A 1H NMR study of the solution conformation of the neuropeptide galanin.
The conformations of the neuropeptide galanin in water and trifluoroethanol solutions have been examined by 1H NMR spectroscopy. Analysis of two-dimensional NMR experiments enabled the assignment of virtually all the 1H resonances of galanin in trifluoroethanol solution and many of the 1H resonances in aqueous solution. Interpretation of the NMR data in structural terms suggests that in trifluoroethanol galanin is predominantly helical while in water it does not adopt a fixed conformation.
Wennerberg
A B
AB
Department of Medical Biophysics, Karolinska Institute, Stockholm, Sweden.
Cooke
R M
RM
Carlquist
M
M
Rigler
R
R
Campbell
I D
ID
D000595:Amino Acid Sequence; D000818:Animals; D019004:Galanin; D006859:Hydrogen; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008969:Molecular Sequence Data; D009479:Neuropeptides; D010455:Peptides / Q000138:chemical synthesis; D011487:Protein Conformation; D051381:Rats; D012996:Solutions
D009479:Neuropeptides; D010455:Peptides; D012996:Solutions; D006859:Hydrogen; D019004:Galanin