, Amino Acid Sequence, NOTCH signaling, Jagged-1 Protein
Protein Folding, Magnetic Resonance Spectroscopy, Sequence Homology, Amino Acid, Circular Dichroism, Calcium-Binding Proteins, Molecular Sequence Data, EGF repeat, Membrane Proteins, Oxidative folding, Exons, Solid phase peptide synthesis, Disulfide topology, Humans, Intercellular Signaling Peptides and Proteins, Serrate-Jagged Proteins, Spectrophotometry, Ultraviolet, Amino Acid Sequence, NOTCH signaling, Jagged-1 Protein
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