NMR Structure of Ac-hGal(17-30)NH2, an N-terminally acetylated fragment of the C-terminus of human galanin
The neuropeptide galanin adopts an irregular secondary structure.
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
galanin N-terminal fragment NMR structure
galanin N-terminal fragment NMR chemical shifts
deposition in progress - full length galanin NMR structure
deposition in progress - full length galanin NMR chemical shifts
sample was dissolved in 10 mM sodium acetate-d3/acetic acid-d4 buffer at pH 4.6; no additional additives were present.
2 mM Ac-hGal(17-30)-NH2, 4.14 mM [U-2H] sodium acetate, 5.86 mM [U-2H] acetic acid, 95% H2O/5% D2O
peptide was suspended and dissolved into deuterated acetate buffer, which had been prepared in 95:5 H2O:D2O to within 0.02 units of pH 4.6.
Brunger, Adams, Clore, Gros, Nilges and Read
MestreLab (Mnova / MestReNova / MestReC)
1D 1H NMR spectra were analyzed between 0.1 mM and 5 mM, a fifty-fold range of concentrations. All spectra were identical (free of dispersion and line-broadening effects), independent of concentration below and inclusive of a peptide concentration of 2mM, which was selected for structure analysis.