A two dimensional 1H NMR study of the solution conformation of gastrin releasing peptide.
An almost complete assignment of the 1H NMR spectrum of gastrin releasing peptide in dimethyl sulphoxide solution and aqueous solution has been carried out using two dimensional NMR techniques. The chemical shifts in both solvents have been compared with the corresponding values in random coil polypeptides and it is concluded that gastrin releasing peptide adopts little short or long range order under either solvation conditions.
Carver
J A
JA
Department of Biochemistry, University of Adelaide, South Australia.
D000595:Amino Acid Sequence; D019886:Gastrin-Releasing Peptide; D005768:Gastrointestinal Hormones; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D010455:Peptides / Q000138:chemical synthesis; D011487:Protein Conformation; D012996:Solutions
D005768:Gastrointestinal Hormones; D010455:Peptides; D012996:Solutions; D019886:Gastrin-Releasing Peptide