The mature part of proNGF induces the structure of its pro-peptide

• Published in: FEBS letters Vol. 566; no. 1; pp. 207 - 212
• Main Authors: Kliemannel, Marco, Rattenholl, Anke, Golbik, Ralph, Balbach, Jochen, Lilie, Hauke, Rudolph, Rainer, Schwarz, Elisabeth
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 21.05.2004
• Subjects: Circular Dichroism; Cross-Linking Reagents - chemistry; Cystine knot proteins; Dimerization; Disulfides - chemistry; Escherichia coli - metabolism; Guanidine - chemistry; Humans; Models, Molecular; Nerve Growth Factors - chemistry; Nerve Growth Factors - genetics; NGF; Nuclear Magnetic Resonance, Biomolecular; Oxidative folding; Pro-peptide stimulated folding; Protein Denaturation; Protein Precursors - chemistry; Protein Precursors - genetics; Protein Renaturation; Protein Structure, Secondary; Recombinant Proteins - chemistry; Recombinant Proteins - genetics; Spectrometry, Fluorescence; Pro-peptide stimulated folding; Cystine knot proteins; NGF; Oxidative folding

Human nerve growth factor (NGF) belongs to the structural family of cystine knot proteins, characterized by a disulfide pattern in which one disulfide bond threads through a ring formed by a pair of two other disulfides connecting two adjacent β-strands. Oxidative folding of NGF revealed that the pr...