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NMR studies of the aggregation of glucagon-like peptide-1: formation of a symmetric helical dimer

✍ Scribed by Xiaoqing Chang; Danielle Keller; Seán I. O’Donoghue; Jens J. Led

Book ID
117104033
Publisher
Elsevier Science
Year
2002
Tongue
English
Weight
166 KB
Volume
515
Category
Article
ISSN
0014-5793

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Structure and folding of glucagon-like p
Structure and folding of glucagon-like peptide-1-(7–36)-amide in aqueous trifluoroethanol studied by NMR spectroscopy
✍ Xiaoqing Chang; Danielle Keller; Søren Bjørn; Jens J. Led 📂 Article 📅 2001 🏛 John Wiley and Sons 🌐 English ⚖ 217 KB

## Abstract The conformational changes of free, monomeric glucagon‐like peptide‐1‐(7–36)‐amide (GLP‐1) in aqueous solution with increasing concentrations of 2,2,2‐trifluoroethanol (TFE) were monitored by NMR spectroscopy. It was found that GLP‐1 gradually assumes a stable, single‐stranded helical s